Show legend Show as text

Structure type: oligomer
Aglycon: Fig. 1
Contained glycoepitopes: IEDB_130646,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_151531,IEDB_153212,IEDB_190606,IEDB_241099,IEDB_423114,SB_165,SB_166,SB_187,SB_195,SB_30,SB_7,SB_74,SB_85,SB_88

• Article ID: 1372
  Bettler E, Samain E, Chazalet V, Bosso C, Heyraud A, Joziasse DH, Wakarchuk WW, Imberty A, Geremia RA "The living factory: In vivo production of N-acetyllactosamine containing carbohydrates in E-coli" - Glycoconjugate Journal 16(3) (1999) 205-212
  

  Scientific and commercial interest in oligosaccharides is increasing, but their availability is limited as production relies on chemical or chemo-enzymatic synthesis. In search for a more economical, alternative procedure, we have investigated the possibility of producing specific oligosaccharides in E. coli that express the appropriate glycosyltransferases. The Azorhizobium chitin pentaose synthase NodC (a β(1,4)GlcNAc-oligosaccharide synthase), and the Neisseria β(1,4)galactosyltransferase LgtB, were co-expressed in E. coli. The major oligosaccharide isolated from the recombinant strain, was subjected to LC-MS, FAB-MS and NMR analysis, and identified as βGal(1,4)[βGlcNAc(1,4)]4GlcNAc. High cell density culture yielded more than 1.0 gr of the hexasaccharide per liter of culture. The compound was found to be an acceptor in vitro for βGal(1,4)GlcNAc α(1,3)galactosyltransferase, which suggests that the expression of additional glycosyltransferases in E. coli will allow the production of more complex oligosaccharides.

  carbohydrates, carbohydrate, production, N-acetyllactosamine, in vivo, in vivo production

  NCBI PubMed ID: 10596895
  Journal NLM ID: 8603310
  Publisher: Kluwer Academic Publishers
  Correspondence: geremia@cermav.cnrs.fr
  Institutions: Centre de Recherches sur les Macromolecules Vegetales CNRS, Grenoble cedex, France
  Methods: FAB-MS, NMR, LC-MS
  
   
  
  Escherichia coli
  CSDB ID 6257 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit ; n=4-5
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_153212,IEDB_241099,IEDB_423114,IEDB_423150,SB_74,SB_85

• Article ID: 1623
  Kannenberg E, Carlson RW "An abundance of nodulation factors" - Chemistry and Biology 12(9) (2005) 956-958
  

  In this issue of Chemistry and Biology, Moron et al. [1] report that Rhizobium tropici CIAT899 produces different Nod factors in response to flavonoid induction under differing environmental conditions. This unanticipated environmental dependence has implications for altering or potentially improving the host-bacteria interaction in bean nodulation

  chemistry, carbohydrate, Research, complex, factor, response, Rhizobia, Rhizobium, interaction, biology, nodulation, implication, Rhizobium tropici, induction, environmental, dependence, flavonoid, nod, nod factors

  NCBI PubMed ID: 16183018
  Journal NLM ID: 9500160
  Publisher: Maryland Heights, MO: Elsevier
  Institutions: Complex Carbohydrate Research Center, The University of Georgia, Athens, 30602, USA
  Methods: biological assays
  
   
  
  Rhizobium tropici CIAT899
  CSDB ID 10560 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit
Trivial name: blastolysin
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_153212,IEDB_241099,IEDB_423114,IEDB_423150,SB_74,SB_85

• Article ID: 2802
  Ivanov VT, Andronova TM, Bezrukov MV, Rar VA, Makarov EA, Kozmin SA, Astapova MV, Barkova TI, Nesmeyanov VA "Structure, design, and synthesis of immunoactive peptides" - Pure and Applied Chemistry 59 (1987) 317-324
  

  The active principle of commercial antitumour bacterial preparation blastolysin was isolated and subjected to the chemical and spectroscoplc structural study. The structure was determined as a tetrasaccharide moiety, (N-acetylglucosamine-l-4-N-acetylmuramyl)2 to which Ala-, Lys-, D-Gln, D-Asp, and D-Ala containing peptides and teichoic acid residues are linked. The latter do not contribute to the antitumour activity of the preparation. Synthetic approaches are developed to di- and tetrasaccharide containing glycopeptides. A series of such compounds is obtained, and their antitumour and immunoadjuvant properties are characterized. Conformation and calcium binding properties of glycopeptides are studied by CD and NMR spectroscopy. Glycopeptide derivatives are incorporated into a variety of presumably immunogenic constructions containing a synthetic peptide (from the C-terminal part of the foot and mouth disease virus VP1 surface protein) and a high molecular carrier.

  Journal NLM ID: 0376514
  WWW link: http://pac.iupac.org/publications/pac/pdf/1987/pdf/5903x0317.pdf
  Publisher: Oxford: Blackwell Scientific Publications
  Institutions: Shemyakin Institute of Bioorganic Chemistry, USSR Academy of Sciences ul. Miklukho—Maklaya, 16/10, 117871 Moscow V—437, USSR
  
   
  
  Lactobacillus bulgaricus
  CSDB ID 148043 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: lipo-chitin oligosaccharide
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_153212,IEDB_241099,IEDB_423114,SB_74,SB_85

• Article ID: 3048
  Spaink HP, Wijfjes AHM, van der Drift KMGM, Haverkamp J, Thomas-Oates J, Lugtenberg BJJ "Structural identification of metabolites produced by the NodB and NodC proteins of Rhizobium leguminosarum" - Molecular Microbiology 13 (1994) 821-831
  

  The Rhizobium nodulation genes nodABC are involved in the synthesis of lipo-chitin oligosaccharides. We have analysed the metabolites which are produced in vivo and in vitro by Rhizobium strains which express the single nodA, nodB and nodC genes or combinations of the three. In vivo radioactive labelling experiments, in which D-[1-14C]-glucosamine was used as a precursor, followed by mass spectrometric analysis of the purified radiolabelled metabolic products, showed that Rhizobium strains that only express the combination of the nodB and nodC genes do not produce lipo-chitin oligosaccharides but instead produce chitin oligomers (mainly pentamers) which are devoid of the N-acetyl group on the non-reducing terminal sugar residue (designated NodBC metabolites). Using the same procedure we have shown that when the nodL gene is expressed in addition to the nodBC genes the majority of metabolites contain an additional O-acetyl substituent on the non-reducing terminal sugar residue (designated NodBCL metabolites). The NodBC and NodBCL metabolites purified after in vivo labelling were compared with the radiolabelled metabolites produced in vitro by Rhizobium bacterial cell lysates to which UDP-N-acetyl-D-[U-14C]-glucosamine was added using thin-layer chromatography. The results show that the lysates of strains which expressed the nodBC or nodBCL genes can also produce NodBC and NodBCL metabolites. The same results were obtained when the NodB and NodC proteins were produced separately in two different strains. On the basis of these and other recent results, we propose that NodB is a chitin oligosaccharide deacetylase, NodC an N-acetylglucosaminyltransferase and, by default, NodA is involved in lipid attachment.

  NCBI PubMed ID: 7815941
  Journal NLM ID: 8712028
  Publisher: Blackwell Publishing
  Institutions: Institute of Molecular Plant Sciences, Leiden University, The Netherlands
  
   
  
  Rhizobium leguminosarum
  CSDB ID 144081 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: lipo-chitin oligosaccharide
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_153212,IEDB_241099,IEDB_423114,SB_74,SB_85

• Article ID: 3048
  Spaink HP, Wijfjes AHM, van der Drift KMGM, Haverkamp J, Thomas-Oates J, Lugtenberg BJJ "Structural identification of metabolites produced by the NodB and NodC proteins of Rhizobium leguminosarum" - Molecular Microbiology 13 (1994) 821-831
  

  The Rhizobium nodulation genes nodABC are involved in the synthesis of lipo-chitin oligosaccharides. We have analysed the metabolites which are produced in vivo and in vitro by Rhizobium strains which express the single nodA, nodB and nodC genes or combinations of the three. In vivo radioactive labelling experiments, in which D-[1-14C]-glucosamine was used as a precursor, followed by mass spectrometric analysis of the purified radiolabelled metabolic products, showed that Rhizobium strains that only express the combination of the nodB and nodC genes do not produce lipo-chitin oligosaccharides but instead produce chitin oligomers (mainly pentamers) which are devoid of the N-acetyl group on the non-reducing terminal sugar residue (designated NodBC metabolites). Using the same procedure we have shown that when the nodL gene is expressed in addition to the nodBC genes the majority of metabolites contain an additional O-acetyl substituent on the non-reducing terminal sugar residue (designated NodBCL metabolites). The NodBC and NodBCL metabolites purified after in vivo labelling were compared with the radiolabelled metabolites produced in vitro by Rhizobium bacterial cell lysates to which UDP-N-acetyl-D-[U-14C]-glucosamine was added using thin-layer chromatography. The results show that the lysates of strains which expressed the nodBC or nodBCL genes can also produce NodBC and NodBCL metabolites. The same results were obtained when the NodB and NodC proteins were produced separately in two different strains. On the basis of these and other recent results, we propose that NodB is a chitin oligosaccharide deacetylase, NodC an N-acetylglucosaminyltransferase and, by default, NodA is involved in lipid attachment.

  NCBI PubMed ID: 7815941
  Journal NLM ID: 8712028
  Publisher: Blackwell Publishing
  Institutions: Institute of Molecular Plant Sciences, Leiden University, The Netherlands
  
   
  
  Rhizobium leguminosarum
  CSDB ID 144082 (all data & tools)

Show legend Show as text

Structure type: homopolymer ; n=3-5
Trivial name: NodRm-III, n=3, NodRm-IV, n=4, NodRm-V, n=5
Compound class: chitin glycolipid
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_153212,IEDB_241099,IEDB_423114,IEDB_423150,SB_74,SB_85

• Article ID: 4176
  Staehelin C, Schultze M, Kondorosi E, Mellor RB, Boller T, Kondorosi A "Structural modifications in Rhizobium meliloti Nod factors influence their stability against hydrolysis by root chitinases" - Plant Journal: for Cell and Molecular Biology 5 (1994) 319-330
  

  Acylated chitooligosaccharide signals (Nod factors) trigger the development of root nodules on leguminous plants and play an important role in determining host specificity in the Rhizobium-plant symbiosis. Here, the ability of plant chitinases to hydrolyze different Nod factors and the potential significance of the structural modifications of Nod factors in stabilizing them against enzymatic inactivation were investigated. Incubation of the sulfated Nod factors of Rhizobium meliloti, NodRm-IV(S) and NodRm-V(S), as well as their desulfated derivatives NodRm-IV and NodRm-V, with purified chitinases from the roots of the host plant Medicago and the nonhost plant Vicia resulted in the release of the acylated lipotrisaccharide NodRm-III from NodRm-V, NodRm-IV and NodRm-V(S), whereas NodRm-IV(S) was completely resistant to digestion by both chitinases. Kinetic analysis showed that the structural parameters determining host specificity, the length of the oligosaccharide chain, the acylation at the nonreducing end and the sulfatation at the reducing end of the lipooligosaccharide, influence the stability of the molecule against degradation by chitinases. When the Nod factors were incubated in the presence of intact roots of Medicago, as well as of Vicia, the acylated lipotrisaccharide was similarly released in vivo from all Nod factors except NodRm-IV(S). In addition, a dimer-forming activity was observed in intact roots which also cleaved NodRm-IV(S). This activity was much greater in Medicago than in Vicia and increased upon incubation. The initial overall degradation rate of the Nod factors on Medicago was inversely correlated with their biological activities on Medicago roots. These results open the possibility that the activity of Nod factors on Medicago may partly be determined by the action of chitinases.

  Publication DOI: 10.1111/j.1365-313X.1994.00319.x
  Journal NLM ID: 9207397
  Publisher: Oxford: Blackwell Scientific Publishers and BIOS Scientific Publishers for the Society for Experimental Biology
  Institutions: Institut des Sciences Végétales, CNRS, Gif-sur-Yvette, France, Institute of Genetics, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary, Botanisches lnstitut der Universität Basel, Basel, Switzerland
  Methods: FAB-MS, SDS-PAGE, TLC, enzymatic hydrolysis
  
   
  
  Rhizobium meliloti
  CSDB ID 146940 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: (->?) folic acid
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_149136,IEDB_151531,IEDB_153212,IEDB_241099,IEDB_423114,SB_74,SB_85

• Article ID: 4245
  White RH "Structures of the modified folates in the extremely thermophilic archaebacterium Thermococcus litoralis" - Journal of Bacteriology 175 (1993) 3661-3663
  

  The chemical structures of the two modified folates present in Thermococcus litoralis were established. These compounds, each containing a core structure of 1-[4-[[1-(2-amino-7-methyl-4-oxo-6-pteridinyl)-ethyl]amino]phenyl]-1-deoxy-[1-α-D-ribofuranosyl]-ribitol, were characterized. The five position of the ribose in this core structure was β-linked to the C-1 of a poly-β(1→4)N-acetylglucosamine having a chain length of four or five N-acetylglucosamine residues. Thus, these compounds are N-acetylglucosamine homologs of the modified folates found in Pyrococcus furiosus.

  NCBI PubMed ID: 8501071
  Journal NLM ID: 2985120R
  Publisher: American Society for Microbiology
  Institutions: Department of Biochemistry and Nutrition, Virginia Polytechnic Institute and State University, Blacksburg 24061-0308
  
   
  
  Thermococcus litoralis
  CSDB ID 131802 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit
Trivial name: peptidoglycan-related polysaccharide
Compound class: O-polysaccharide, CPS
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_153212,IEDB_241099,IEDB_423114,IEDB_423150,SB_74,SB_85

• Article ID: 4363
  Ovchinnikova OG, Liu B, Kocharova NA, Shashkov AS, Kondakova AN, Siwinska M, Feng L, Rozalski A, Wang L, Knirel YA "Structure of a peptidoglycan-related polysaccharide from Providencia alcalifaciens O45" - Biochemistry (Moscow) 77(6) (2012) 609-615
  

  A polysaccharide was isolated from the opportunistic human pathogen Providencia alcalifaciens O45:H26 by extraction with aqueous phenol and studied by sugar and methylation analyses along with (1)H and (13)C NMR spectroscopy, including two-dimensional ROESY and H-detected (1)H,(13)C HSQC experiments. The polysaccharide contains N-acetylglucosamine and N-acetylmuramic acid (D-GlcpNAc3Rlac) amidated with L-alanine and has the following structure:-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc3(Rlac-L-Ala)-(1-. The polysaccharide possesses a remarkable structural similarity to the bacterial cell wall peptidoglycan. It is not unique to the strain studied but is common to strains of at least four P. alcalifaciens O-serogroups (O3, O24, O38, and O45). No evidence was obtained that the polysaccharide is associated with the LPS, and hence it might represent a bacterial capsule component.

  Lipopolysaccharide, Providencia alcalifaciens, Bacterial polysaccharide, peptidoglycan, N-acetylmuramic acid

  NCBI PubMed ID: 22817460
  Publication DOI: 10.1134/S0006297912060077
  Journal NLM ID: 0376536
  Publisher: Nauka/Interperiodica
  Correspondence: olga.ovchinnikova@gmail.com
  Institutions: Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia
  Methods: 13C NMR, 1H NMR, NMR-2D, methylation, GLC-MS, sugar analysis
  
   
  
  Providencia alcalifaciens O45
  CSDB ID 27269 (all data & tools)
• Article ID: 4875
  Guo X, Senchenkova SN, Shashkov AS, Perepelov AV, Liu B, Knirel YA "Structure and gene cluster of the O-antigen of Escherichia coli O96" - Carbohydrate Research 420 (2016) 1-5
  

  Mild acid degradation of the lipopolysaccharide of Escherichia coli O96 afforded a mixture of two polysaccharides. The following structure of the pentasaccharide repeating unit of the major polymer was established by sugar analysis, Smith degradation, and (1)H and (13)C NMR spectroscopy: [Formula: see text]. The O-antigen gene cluster of E. coli O96 between conserved galF and gnd genes was found to be consistent with this structure, and hence, the major polysaccharide represents the O96-antigen. The O96-antigen structure and gene cluster are similar to those of E. coli O170, and two proteins encoded in the gene clusters of both bacteria were putatively assigned a function of galactofuranosyltransferases. The minor polymer has the same structure as a peptidoglycan-related polysaccharide reported earlier in Providencia alcalifeciens O45 and several other O-serogoups of this species (Ovchinnikova OG, Liu B, Kocharova NA, Shashkov AS, Kondakova AN, Siwinska M, Feng L, Rozalski A, Wang L, Knirel YA. Biochemistry (Moscow) 2012;77:609-15) →4)-β-D-GlcpNAc-(1→4)-β-D-GlcpNAc3(Rlac-lAla)-(1→ where Rlac-lAla indicates (R)-1-[(S)-1-carboxyethylaminocarbonyl]ethyl.

  O-antigen, Escherichia coli, O-polysaccharide, bacterial polysaccharide structure, O-antigen gene cluster, Peptidoglycan-related polysaccharide

  NCBI PubMed ID: 26706815
  Publication DOI: 10.1016/j.carres.2015.11.005
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: perepel@ioc.ac.ru
  Institutions: N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, TEDA Institute of Biological Sciences and Biotechnology, Nankai University, TEDA, Tianjin, China
  Methods: 13C NMR, 1H NMR, NMR-2D, sugar analysis, ESI-MS, acid hydrolysis, GLC, Smith degradation, GPC, mild acid degradation, function analysis of gene clusters
  
   
  
  Escherichia coli O96 (G3132), Providencia alcalifaciens O45
  CSDB ID 11544 (all data & tools)

Show legend Show as text

Structure type: homopolymer
Trivial name: chitin
Compound class: O-polysaccharide, cell wall polysaccharide, glucan, polysaccharide, chitin
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_153212,IEDB_241099,IEDB_423114,IEDB_423150,SB_74,SB_85

• Article ID: 5943
  Heng J, Naderer T, Ralph SA, McConville MJ "Glycosylated compounds of parasitic protozoa" - Book: Microbial Glycobiology (series: Structures, Relevance and Applications) (2010) 203-231
  

  This chapter describes the range of glycan structures and pathways that are found in different parasitic protozoa. All parasitic protists express a range of glycoconjugates that form protective protein-rich or carbohydrate-rich surface coats. Protein-rich coats are typically found on developmental stages that inhabit nonhydrolytic niches, such as the bloodstream and nonacidified intracellular vacuoles. These coats are commonly dominated by a limited repertoire of antigenically diverse proteins that are commonly, but not always, glycosylphosphatidylinositol- (GPI-) anchored and modified with N- or O-glycans. Carbohydrate-rich coats are commonly found on developmental stages that dwell within hydrolytic environments, such as vertebrate and arthropod digestive tracts and lysosomal vacuoles. These coats are dominated by GPI-anchored glycoproteins that are heavily modified with N-glycans, O-glycans, or phosphoglycans. Free GPI glycolipids (not attached to protein) can also be abundant or dominant components of these coats. Some parasitic protists can also form highly resistant cyst stages encased within polysaccharide-rich cell walls. Considerable progress has been made in defining the structures of the surface and intracellular glycans of the parasitic protists, their biosynthesis and the role that individual components play in parasite infectivity.

  O-glycosylation, Glycosylphosphatidylinositol, N-glycosylation, protozoan parasites, Phosphoglycosylation

  Publication DOI: 10.1016/B978-0-12-374546-0.00012-2
  Publisher: Amsterdam: Elsevier
  Correspondence: malcolmm@unimelb.edu.au
  Editors: Moran A
  Institutions: Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Australia
  
   
  
  Entamoeba invadens
  CSDB ID 4580 (all data & tools)
• Article ID: 6180
  Ahmadipour S, Field RA, Miller GJ "Prospects for anti-Candida therapy through targeting the cell wall: A mini-review" - Cell Surface 7 (2021) ID 100063
  

  The impact of fungal infections on humans is a serious public health issue that has received much less attention than bacterial infection and treatment, despite ever-increasing incidence exacerbated by an increased incidence of immunocompromised individuals in the population. Candida species, in particular, cause some of the most prevalent hospital-related fungal infections. Fungal infections are also detrimental to the well-being of grazing livestock, with milk production in dairy cows, and body and coat condition adversely affected by fungal infections. Fungal cell walls are essential for viability, morphogenesis and pathogenesis: numerous anti-fungal drugs rely on targeting either the cell wall or cell membrane, but the pipeline of available bioactives is limited. There is a clear and unmet need to identify novel targets and develop new classes of anti-fungal agents. This mini review focuses on fungal cell wall structure, composition and biosynthesis in Candida spp., including C. auris. In addition, an overview of current advances in the development of cell wall targeted therapies is considered.

  vaccines, glycoproteins, inhibitors, chitin, fungal cell wall

  NCBI PubMed ID: 34746525
  Publication DOI: 10.1016/j.tcsw.2021.100063
  Journal NLM ID: 101728565
  Publisher: Amsterdam: Elsevier
  Correspondence: sanaz.ahmadipour@manchester.ac.uk
  Institutions: Department of Chemistry and Manchester Institute of Biotechnology, The University of Manchester, Manchester, UK, Iceni Diagnostics Ltd, The Innovation Centre, Norwich Research Park, Norwich, UK, Lennard-Jones Laboratory, School of Chemical and Physical Sciences, Keele University, Keele, UK
  
   
  
  Candida albicans
  CSDB ID 40868 (all data & tools)
• Article ID: 6503
  Depree J, Emerson GW, Sullivan PA "The cell wall of the oleaginous yeast Trichosporon cutaneum" - Journal of General Microbiology 139 (1993) 2123-2133
  

  The cell wall of Trichosporon cutaneum consists of 11% protein, 63% neutral carbohydrate, 9% glucosamine and 13% glucuronic acid. The sugars include glucose (32%), mannose (6%) and traces of xylose and galactose. The cell wall was fractionated with alkali to yield a mixture of alkali-soluble matrix components, and an alkali-insoluble glucan associated with chitin. The alkali-insoluble glucan contained a mixture of (1-3) and (1-6) glycosidic linkages. It was only partly susceptible to digestion by the β(1-3) glucanase, Zymolyase. The alkali-soluble fraction contained glucan, mannan and acidic polymers. The glucan was (1-3)-linked with no (1-6) linkages and only trace amounts of (1-3-6)-linked glucose. It was resistant to digestion by Zymolyase. Extensive hydrolysis of this fraction with trifluoroacetic acid released a high-molecular-mass glucuronan which had 1H- and 13C-NMR profiles matching those of the β(1-4) glucuronan, mucoric acid. Xylomannan was purified from isolated cell walls and from whole cells. It contained glucose, mannose, xylose, and D-glucuronic acid. It was very similar in composition and structure to the capsular polysaccharides of Cryptococcus neoformans, and to an extracellular polysaccharide produced by another yeast described as T. cutaneum. Electron microscopy showed that the cell wall of T. cutaneum has a lamellar structure characteristic of a basidiomycetous yeast rather than the electron-dense 'fuzzy coat' seen in Candida albicans.

  NCBI PubMed ID: 8245838
  Journal NLM ID: 0375371
  Institutions: Department of Biochemistry, University of Otago, Dunedin, New Zealand
  Methods: 13C NMR, 1H NMR, acid hydrolysis, GLC, electron microscopy, enzymatic digestion, anion exchange chromatography, methylation assay, alkali extraction, alkali extrnction
  
   
  
  Trichosporon cutaneum
  CSDB ID 139869 (all data & tools)
• Article ID: 6570
  Lestan M, Pecavar A, Lestan D, Perdih A "Amino acids in chitin-glucan complex of Aspergillus niger" - Amino Acids 4 (1993) 169-176
  

  Deproteinated A. niger biomass contains several covalently bound amino acids. The most abundant are arginine, serine, and proline in molar ratio of 3: 2: 2. One order of magnitude less is the amount of valine, phenylalanine, leucine and glycine. On deacetylation and separation of chitosan from glucan, the main three amino acids remain bound predominantly to chitosan, whereas the hydrophobic amino acids accompany mainly glucan. The presence of arginine could be the cause of stronger basicity of fungal chitosan compared to polyglucosamine.

  Publication DOI: 10.1007/BF00805812
  Journal NLM ID: 9200312
  Publisher: Wien; New York: Springer
  
   
  
  Aspergillus niger
  CSDB ID 101632 (all data & tools)
• Article ID: 6609
  Benhamou N "Immunocytochemistry of plant defense mechanisms induced upon microbial attack" - Microscopy Research and Technique 31 (1995) 63-78
  

  During the past few years, cyto- and immunocytochemical techniques have been developed and widely used for locating and identifying various molecules in plant cell compartments. The last decade has witnessed tremendous improvements in molecular cytology, thus allowing an accurate in situ detection of various components thought to play important biological functions in the plant metabolism. The use of immunocytochemistry to investigate resistance mechanisms of plants upon pathogen attack has provided key information on the defense strategy that plants elaborate during a host-pathogen interaction. Of the various proteins induced in response to infection, chitinases and β-1,3-glucanases have been the focus of particular attention due to their believed antimicrobial activity through the hydrolysis of the main fungal wall components, chitin and β-1,3-glucans. Attention has also been paid to β-fructosidase, the enzyme that hydrolyzes sucrose into glucose and fructoside. The marked accumulation of this enzyme upon pathogen infection has led to the consideration that infection may greatly influence the metabolic activity of colonized tissues by creating alterations of source-sink relationships. Another facet of the plant's defense strategy that has been the focus of considerable interest is related to the accumulation of structural compounds, such as hydroxyproline-rich glycoproteins and callose, to reinforce the wall architecture, thus decreasing vulnerability to microbial enzymes. A number of alternatives designed to improve plant protection towards pathogen invasion have been suggested. Among these, the production of transgenic plants expressing constitutively a foreign resistance gene and the pretreatment of plants with elicitors of defense reactions have been the subject of intensive studies at the molecular, biochemical, and cytological levels. Results of such studies clearly demonstrate the important contribution that cyto- and immunocytochemical approaches can make to our knowledge of how plants defend themselves and how plant disease resistance can be directly enhanced. These approaches will undoubtedly be active areas for future research in the development of biological control alternatives in which the mode of action of the product used is of key importance.

  NCBI PubMed ID: 7626800
  Publication DOI: 10.1002/jemt.1070310106
  Journal NLM ID: 9203012
  Publisher: Wiley-Liss
  Institutions: Recherche en Sciences de la vie et de la santé, Pavillon Charles-Eugène-Marchand, Université Laval, Sainte-Foy, Quebec, Canada
  
   
  
  Rhizoctonia solani
  CSDB ID 143703 (all data & tools)
• Article ID: 6610
  Nicole MR, Benhamou N "Ultrastructural localization of chitin in cell walls of Rigidoporus lignosus, the white-rot fungus of rubber tree roots" - Physiological and Molecular Plant Pathology 39 (1991) 415-431
  
  Journal NLM ID: 9882868
  Publisher: Academic Press
  
   
  
  Rigidoporus lignosus
  CSDB ID 145244 (all data & tools)
• Article ID: 6613
  Balestrini R, Romera C, Puigdomenech P, Bonfante P "Location of a cell-wall hydroxyproline-rich glycoprotein, cellulose and β-1,3-glucans in apical and differentiated regions of maize mycorrhizal roots" - Planta 195 (1994) 201-209
  

  The cell-wall components of the interface compartment in functioning mycorrhizal roots of maize (Zea mays L. cv. W64A) have been investigated with the use of immunocytochemistry and enzyme/lectin-gold techniques. The distribution of specific cell-wall probes was determined in the apical and differentiated regions of maize roots in the presence and in the absence of the mycorrhizal fungus, Glomus versiforme. Labelling experiments showed that a maize hydroxyproline-rich glycoprotein (HRGP), identified with a specific antibody, was particularly abundant in the apical dividing cells of the root meristem. Cellulose, located with a cellobiohydrolase-gold complex, showed a similar labelling pattern in the walls of both meristematic and differentiated parts of the roots. When the cortex was colonized by the mycorrhizal fungus, the HRGP and cellulose were expressed in two sites: the wall and the interface area created by invagination of the host membrane around the developing fungus. In contrast, in uninfected roots of the same age, they were only present in the inner part of the wall. A specific antibody against β-1,3-glucans demonstrated that these glucans were not laid down at the interface between the plant and fungus, while they appeared to be a skeletal component of the fungal wall, together with chitin.

  cell wall, cellulose, β-1, arbuscular mycorrhizae, 3-glucans, hydroxyproline-rich glycoprotein, zea root meristem

  Publication DOI: 10.1007/BF00199680
  Journal NLM ID: 1250576
  Publisher: Berlin, New York, Springer
  Institutions: Dipartimento di Biologia, Vegetale dell'Università, Torino, Italy, Departamento de Genetica Molecular, CID-CSIC, Barcelona, Spain
  Methods: microscopy, immunocytochemistry
  
   
  
  Glomus versiforme
  CSDB ID 147175 (all data & tools)
• Article ID: 6624
  de Nobel H, Lipke PN "Is there a role for GPIs in yeast cell-wall assembly?" - Trends in Cell Biology 4 (1994) 42-45
  

  Glycosylphosphatidylinositol (GPI) membrane anchors are essential for the integration of yeast cell adhesion proteins into the cell wall, but mature cell-wall proteins are unlikely to be attached directly to the membrane. We thus propose that GPI-anchored glycoprotein forms are intermediates in a process that crosslinks the major components of the cell wall by transglycosylation. This mechanism may be critical for both the biosynthesis and overall architecture of the cell wall.

  NCBI PubMed ID: 14731865
  Journal NLM ID: 9200566
  Publisher: Elsevier
  Institutions: Department of Microbiology and Molecular Genetics, University of Vermont College of Medicine, Burlington, VT 05405, USA
  
   
  
  Saccharomyces cerevisiae
  CSDB ID 149428 (all data & tools)
• Article ID: 6625
  Klis FM "Review: cell wall assembly in yeast" - Yeast 10 (1994) 851-869
  
  NCBI PubMed ID: 7985414
  Publication DOI: 10.1002/yea.320100702
  Journal NLM ID: 8607637
  Publisher: Chichester, Wiley
  Institutions: BioCentrum Amsterdam, Institute of Molecular Cell Biology, University of Amsterdam, The Netherlands
  
   
  
  Saccharomyces cerevisiae
  CSDB ID 149871 (all data & tools)
• Article ID: 6626
  Hong Z, Mann P, Shaw KJ, Didomenico B "Analysis of b-glucans and chitin in a Saccharomyces cerevisiae cell wall mutant using high-performance liquid chromatography" - Yeast 10 (1994) 1083-1092
  

  We have previously shown that mutations in the yeast KNR4 gene resulted in pleiotropic cell wall defects, including resistance to killer 9 toxin, elevated osmotic sensitivity to SDS and increased resistance to zymolyase, a (1-->3)-β-glucanase. In this report, we further demonstrated that knr4 mutant cells were more permeable to a chromogenic substrate, X-GAL, suggesting that the mutant cell walls were leakier to certain non-permeable molecules. To determine if these defects resulted from structural changes in the cell walls, we analysed the alkali-insoluble cell wall components using HPLC assays developed for this purpose. Comparative analysis using four isogenic strains from a 'knr4 disrupted' tetrad demonstrated that mutant cell walls contained much less (1-->3)-β-glucan and (1-->6)-β-glucan; however, the level of chitin, a minor cell wall component, was found to be five times higher in the mutant strains compared to the wild-type strains. The data suggested that the knr4 mutant cell walls were dramatically weakened, which may explain the pleiotropic cell wall defects.

  NCBI PubMed ID: 7992508
  Publication DOI: 10.1002/yea.320100810
  Journal NLM ID: 8607637
  Publisher: Chichester, Wiley
  Institutions: Chemotherapy and Molecular Genetics, Schering-Plough Research Institute, Kenilworth, New Jersey 07033-0539
  Methods: acid hydrolysis, HPLC, enzymatic digestion, periodate oxidation, in vivo labeling
  
   
  
  Saccharomyces cerevisiae
  CSDB ID 149874 (all data & tools)
• Article ID: 6769
  Munro CA, Gow NA "Chitin synthesis in human pathogenic fungi" - Medical Mycology 39 (2001) 41-53
  

  In recent years it has become evident that the structural polysaccharide chitin is synthesized from a family of enzymes encoded by multiple CHS chitin synthase genes, and regulated by an array of ancillary gene products that influence CHS activation and localization. Considerable attention has therefore been given to elucidating the function of specific CHS gene products in individual fungi. In those fungi in which individual CHS genes have been deleted systematically, there is little evidence for redundancy of function in family members. Chs enzymes are now known that participate in lateral wall biosynthesis, septum synthesis and spore formation but the phenotype of some CHS gene mutations is subtle, and so the role of the corresponding isoenzymes remains obscure. Nonetheless, it has become clear that certain members of the CHS gene families of fungi are more important for growth, integrity and viability than others, and this knowledge has already led to the design of new classes of antifungal agents that are targeted against key enzyme activities. Future work in this area will help define how individual Chs enzymes are targeted to specific regions of the cell wall and at specific times of the cell cycle, and should facilitate the rational development of novel and highly specific antifungal agents.

  cell wall, mutagenesis, morphogenesis, antifungal drugs, chitin synthesis

  Publication DOI: 10.1080/mmy.39.1.41.53
  Journal NLM ID: 9815835
  Publisher: Oxford: Oxford University Press
  Correspondence: n.gow@abdn.ac.uk
  Institutions: Department of Molecular and Cell Biology, Institute of Medical Sciences, University of Aberdeen, Aberdeen AB25 2ZD, UK
  
   
  
  Saccharomyces cerevisiae, Candida albicans, Paracoccidioides brasiliensis, Aspergillus nidulans, Aspergillus fumigatus, Wangiella dermatitidis
  CSDB ID 40517 (all data & tools)
• Article ID: 6791
  Yamaguchi T, Ito Y, Shibuya N "Oligosaccharide elicitors and their receptors for plant defense responses" - Trends in Glycoscience and Glycotechnology 12 (2000) 113-120
  

  N-Acetylchitooligosaccharides (oligochitin, chitin oligosaccharides) of a specific size can act as potent elicitor signals for suspension-cultured rice cells as well as various plant cells which include many monocots and some dicots. We recently isolated and characterized a highly elicitor-active glucopentaose from the cell wall P-Glucan from rice blast disease fungus. The results indicated that rice and soybean cells recognize different structural units of fugal glucans as elicitor signals. Because this elicitor treatment can induce many defense reactions, it has been serving as an excellent model system for the study of the signal transduction cascade leading to the activation of defense-related genes. It is critically important to identify and characterize the receptor molecules which perceive the elicitor signal to clarify the whole signal transduction cascade. A 75 kDa chitin oligosaccharide binding protein in the plasma membrane of suspension-cultured rice cells was identified as a putative receptor for the elicitor and purified. Recent studies on the structure and function of the binding proteins for these oligosaccharide elicitors will provide a clue to understanding how these elicitors are perceived and transduced in rice and other plant cells and also how such recognition systems have evolved.

  receptor, signal transduction, elicitor

  Publication DOI: 10.4052/tigg.12.113
  Journal NLM ID: 9425898
  Correspondence: shibuya@abr.affrc.go.jp
  Institutions: Department of Biotechnology, National Institute of Agrobiological Resources, Ministry of Agriculture, Forestry and Fisheries, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8602, Japan, Department of Biotechnology, National Institute of Agrobiological Resources, Ministry of Agriculture, Forestry and Fisheries, Tsukuba, Japan
  
   
  
  (plant)
  CSDB ID 68682 (all data & tools)
• Article ID: 7030
  Becker HF, Piffeteau A, Thellend A "Saccharomyces cerevisiae chitin biosynthesis activation by N-acetylchitooses depends on size and structure of chito-oligosaccharides" - BMC Research Notes 4(454) (2011) 1-6
  

  Background: To explore chitin synthesis initiation, the effect of addition of exogenous oligosaccharides on in vitro chitin synthesis was studied. Oligosaccharides of various natures and lengths were added to a chitin synthase assay performed on a Saccharomyces cerevisiae membrane fraction. Findings. N-acetylchito-tetra, -penta and -octaoses resulted in 11 to 25% [14C]-GlcNAc incorporation into [14C]-chitin, corresponding to an increase in the initial velocity. The activation appeared specific to N-acetylchitooses as it was not observed with oligosaccharides in other series, such as beta-(1,4), beta-(1,3) or alpha-(1,6) glucooligosaccharides. Conclusions: The effect induced by the N-acetylchitooses was a saturable phenomenon and did not interfere with free GlcNAc and trypsin which are two known activators of yeast chitin synthase activity in vitro. The magnitude of the activation was dependent on both oligosaccharide concentration and oligosaccharide size.

  Oligosaccharides, glycosyltransferase, chitin synthase, polymerization activation, polysaccharide synthase

  NCBI PubMed ID: 22032207
  Publication DOI: 10.1186/1756-0500-4-454
  Journal NLM ID: 101462768
  Publisher: London: Biomed Central, 2008
  Correspondence: hubert.becker@polytechnique.edu
  Institutions: Laboratoire d’Optique et Biosciences, INSERM, CNRS, Ecole Polytechnique, Palaiseau, France, UPMC Univ Paris 06, CNRS UMR, Laboratoire des Biomolécules, Paris, France, Université Paris-Diderot, Paris, France
  Methods: TLC, radiolabeling, enzymatic digestion, enzymatic assay
  
   
  
  Saccharomyces cerevisiae
  CSDB ID 43385 (all data & tools)
• Article ID: 7856
  Azuma K, Ifuku S, Osaki T, Okamoto Y, Minami S "Preparation and biomedical applications of chitin and chitosan nanofibers" - Journal of Biomedical Nanotechnology 10(10) (2014) 2891-2920
  

  Chitin (β-(1-4)-poly-N-acetyl-D-glucosamine) is widely distributed in nature and is the second most abundant polysaccharide after cellulose. Chitin occurs in nature as ordered macrofibrils. It is the major structural component in the exoskeleton of crab and shrimp shells and the cell wall of fungi and yeast. As chitin is not readily dissolved in common solvents, it is often converted to its more deacetylated derivative, chitosan. Chitin, chitosan, and its derivatives are widely used in tissue engineering, wound healing, and as functional foods. Recently, easy methods for the preparation of chitin and chitosan nanofibers have been developed, and studies on biomedical applications of chitin and chitosan nanofibers are ongoing. Chitin and chitosan nanofibers are considered to have great potential for various biomedical applications, because they have several useful properties such as high specific surface area and high porosity. This review summarizes methods for the preparation of chitin and chitosan nanofibers. Further, biomedical applications of chitin and chitosan nanofibers in (i) tissue engineering, (ii) wound dressing, (iii) cosmetic and skin health, (iv) stem cell technology, (v) anti-cancer treatments and drug delivery, (vi) anti-inflammatory treatments, and (vii) obesity treatment are summarized. Many studies indicate that chitin and chitosan nanofibers are suitable materials for various biomedical applications.

  drug delivery, cosmetics, chitosan, chitin, nanofibers, biomedical applications, tissue engineering, stem cells, obesity

  NCBI PubMed ID: 25992423
  Journal NLM ID: 101230869
  Publisher: Stevenson Ranch, CA: American Scientific Publishers
  Correspondence: Azuma K ; Ifuku S
  Institutions: Faculty of Agriculture, Tottori University, Tottori, Japan, Graduated School of Engineering, Tottori University, Tottori, Japan
  
   
  
  Pleurotus eryngii, Agaricus bisporus, Lentinula edodes, Grifola frondosa, Hypsizygus marmoreus
  CSDB ID 46290 (all data & tools)
• Article ID: 7857
  Dorfmueller HC, Ferenbach AT, Borodkin VS "A structural and biochemical model of processive chitin synthesis" - Journal of Biological Chemistry 289(33) (2014) 23020-23028
  

  Chitin synthases (CHS) produce chitin, an essential component of the fungal cell wall. The molecular mechanism of processive chitin synthesis is not understood, limiting the discovery of new inhibitors of this enzyme class. We identified the bacterial glycosyltransferase NodC as an appropriate model system to study the general structure and reaction mechanism of CHS. A high throughput screening-compatible novel assay demonstrates that a known inhibitor of fungal CHS also inhibit NodC. A structural model of NodC, on the basis of the recently published BcsA cellulose synthase structure, enabled probing of the catalytic mechanism by mutagenesis, demonstrating the essential roles of the DD and QXXRW catalytic motifs. The NodC membrane topology was mapped, validating the structural model. Together, these approaches give insight into the CHS structure and mechanism and provide a platform for the discovery of inhibitors for this antifungal target.

  cell wall, chitin, chitin synthase

  NCBI PubMed ID: 24942743
  Publication DOI: 10.1074/jbc.M114.563353
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: Dorfmueller HC ; van Aalten DM
  Institutions: Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee, UK, MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee, UK
  Methods: DNA techniques, enzymatic assays
  
   
  
  Saccharomyces cerevisiae
  CSDB ID 46291 (all data & tools)
• Article ID: 7858
  Dubey LK, Moeller JB, Schlosser A, Sorensen GL, Holmskov U "Induction of innate immunity by Aspergillus fumigatus cell wall polysaccharides is enhanced by the composite presentation of chitin and beta-glucan" - Immunobiology 219(3) (2013) 179-188
  

  Chitin and β-glucan are conserved throughout evolution in the fungal cell wall and are the most common polysaccharides in fungal species. Together, these two polysaccharides form a structural scaffold that is essential for the survival of the fungus. In the present study, we demonstrated that Aspergillus fumigatus alkali-insoluble cell wall fragments (AIF), composed of chitin linked covalently to β-glucan, induced enhanced immune responses when compared with individual cell wall polysaccharides. Intranasal administration of AIF induced eosinophil and neutrophil recruitment, chitinase activity, TNF-α and TSLP production in mice lungs. Selective destruction of chitin or β-glucan from AIF significantly reduced eosinophil and neutrophil recruitment as well as chitinase activity and cytokine expression by macrophages, indicating the synergistic effect of the cell wall polysaccharides when presented together as a composite PAMP. We also showed that these cell wall polysaccharides induced chitin-specific IgM in mouse serum. Our in vivo and in vitro data indicate that chitin and β-glucan play important roles in activating innate immunity when presented as composite cell wall PAMPs.

  inflammation, glucan, innate immunity, lung, chitin, Fungal cell wall polysaccharides

  NCBI PubMed ID: 24286790
  Publication DOI: 10.1016/j.imbio.2013.10.003
  Journal NLM ID: 8002742
  Publisher: Amsterdam: Elsevier
  Correspondence: Holmskov U
  Institutions: Institute of Molecular Medicine, Department of Cardiovascular and Renal Research, University of Southern Denmark, Odense, Denmark
  Methods: SDS-PAGE, enzymatic digestion, extraction, enzymatic assay, cytokine production, FACS analysis
  
   
  
  Aspergillus fumigatus
  CSDB ID 46292 (all data & tools)
• Article ID: 7860
  Barreto-Bergter E, Figueiredo RT "Fungal glycans and the innate immune recognition" - Frontiers in Cellular and Infection Microbiology 4(145) (2014) 1-15
  

  Polysaccharides such as α- and β-glucans, chitin, and glycoproteins extensively modified with both N- and O-linked carbohydrates are the major components of fungal surfaces. The fungal cell wall is an excellent target for the action of antifungal agents, since most of its components are absent from mammalian cells. Recognition of these carbohydrate-containing molecules by the innate immune system triggers inflammatory responses and activation of microbicidal mechanisms by leukocytes. This review will discuss the structure of surface fungal glycoconjugates and polysaccharides and their recognition by innate immune receptors.

  polysaccharides, glycoconjugates, innate immunity, fungal pathogens, pattern recognition receptors

  NCBI PubMed ID: 25353009
  Publication DOI: 10.3389/fcimb.2014.00145
  Journal NLM ID: 101585359
  Publisher: Lausanne: Frontiers Media SA
  Correspondence: Barreto-Bergter E ; Figueiredo RT
  Institutions: Departamento de Microbiologia Geral, Instituto de Microbiologia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil, Instituto de Ciências Biomédicas/Unidade de Xerém, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil, Departamento de Microbiologia Geral, Instituto de Microbiologia, Universidade Federal do Rio de Janeiro Rio de Janeiro, Brazil, Instituto de Ciências Biomédicas/Unidade de Xerém, Universidade Federal do Rio de Janeiro Rio de Janeiro, Brazil
  Methods: 13C NMR, 1H NMR, GC-MS, ESI-MS, TOCSY, methylation analysis, HMQC-NMR
  
   
  
  Saccharomyces cerevisiae, Aspergillus fumigatus
  CSDB ID 46304 (all data & tools)
• Article ID: 7871
  Bain JM, Louw J, Lewis LE, Okai B, Walls CA, Ballou ER, Walker LA, Reid D, Munro CA, Brown AJ, Brown GD, Gow NA, Erwig LP "Candida albicans hypha formation and mannan masking of β-glucan inhibit macrophage phagosome maturation" - mBio 5(6) (2014) 1-17
  

  Candida albicans is a major life-threatening human fungal pathogen in the immunocompromised host. Host defense against systemic Candida infection relies heavily on the capacity of professional phagocytes of the innate immune system to ingest and destroy fungal cells. A number of pathogens, including C. albicans, have evolved mechanisms that attenuate the efficiency of phagosome-mediated inactivation, promoting their survival and replication within the host. Here we visualize host-pathogen interactions using live-cell imaging and show that viable, but not heat- or UV-killed C. albicans cells profoundly delay phagosome maturation in macrophage cell lines and primary macrophages. The ability of C. albicans to delay phagosome maturation is dependent on cell wall composition and fungal morphology. Loss of cell wall O-mannan is associated with enhanced acquisition of phagosome maturation markers, distinct changes in Rab GTPase acquisition by the maturing phagosome, impaired hyphal growth within macrophage phagosomes, profound changes in macrophage actin dynamics, and ultimately a reduced ability of fungal cells to escape from macrophage phagosomes. The loss of cell wall O-mannan leads to exposure of β-glucan in the inner cell wall, facilitating recognition by Dectin-1, which is associated with enhanced phagosome maturation.

  cell wall, β-glucan, Candida albicans, b-glucan

  NCBI PubMed ID: 25467440
  Publication DOI: 10.1128/mBio.01874-14
  Journal NLM ID: 101519231
  Publisher: Washington, DC: American Society for Microbiology
  Correspondence: Bain JM
  Institutions: Aberdeen Fungal Group, University of Aberdeen, Aberdeen, UK
  
   
  
  Candida albicans
  CSDB ID 46323 (all data & tools)
• Article ID: 7881
  Chung D, Thammahong A, Shepardson KM, Blosser SJ, Cramer RA "Endoplasmic reticulum localized PerA is required for cell wall integrity, azole drug resistance, and virulence in Aspergillus fumigatus" - Molecular Microbiology 92(6) (2014) 1279-1298
  

  GPI-anchoring is a universal and critical post-translational protein modification in eukaryotes. In fungi, many cell wall proteins are GPI-anchored, and disruption of GPI-anchored proteins impairs cell wall integrity. After being synthesized and attached to target proteins, GPI anchors undergo modification on lipid moieties. In spite of its importance for GPI-anchored protein functions, our current knowledge of GPI lipid remodelling in pathogenic fungi is limited. In this study, we characterized the role of a putative GPI lipid remodelling protein, designated PerA, in the human pathogenic fungus Aspergillus fumigatus. PerA localizes to the endoplasmic reticulum and loss of PerA leads to striking defects in cell wall integrity. A perA null mutant has decreased conidia production, increased susceptibility to triazole antifungal drugs, and is avirulent in a murine model of invasive pulmonary aspergillosis. Interestingly, loss of PerA increases exposure of β-glucan and chitin content on the hyphal cell surface, but diminished TNF production by bone marrow-derived macrophages relative to wild type. Given the structural specificity of fungal GPI-anchors, which is different from humans, understanding GPI lipid remodelling and PerA function in A. fumigatus is a promising research direction to uncover a new fungal specific antifungal drug target.

  Aspergillus fumigatus, GPI

  NCBI PubMed ID: 24779420
  Publication DOI: 10.1111/mmi.12626
  Journal NLM ID: 8712028
  Publisher: Blackwell Publishing
  Correspondence: Cramer RA
  Institutions: Department of Microbiology and Immunology, Geisel School of Medicine at Dartmouth, Hanover, USA, Department of Immunology and Infectious Disease, Montana State University, Bozeman, USA
  Methods: ELISA, DNA extraction, RNA extraction, qRT-PCR, light microscopy, germination assay, XTT assay
  
   
  
  Aspergillus fumigatus, Candida albicans
  CSDB ID 46396 (all data & tools)
• Article ID: 7883
  Chen L, Xu WW, Lin SL, Cheung PCK "Cell wall structure of mushroom sclerotium (Pleurotus tuber regium): Part 1. Fractionation and characterization of soluble cell wall polysaccharides" - Food Hydrocolloids 36 (2014) 189-195
  

  The cell wall structure of mushroom sclerotium was investigated by a fractionation of its soluble cell wall polysaccharides followed by chemical, physico-chemical and microscopic analyses. The present results suggest that cell wall structure of Pleurotus tuber regium sclerotium contains three main layers: an outer layer of glycoproteins, a middle layer of hyper-branched glucans and an inner layer of complex between hyper-branched glucan and chitin. The structure of the hyper-branched glucans were elucidated by the methylation analysis to be composed of →1)-Glcp-(4→ linkages as the backbone with some →1)-Glcp(6→ linkages existed in the side chains, while some →1)-Glcp-(3→ linkages might exist in the backbone or side chains. SEC-MALLS analysis revealed that hyper-branched β-glucans had a M-w ranging from 1400000 to 5200000 g/mol and R.M.S. radius ranging from 26 nm to 38.5 nm. SEM and AFM further showed that hyper-branched beta-glucans were spherical in shape when dispersed in water.

  Publication DOI: 10.1016/j.foodhyd.2013.09.023
  Journal NLM ID: 8701770
  Publisher: New York, NY: Elsevier
  Correspondence: Cheung PCK
  Institutions: School of Life Sciences, The Chinese University of Hong Kong, Shatin, China, CUHK Shenzhen Research Institute, Shenzhen, China
  Methods: methylation, IR, GC-MS, SDS-PAGE, extraction, cell growth, SEC-MALLS, precipitation, microscopic analysis
  
   
  
  Pleurotus tuber-regium
  CSDB ID 46404 (all data & tools)
• Article ID: 8480
  Kothe E, Freihorst D "Form follows function: The fungal cell wall as a support structure" - Biologie in Unserer Zeit = Biology in our Time [German] 46(6) (2016) 244-250
  

  Within the domain of Eukarya, the fungi form a seperate kingdom. The typical formation of branched mycelia from single hyphae is based on cell wall production at the growing hyphal tip. There, excretory vesicle fuse with the membrane releasing cell wall synthesis enzymes like chitin synthase forming the polymer of N-acetyl glucosamin, the backbone of fungal cell walls. In addition, glucan synthases form the structural component β-1,3-glucan. Via β-1,6-glucan, cell wall proteins can be linked to the maturing cell wall, and α-1,3-glucan can form a matrix within the cell wall, but also a slimy matrix secreted into the medium. A layer of hydrophobins allows for growth into the air, but also facilitates formation of macroscopic structures like mushrooms.

  cell wall, glucan, fungi, chitin

  Publication DOI: 10.1002/biuz.201610599
  Journal NLM ID: 9201874
  Publisher: Weinheim: Wiley-VCH
  Correspondence: Kothe E
  Institutions: Institute of Microbiology, Friedrich Schiller University, Jena, Germany
  
   
  
  Saccharomyces cerevisiae
  CSDB ID 42638 (all data & tools)
• Article ID: 8658
  Aili D, Adour L, Houali K, Amrane A "Effect of temperature in chitin and chitosan production by solid culture of Penicillium camembertii on YPG medium" - International Journal of Biological Macromolecules 133 (2019) 998–1007
  

  This study was devoted to polysaccharides extraction (chitin and chitosan) from Penicillium camembertii cell wall. A culture on solid medium was adopted under carefully selected conditions, appropriate to mycelium growth: duration 6 days, medium YPGA and pH 5. The temperature was adjusted (20 °C to 28 °C) in order to study the effect of temperature on chitin/chitosan production. Biomass decreased with increasing temperatures: 13 g/L at 20 °C and 11.6 g/L at 28 °C. For all tested temperatures, the yields of insoluble alkaline fractions (AIM) were almost identical (200 mg/g). The solubility of fractions in 2% acetic acid allowed obtaining two fractions: an insoluble fraction (AcIM) with 18% of maximum yield and soluble fraction (AcSM) with 1% yield. The SEM micrographs of AcIM fractions were similar to AIM fractions. These showed a compact structure different from commercial chitin. The presence of chitin in P. Camembertii cultured in YPGA medium was also confirmed by ATR spectroscopy.

  chitin, Biomass, free chitosan, Penicillium camembertii, YPGA

  NCBI PubMed ID: 31004649
  Publication DOI: 10.1016/j.ijbiomac.2019.04.116
  Journal NLM ID: 7909578
  Publisher: Butterworth-Heinemann
  Correspondence: lyadour@gmail.com
  Institutions: Department of Chemistry, Faculty of Sciences, University Mouloud MAMMERI, Tizi-Ouzou, Algeria, Laboratory of analytical biochemistry and biotechnology, University Mouloud MAMMERI, Tizi-Ouzou, Algeria, Department of Chemistry, Faculty of Sciences, University Algiers, Algiers, Algeria, Bioengineering et Génie des Procédés (BIOGEP), Ecole Nationale Polytechnique, El Harrach, Algeria, Université de Rennes, Ecole Nationale Supérieure de Chimie de Rennes, Rennes, France
  Methods: IR, extraction, cell growth, SEM, centrifugation, optical microscopy
  
   
  
  Penicillium Camemberti Pc TT033
  CSDB ID 49501 (all data & tools)
• Article ID: 8666
  Crini G "Historical review on chitin and chitosan biopolymers" - Environmental Chemistry Letters 17 (2019) 1623–1643
  

  In 1799, Hatchett decalcified shells of crabs, lobsters, prawns and crayfish with mineral acids, observing that they produced a moderate effervescence and in a short time were found to be soft and plastic of a yellowish color and like a cartilage, which retained the original figure. Although this is the first mention of calcified chitin in invertebrates, the discovery of chitin is usually attributed both to Braconnot in 1811 who discovered chitin from fungi, and to Odier in 1823 who obtained a hornlike material after treatment of cockchafer elytra with potassium hydroxide. Chitin was first named fongine by Braconnot and then chitine by Odier. Children revealed the nitrogenous nature of chitin in 1824. The history of chitosan, the main derivative of chitin, dates back to 1859 with the work of Rouget. The name of chitosan was, however, introduced in 1894 by Hoppe-Seyler. In 1876, Ledderhose hydrolyzed arthropod chitin and discovered glykosamin, the first derivative of chitin. This review describes the 220 years of the development of chitin. I have roughly divided the story into five periods: discovery from 1799 to 1894, a period of confusion and controversy from 1894 to 1930, exploration in 1930–1950, a period of doubt from 1950 to 1970, and finally the period of application from 1970. The different periods are illustrated by examples of published studies, in particular from outstanding scholars who have left their mark on the history of this polysaccharide. Although this historic review is not exhaustive, it highlights the work of researchers who have contributed to the development of our knowledge of chitin throughout the 220 years of its history.

  History, chitosan, chitin, discovery, Braconnot, controversy, exploration, period of doubt, period of application

  Publication DOI: 10.1007/s10311-019-00901-0
  Journal NLM ID: 101220458
  Publisher: Secaucus, NJ: Springer-Verlag
  Correspondence: gregorio.crini@univ-fcomte.fr
  Institutions: Laboratoire Chrono-environnement, UMR 6249, UFR Sciences et Techniques, Université Bourgogne Franche-Comté, Besançon, France
  
   
  
  (fungi)
  CSDB ID 49523 (all data & tools)
• Article ID: 8674
  Moussian B "Chitin: structure, chemistry and biology" - Book: Targeting Chitin-containing Organisms (series: Advances in Experimental Medicine and Biology) (2019) Vol. 1142, Chapter 2, 5-18
  

  Chitin is a linear polysaccharide of the amino sugar N-acetyl glucosamine. It is present in the extracellular matrix of a variety of invertebrates including sponges, molluscs, nematodes and arthropods and fungi. Generally, it is an important component of protective or supportive extracellular matrices that cover the tissue that produces it or the whole body of the organism. Chitin fibres associate with each other adopting one of three possible crystalline organisations, i.e. α-, β- or γ-chitin. Usually, chitin fibre bundles interact with chitin-binding proteins forming higher order structures. Chitin laminae, which are two-dimensional sheets of α-chitin crystals with antiparallel running chitin fibres in association with β-folded proteins, are primary constituents of the arthropod cuticle and the fibrous extracellular matrix in sponges. A tri-dimensional composite material of proteins coacervates and β-chitin constitute hard biomaterials such as the squid beak. The molecular composition of γ-chitin-based structures that contribute to the physical barrier found in insect cocoons is less well studied. In principle, chitin is a versatile extracellular polysaccharide that in association with proteins defines the mechanical properties of tissues and organisms.

  evolution, Extracellular matrix, barrier, Cuticle, body shape

  NCBI PubMed ID: 31102240
  Publication DOI: 10.1007/978-981-13-7318-3_2
  Publisher: Singapore: Springer
  Correspondence: bernard.moussian@unice.fr
  Editors: Yang Q, Fukamizo T
  Institutions: Université Côte d'Azur, CNRS, Inserm, Institute of Biology Valrose, Nice, France
  
   
  
  (fungi)
  CSDB ID 49544 (all data & tools)
• Article ID: 8679
  Steinfeld L, Vafaei A, Rösner J, Merzendorfer H "Chitin prevalence and function in bacteria, fungi and protists" - Book: Targeting Chitin-containing Organisms (series: Advances in Experimental Medicine and Biology) (2019) Vol. 1142, Chapter 3, 19-59
  

  Chitin is an important structural polysaccharide, which supports and organizes extracellular matrices in a variety of taxonomic groups including bacteria, fungi, protists, and animals. Additionally, chitin has been recognized as a molecule that is required for Rhizobia-legume symbiosis and involved in arbuscular mycorrhizal signaling in the symbiotic interaction between terrestrial plants and fungi. Moreover, it serves as a unique molecular pattern in the plant defense system against pathogenic fungi and parasites, and in the innate and adaptive immune response of mammals and humans. In this review, we will focus on the prevalence and structural function of chitin in bacteria, fungi, and protists, with a particular focus on the evolution of chitin synthases and the function of chitin oligosaccharides as a signaling molecule in symbiosis and immunity.

  Rhizobia, cell wall, fungi, protists, skeleton

  NCBI PubMed ID: 31102241
  Publication DOI: 10.1007/978-981-13-7318-3_3
  Publisher: Singapore: Springer
  Correspondence: Merzendorfer H
  Editors: Yang Q, Fukamizo T
  Institutions: Department of Chemistry and Biology - Molecular Biology, University of Siegen, Siegen, Germany
  
   
  
  Azorhizobium caulinodans, Rhizobium leguminosarum, Sinorhizobium meliloti, Saccharomyces cerevisiae
  CSDB ID 49564 (all data & tools)
• Article ID: 8681
  Yang J, Zhang K-Q "Chitin synthesis and degradation in fungi: biology and enzymes" - Book: Targeting Chitin-containing Organisms (series: Advances in Experimental Medicine and Biology) (2019) Vol. 1142, Chapter 8, 153-167
  

  Chitin is one of the most important carbohydrates of the fungal cell wall, and is synthesized by chitin synthases. Chitin can be degraded by chitinases, which are important virulence factors in pathogenic fungi. Knowledge about the biosynthesis and degradation of chitin, and the enzymes responsible, has accumulated in recent years. In this review, we analyze the amino acid sequences of chitin synthases from several typical fungi. These enzymes can be divided into seven groups. While the different chitin synthases from a single fungus share a low degree of similarity, the same type of chitin synthase from different fungi shows high similarity. The number of chitinase genes in fungi display wide variation, from a single gene in Schizosaccharomyces pombe, to 36 genes in Trichoderma virens. Chitinases from different fungi can be divided into four groups. The functions of chitin synthases and chitinases in several typical fungi are summarized, and the crystal structures of chitinases and chitinase modification are also discussed.

  crystal structure, modification, chitin, chitin synthase, chitinase

  NCBI PubMed ID: 31102246
  Publication DOI: 10.1007/978-981-13-7318-3_8
  Publisher: Singapore: Springer
  Correspondence: kqzhang1@ynu.edu.cn
  Editors: Yang Q, Fukamizo T
  Institutions: State Key Laboratory for Conservation and Utilization of Bio-Resources in Yunnan, and Key Laboratory for Microbial Resources of the Ministry of Education, Yunnan University, Kunming, China
  
   
  
  (fungi)
  CSDB ID 49568 (all data & tools)
• Article ID: 8767
  Luu VT, Moon HY, Yoo SJ, Choo JH, Thak EJ, Kang HA "Development of conditional cell lysis mutants of Saccharomyces cerevisiae as production hosts by modulating OCH1 and CHS3 expression" - Applied Microbiology and Biotechnology 103(5) (2019) 2277-2293
  

  The traditional yeast Saccharomyces cerevisiae has been widely used as a host for the production of recombinant proteins and metabolites with industrial potential. However, its thick and rigid cell wall presents problems for the effective recovery of products. In this study, we modulated the expression of ScOCH1, encoding the α-1,6-mannosyltransferase responsible for outer chain biosynthesis of N-glycans, and ScCHS3, encoding the chitin synthase III required for synthesis of the majority of cell wall chitin, by exploiting the repressible ScMET3 promoter. The conditional single mutants PMET3-OCH1 and PMET3-CHS3 and the double mutant PMET3-OCH1/PMET3-CHS3 showed comparable growth to the wild-type strain under normal conditions but exhibited increased sensitivity to temperature and cell wall-disturbing agents in the presence of methionine. Such conditional growth defects were fully recovered by supplementation with 1 M sorbitol. The osmotic lysis of the conditional mutants cultivated with methionine was sufficient to release the intracellularly expressed recombinant protein, nodavirus capsid protein, with up to 60% efficiency, compared to lysis by glass bead breakage. These mutant strains also showed approximately three-fold-enhanced secretion of a recombinant extracellular glycoprotein, Saccharomycopsis fibuligera β-glucosidase, with markedly reduced hypermannosylation, particularly in the PMET3-OCH1 mutants. Furthermore, a substantial increase of extracellular glutathione production, up to four-fold, was achieved with the conditional mutant yeast cells. Together, our data support that the conditional cell wall lysis mutants constructed based on the modulation of ScOCH1 and ScCHS3 expression would likely be useful hosts for the improved recovery of proteins and metabolites with industrial application.

  α-1, conditional mutant, Saccharomyces cerevisiae, 6-mannosyltransferase, chitin synthase III, MET3 promoter

  NCBI PubMed ID: 30706115
  Publication DOI: 10.1007/s00253-019-09614-4
  Journal NLM ID: 8406612
  Publisher: Springer
  Correspondence: Kang HA
  Institutions: Department of Life Science, College of Natural Science, Chung-Ang University, Seoul, South Korea
  Methods: PCR, DNA techniques, Western blotting, colorimetry, cloning, cell growth, enzymatic assay, gene expression, qRT-PCR, osmotic lysis
  
   
  
  Saccharomyces cerevisiae
  CSDB ID 49870 (all data & tools)
• Article ID: 8770
  Patel PK, Free SJ "The genetics and biochemistry of cell wall structure and synthesis in Neurospora crassa, a model filamentous fungus" - Frontiers in Microbiology 10 (2019) ID 2294
  

  This review discusses the wealth of information available for the N. crassa cell wall. The basic organization and structure of the cell wall is presented and how the wall changes during the N. crassa life cycle is discussed. Over forty cell wall glycoproteins have been identified by proteomic analyses. Genetic and biochemical studies have identified many of the key enzymes needed for cell wall biogenesis, and the roles these enzymes play in cell wall biogenesis are discussed. The review includes a discussion of how the major cell wall components (chitin, β-1,3-glucan, mixed β-1,3-/β-1,4- glucans, glycoproteins, and melanin) are synthesized and incorporated into the cell wall. We present a four-step model for how cell wall glycoproteins are covalently incorporated into the cell wall. In N. crassa, the covalent incorporation of cell wall glycoproteins into the wall occurs through a glycosidic linkage between lichenin (a mixed β-1,3-/β-1,4- glucan) and a "processed" galactomannan that has been attached to the glycoprotein N-linked oligosaccharides. The first step is the addition of the galactomannan to the N-linked oligosaccharide. Mutants affected in galactomannan formation are unable to incorporate glycoproteins into their cell walls. The second step is carried out by the enzymes from the GH76 family of α-1,6-mannanases, which cleave the galactomannan to generate a processed galactomannan. The model suggests that the third and fourth steps are carried out by members of the GH72 family of glucanosyltransferases. In the third step the glucanosyltransferases cleave lichenin and generate enzyme/substrate intermediates in which the lichenin is covalently attached to the active site of the glucanosyltransferases. In the final step, the glucanosyltransferases attach the lichenin onto the processed galactomannans, which creates new glycosidic bonds and effectively incorporates the glycoproteins into the cross-linked cell wall glucan/chitin matrix.

  cell wall, Galactomannan, glucan, filamentous fungi, melanin, Neurospora, glucanosyltransferase, mannanase

  NCBI PubMed ID: 31649638
  Publication DOI: 10.3389/fmicb.2019.02294
  Journal NLM ID: 101548977
  Publisher: Lausanne: Frontiers Research Foundation
  Correspondence: free@buffalo.edu
  Institutions: Department of Biological Sciences, SUNY University at Buffalo, Buffalo, NY, USA
  
   
  
  Neurospora crassa (Δdfg-5 mutant), Neurospora crassa (Δdcw-1 mutant), Neurospora crassa (Δgel-1 mutant), Neurospora crassa (Δgel-2 mutant), Neurospora crassa (Δgel-5 mutant), Neurospora crassa (Δoch-1 mutant)
  CSDB ID 49873 (all data & tools)
• Article ID: 8833
  Lecointe K, Cornu M, Leroy J, Coulon P, Sendid B "Polysaccharides cell wall architecture of Mucorales" - Frontiers in Microbiology 10 (2019) ID 469
  

  Invasive fungal infections are some of the most life-threatening infectious diseases in the hospital setting. In industrialized countries, the most common fungal species isolated from immunocompromised patients are Candida and Aspergillus spp. However, the number of infections due to Mucorales spp. is constantly increasing and little is known about the virulence factors of these fungi. The fungal cell wall is an important structure protecting fungi from the environment. A better knowledge of its composition should improve our understanding of host-pathogen interactions. Cell wall molecules are involved in tissue adherence, immune escape strategies, and stimulation of host defenses including phagocytosis and mediators of humoral immunity. The fungal cell wall is also a target of choice for the development of diagnostic or therapeutic tools. The present review discusses our current knowledge on the cell wall structure of Mucorales in terms of the polysaccharides and glyco-enzymes involved in its biosynthesis and degradation, with an emphasis on the missing gaps in our knowledge.

  polysaccharides, cell wall, glucuronic acid, Mucorales, glyco-enzymes

  NCBI PubMed ID: 30941108
  Publication DOI: 10.3389/fmicb.2019.00469
  Journal NLM ID: 101548977
  Publisher: Lausanne: Frontiers Research Foundation
  Correspondence: Sendid B
  Institutions: Lille Inflammation Research International Center, UMR 995 Inserm, Fungal Associated Invasive and Inflammatory Diseases, CHU Lille, Lille University, Lille, France, Laboratory of Parasitology and Mycology, Institute of Microbiology, CHU Lille, Lille, France
  
   
  
  Mucorales
  CSDB ID 50015 (all data & tools)
• Article ID: 8931
  Araújo D, Ferreira IC, Torres CAV, Neves L, Freitas F "Chitinous polymers: extraction from fungal sources, characterization and processing towards value-added applications" - Journal of Chemical Technology and Biotechnology 95(5) (2020) 1277-1289
  

  Chitin, chitosan and their complexes with β-glucan (chitin–glucan complex, CGC, and chitosan–glucan complex, ChGC) are value-added polysaccharides extracted from the cell-walls of many fungi. Commercial chitin and its deacetylated form, chitosan, are currently obtained from marine waste material, mostly animal sources (crustaceans and marine invertebrates), through harsh chemical procedures that have low reproducibility due to the variability of the composition of the sources and their seasonal character. These disadvantages are overcome by using fungi as sources of chitinous polymers. The extraction of chitin/chitosan from fungi cell-walls has the great advantage of yielding products with stable composition and properties, using simpler procedures, with the added benefit of also generating CGC and ChGC, two copolymers that combine the proven properties of chitin/chitosan with those of β-glucans. Over the last decades, fungal chitinous polymers have been the focus of extensive research that included optimization of the cultivation conditions of a wide range of species and the development of optimized extraction, purification and characterization techniques, as well as the demonstration of the biopolymers' biological properties, which include immunomodulatory, anticancer, antioxidant and antimicrobial activity. Given these properties, several attempts were made to develop applications for them in areas ranging from biomedicine and pharmaceuticals to food and agriculture. Despite their wide range of proven functional properties that include the ability to form different polymeric structures, as well as biological activity, fungal chitinous biopolymers are still underexplored. Nevertheless, these biopolymers hold great potential for development into valuable products or applications that are surely worth further investigation.

  fungi, chitosan, chitin, cell-wall polysaccharides, chitin–glucan complex (CGC), chitosan–glucan complex (ChGC)

  Publication DOI: 10.1002/jctb.6325
  Journal NLM ID: 8711102
  Publisher: Chichester Sussex: Published For The Society Of Chemical Industry By Wiley And Sons Ltd
  Correspondence: Freitas F
  Institutions: UCIBIO-REQUIMTE, Chemistry Department, Faculty of Sciences and Technology, NOVA University of Lisbon, Lisbon, Portugal, LAQV-REQUIMTE, Chemistry Department, Faculty of Sciences and Technology, NOVA University of Lisbon, Lisbon, Portugal
  
   
  
  Rhizopus arrhizus, Cunninghamella elegans, Aspergillus terreus, Ganoderma tsugae, Saccharomyces cerevisiae, Mucor mucedo, Phycomyces blakesleeanus, Aspergillus niger, Mucor rouxii
  CSDB ID 50302 (all data & tools)
• Article ID: 8933
  Asif T, Javed U, Zafar SB, Ansari A, Qader SAU, Aman A "Bioconversion of colloidal chitin using novel chitinase from Glutamicibacter uratoxydans exhibiting anti-fungal potential by hydrolyzing chitin within fungal cell wall" - Waste and Biomass Valorization 11 (2020) 4129–4143
  

  Chitin is a unique structural exopolysaccharide abundantly found in nature. This exopolysaccharide has a unique chemical structure that acts as a protective outermost covering for most of the crustaceans in aquatic ecosystem. This fortification is because of the insoluble nature of this exopolysaccharide which consist of a linear chain of β-(1→4)-linked-N-acetylglucosamine units. Chitin is hydrolyzed with the help of a hydrolase known as chitinase. Variety of microbial species have been explored for chitinase production. Chitinolytic microbial species can be alternatively used for degradation of chitin instead of chemical treatment in agricultural sector. This biological approach has lesser environmental impact because of its apparently safe nature. In the current study, bioprospecting of chitinase producing species was conducted and different chitinolytic bacterial strains were screened for chitinase production which could have anti-fungal potential. Bacterial isolates were identified based on polyphasic approach and the enzyme production was optimized using one-variable-at-a-time technique. Hyphal extension method was used for determination of anti-fungal potential of chitinase.Glutamicibacter uratoxydans was indigenously isolated and identified for chitinase production. G. uratoxydans is a novel bacterial species which has not been previously explored to produce chitinase or other hydrolases. G. uratoxydans biosynthesized chitinase utilizing colloidal chitin as a sole source of carbon. The chitinase biosynthesized by G. uratoxydans is effectively potent against Aspergillus fumigatus thus, suggesting that this extracellular enzyme could be used for the treatment of fungal infection caused by filamentous fungi.

  cell wall, antifungal activity, chitin, chitinase, Glutamicibacter uratoxydans

  Publication DOI: 10.1007/s12649-019-00746-2
  Journal NLM ID: 101670525
  Publisher: Dordrecht, Netherlands: Springer
  Correspondence: saqader@uok.edu.pk
  Institutions: The Karachi Institute of Biotechnology & Genetic Engineering (KIBGE), University of Karachi, Karachi, Pakistan, Department of Biochemistry, University of Karachi, Karachi, Pakistan
  Methods: PCR, cell growth, enzymatic assay, DNA extraction, precipitation, SEM, centrifugation, antifungal activity test, protein determination, BLAST
  
   
  
  Aspergillus fumigatus KIBGE-IB33, Aspergillus flavus KIBGE-IB34, Aspergillus terreus KIBGE-IB35, Aspergillus niger KIBGE-IB36
  CSDB ID 50305 (all data & tools)
• Article ID: 8934
  Brown HE, Esher SK, Alspaugh JA "Chitin: A "hidden figure" in the fungal cell wall" - Current Topics in Microbiology and Immunology 425 (2020) 83-111
  

  Chitin and chitosan are two related polysaccharides that provide important structural stability to fungal cell walls. Often embedded deeply within the cell wall structure, these molecules anchor other components at the cell surface. Chitin-directed organization of the cell wall layers allows the fungal cell to effectively monitor and interact with the external environment. For fungal pathogens, this interaction includes maintaining cellular strategies to avoid excessive detection by the host innate immune system. In turn, mammalian and plant hosts have developed their own strategies to process fungal chitin, resulting in chitin fragments of varying molecular size. The size-dependent differences in the immune activation behaviors of variably sized chitin molecules help to explain how chitin and related chitooligomers can both inhibit and activate host immunity. Moreover, chitin and chitosan have recently been exploited for many biomedical applications, including targeted drug delivery and vaccine development.

  NCBI PubMed ID: 31807896
  Publication DOI: 10.1007/82_2019_184
  Journal NLM ID: 0110513
  Publisher: Heidelberg: Springer Verlag
  Correspondence: andrew.alspaugh@duke.edu
  Institutions: Department of Medicine, Department of Molecular Genetics and Microbiology, Duke University School of Medicine, Durham, USA, Department of Microbiology and Immunology, Tulane University School of Medicine, New Orleans, USA
  
   
  
  (fungi)
  CSDB ID 50306 (all data & tools)
• Article ID: 8936
  Chrissian C, Lin CP, Camacho E, Casadevall A, Neiman AM, Stark RE "Unconventional constituents and shared molecular architecture of the melanized cell wall of C. neoformans and spore wall of S. cerevisiae" - Journal of Fungi 6(4) (2020) ID 329
  

  The fungal cell wall serves as the interface between the cell and the environment. Fungal cell walls are composed largely of polysaccharides, primarily glucans and chitin, though in many fungi stress-resistant cell types elaborate additional cell wall structures. Here, we use solid-state nuclear magnetic resonance spectroscopy to compare the architecture of cell wall fractions isolated from Saccharomyces cerevisiae spores and Cryptococcus neoformans melanized cells. The specialized cell walls of these two divergent fungi are highly similar in composition. Both use chitosan, the deacetylated derivative of chitin, as a scaffold on which a polyaromatic polymer, dityrosine and melanin, respectively, is assembled. Additionally, we demonstrate that a previously identified but uncharacterized component of the S. cerevisiae spore wall is composed of triglycerides, which are also present in the C. neoformans melanized cell wall. Moreover, we identify a tyrosine-derived constituent in the C. neoformans wall that, although it is not dityrosine, is a non-pigment constituent of the cell wall. The similar composition of the walls of these two phylogenetically distant species suggests that triglycerides, polyaromatics, and chitosan are basic building blocks used to assemble highly stress-resistant cell walls and the use of these constituents may be broadly conserved in other fungal species.

  chitosan, Saccharomyces cerevisiae, chitin, fungal cell wall, Cryptococcus neoformans, melanin, solid-state NMR, macromolecular assembly, dityrosine, triglycerides

  NCBI PubMed ID: 33271921
  Publication DOI: 10.3390/jof6040329
  Journal NLM ID: 101671827
  Publisher: Basel, Switzerland: MDPI AG
  Correspondence: Neiman AM ; Stark RE
  Institutions: Department of Molecular Microbiology and Immunology, Johns Hopkins Bloomberg School of Public Health, Johns Hopkins University, Baltimore, USA, CUNY Institute for Macromolecular Assemblies, City University of New York, New York, NY, USA, Department of Chemistry and Biochemistry, The City College of New York, New York, USA, Ph.D. Program in Biochemistry, The Graduate Center of the City University of New York, New York, NY, USA, Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, USA
  Methods: enzymatic digestion, isotopic labeling, cell growth, delipidation, centrifugation, hydrolysis, 13C CPMAS NMR, 13C-13C DARR NMR
  
   
  
  Saccharomyces cerevisiae AN120, Cryptococcus neoformans H99
  CSDB ID 50309 (all data & tools)
• Article ID: 8937
  Chrissian C, Camacho E, Fu MS, Prados-Rosales R, Chatterjee S, Cordero RJB, Lodge JK, Casadevall A, Stark RE "Melanin deposition in two Cryptococcus species depends on cell-wall composition and flexibility" - Journal of Biological Chemistry 295(7) (2020) 1815-1828
  

  Cryptococcus neoformans and Cryptococcus gattii are two species complexes in the large fungal genus Cryptococcus and are responsible for potentially lethal disseminated infections. These two complexes share several phenotypic traits, such as production of the protective compound melanin. In C. neoformans, the pigment associates with key cellular constituents that are essential for melanin deposition within the cell wall. Consequently, melanization is modulated by changes in cell-wall composition or ultrastructure. However, whether similar factors influence melanization in C. gattii is unknown. Herein, we used transmission EM, biochemical assays, and solid-state NMR spectroscopy of representative isolates and "leaky melanin" mutant strains from each species complex to examine the compositional and structural factors governing cell-wall pigment deposition in C. neoformans and C. gattii. The principal findings were the following. 1) C. gattii R265 had an exceptionally high chitosan content compared with C. neoformans H99; a rich chitosan composition promoted homogeneous melanin distribution throughout the cell wall but did not increase the propensity of pigment deposition. 2) Strains from both species manifesting the leaky melanin phenotype had reduced chitosan content, which was compensated for by the production of lipids and other nonpolysaccharide constituents that depended on the species or mutation. 3) Changes in the relative rigidity of cell-wall chitin were associated with aberrant pigment retention, implicating cell-wall flexibility as an independent variable in cryptococcal melanin assembly. Overall, our results indicate that cell-wall composition and molecular architecture are critical factors for the anchoring and arrangement of melanin pigments in both C. neoformans and C. gattii species complexes.

  polysaccharides, Molecular Structure, cell wall, virulence factor, opportunistic pathogen, nuclear magnetic resonance (NMR), fungi, Cryptococcus, melanin, solid-state NMR

  NCBI PubMed ID: 31896575
  Publication DOI: 10.1074/jbc.RA119.011949
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: rstark@ccny.cuny.edu
  Institutions: Department of Preventive Medicine and Public Health and Microbiology, Autonoma University of Madrid, Madrid, Spain, Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, USA, Department of Molecular Microbiology and Immunology, Johns Hopkins Bloomberg School of Public Health, Johns Hopkins University, Baltimore, USA, Ph.D. Program in Biochemistry, The Graduate Center of the City University of New York, New York, NY, USA, Department of Chemistry and Biochemistry, City College of New York and CUNY Institute for Macromolecular Assemblies, New York, USA, Department of Microbiology and Immunology, Albert Einstein College of Medicine, Yeshiva University, Bronx, USA
  Methods: acid hydrolysis, extraction, isotopic labeling, cell growth, derivatization, TEM, light microscopy, 13C CPMAS NMR, 2D NMR, 13C-13C DARR NMR, 13C DPMAS NMR
  
   
  
  Cryptococcus neoformans H99, Cryptococcus neoformans ST211A, Cryptococcus gattii R265, Cryptococcus gattii Cg53
  CSDB ID 50312 (all data & tools)
• Article ID: 8938
  Lopez-Santamarina A, Mondragon ADC, Lamas A, Miranda JM, Franco CM, Cepeda A "Animal-origin prebiotics based on chitin: An alternative for the future? A critical review" - Foods 9(6) (2020) ID 782
  

  The human gut microbiota has been revealed in recent years as a factor that plays a decisive role in the maintenance of human health, as well as in the development of many non-communicable diseases. This microbiota can be modulated by various dietary factors, among which complex carbohydrates have a great influence. Although most complex carbohydrates included in the human diet come from vegetables, there are also options to include complex carbohydrates from non-vegetable sources, such as chitin and its derivatives. Chitin, and its derivatives such as chitosan can be obtained from non-vegetable sources, the best being insects, crustacean exoskeletons and fungi. The present review offers a broad perspective of the current knowledge surrounding the impacts of chitin and its derived polysaccharides on the human gut microbiota and the profound need for more in-depth investigations into this topic. Overall, the effects of whole insects or meal on the gut microbiota have contradictory results, possibly due to their high protein content. Better results are obtained for the case of chitin derivatives, regarding both metabolic effects and effects on the gut microbiota composition.

  polysaccharides, insect, gut microbiota, prebiotic, chitosan, chitin, crustacean

  NCBI PubMed ID: 32545663
  Publication DOI: 10.3390/foods9060782
  Journal NLM ID: 101670569
  Publisher: Basel, Switzerland: MDPI AG
  Correspondence: Lopez-Santamarina A ; Mondragon ADC ; Lamas A ; Miranda JM ; Franco CM ; Cepeda A
  Institutions: Laboratorio de Higiene Inspección y Control de Alimentos, Departamento de Química Analítica, Nutrición y Bromatología, Facultad de Veterinaria, Universidade de Santiago de Compostela, Lugo, Spain
  
   
  
  (fungi)
  CSDB ID 50313 (all data & tools)
• Article ID: 8940
  Savin S, Craciunescu O, Oancea A, Ilie D, Ciucan T, Antohi LS, Toma A, Nicolescu A, Deleanu C, Oancea F "Antioxidant, cytotoxic and antimicrobial activity of chitosan preparations extracted from Ganoderma lucidum mushroom" - Chemistry and Biodiversity 17(7) (2020) ID e2000175
  

  Two chitosan extracts were prepared by chemical and enzymatic treatment of Ganoderma lucidum mushroom, as an alternative source to crustacean shells. The molecular weight of the enzymatic extract was lower than that of the chemical one and of shrimp chitosan, as determined by viscosity measurements. Characteristic signals were identified in the 1 H-NMR spectra and high deacetylation degree indicated good physico-chemical properties for both mushroom chitosan extracts. The scavenging capacity of mushroom chitosan extracts was moderate against the synthetic radicals of 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and 1,1-diphenyl-2-picrylhydrazyl (DPPH), but higher values were observed for the enzymatic extract, compared to the chemical extract and shrimp chitosan. In vitro cytotoxicity was evaluated in L929 mouse fibroblast cell lines and the results of MTT assay showed good cytocompatibility in the tested range of concentrations. The growth of Gram-positive bacteria was inhibited more than Gram-negative bacteria in the presence of mushroom chitosan extracts, in particular by the chemical one, indicating their efficiency as antimicrobial agents. All these results strengthen the evidence of mushroom polysaccharide preparations availability for biomedical applications.

  extraction, deacetylation, fungi, radical scavenging activity, α-amylase

  NCBI PubMed ID: 32333466
  Publication DOI: 10.1002/cbdv.202000175
  Journal NLM ID: 101197449
  Publisher: Verlag Helvetica Chimica Acta
  Correspondence: Craciunescu O ; office@incdsb.ro
  Institutions: National Institute of Research and Development for Biological Sciences, Bucharest, Romania, ''Petru Poni'' Institute of Macromolecular Chemistry, Iasi, Romania, National Institute for Research and Development in Chemistry and Petrochemistry - ICECHIM, Bucharest, Romania
  Methods: 1H NMR, alkaline hydrolysis, enzymatic digestion, extraction, antioxidant activities, cell viability assay, cytotoxicity assay, precipitation, antimicrobial assay, centrifugation, optical density measurement, deproteinization
  
   
  
  Ganoderma lucidum
  CSDB ID 50316 (all data & tools)
• Article ID: 8941
  Schönbichler A, Díaz-Moreno SM, Srivastava V, McKee LS "Exploring the potential for fungal antagonism and cell wall attack by Bacillus subtilis natto" - Frontiers in Microbiology 11 (2020) ID 521
  

  To develop more ecologically sustainable agricultural practices requires that we reduce our reliance on synthetic chemical pesticides for crop protection. This will likely involve optimized biocontrol approaches - the use of beneficial soil microbes to attack potential plant pathogens to protect plants from diseases. Many bacterial species, including strains of Bacillus subtilis, have been explored for their biocontrol properties, as they can control the growth of harmful fungi, often by disrupting the fungal cell wall. A strain that is not often considered for this particular application is Bacillus subtilis natto, primarily known for fermenting soybeans via cell wall degradation in the Japanese probiotic dish "natto." Because deconstruction of the fungal cell wall is considered an important biocontrol trait, we were motivated to explore the possible anti-fungal properties of the B. subtilis natto strain. We show that B. subtilis natto can use complex fungal material as a carbon source for growth, and can effectively deconstruct fungal cell walls. We found degradation of fungal cell wall proteins, and showed that growth on a mix of peptides was very strong. We also found that intact fungal cell walls can induce the secretion of chitinases and proteases. Surprisingly, we could show that chitin, the bulk component of the fungal cell wall, does not permit successful growth of the natto strain or induce the secretion of chitinolytic enzymes, although these were produced during exposure to proteins or to complex fungal material. We have further shown that protease secretion is likely a constitutively enabled mechanism for nutrient scavenging by B. subtilis natto, as well as a potent tool for the degradation of fungal cell walls. Overall, our data highlight B. subtilis natto as a promising candidate for biocontrol products, with relevant behaviors that can be optimized by altering growth conditions. Whereas it is common for bacterial biocontrol products to be supplied with chitin or chitosan as a priming polysaccharide, our data indicate that this is not a useful approach with this particular bacterium, which should instead be supplied with either glucose or attenuated fungal material.

  protease, secretome, fungal cell wall, chitinase, biocontrol, Bacillus subtilis natto

  NCBI PubMed ID: 32296406
  Publication DOI: 10.3389/fmicb.2020.00521
  Journal NLM ID: 101548977
  Publisher: Lausanne: Frontiers Research Foundation
  Correspondence: mckee@kth.se
  Institutions: Division of Glycoscience, Department of Chemistry, KTH Royal Institute of Technology, AlbaNova University Centre, Stockholm, Sweden, Wallenberg Wood Science Center, Stockholm, Sweden
  Methods: SDS-PAGE, extraction, cell growth, LC-ESI-MS/MS, enzymatic assay, spectrophotometry, Bradford method, centrifugation
  
   
  
  Agaricus bisporus
  CSDB ID 50318 (all data & tools)
• Article ID: 9235
  Chakraborty A, Fernando LD, Fang W, Dickwella Widanage MC, Wei P, Jin C, Fontaine T, Latgé J-P, Wang T "A molecular vision of fungal cell wall organization by functional genomics and solid-state NMR" - Nature Communications 12(1) (2021) ID 6346
  

  Vast efforts have been devoted to the development of antifungal drugs targeting the cell wall, but the supramolecular architecture of this carbohydrate-rich composite remains insufficiently understood. Here we compare the cell wall structure of a fungal pathogen Aspergillus fumigatus and four mutants depleted of major structural polysaccharides. High-resolution solid-state NMR spectroscopy of intact cells reveals a rigid core formed by chitin, β-1,3-glucan, and α-1,3-glucan, with galactosaminogalactan and galactomannan present in the mobile phase. Gene deletion reshuffles the composition and spatial organization of polysaccharides, with significant changes in their dynamics and water accessibility. The distribution of α-1,3-glucan in chemically isolated and dynamically distinct domains supports its functional diversity. Identification of valines in the alkali-insoluble carbohydrate core suggests a putative function in stabilizing macromolecular complexes. We propose a revised model of cell wall architecture which will improve our understanding of the structural response of fungal pathogens to stresses.

  polysaccharides, Aspergillus fumigatus, chitin, fungal cell wall, solid-state NMR

  NCBI PubMed ID: 34732740
  Publication DOI: 10.1038/s41467-021-26749-z
  Journal NLM ID: 101528555
  Publisher: London: Nature Publishing Group
  Correspondence: Latgé J-P ; Wang T
  Institutions: State Key Laboratory of Mycology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China, Department of Chemistry, Louisiana State University, Baton Rouge, USA, State Key Laboratory of Non-food Biomass and Enzyme Technology, Guangxi Academy of Sciences, Nanning, China, Unité de Biologie et pathogénicité fongiques, INRAE, USC2019, Institut Pasteur, Paris, France, Institute of Molecular biology and Biotechnology (IMBBFORTH), University of Crete, Heraklion, Greece
  Methods: acid hydrolysis, GLC, HPAEC, enzymatic digestion, extraction, acetylation, reduction, isotopic labeling, cell growth, mutagenesis, derivatization, evaporation, centrifugation, ssNMR
  
   
  
  Aspergillus fumigatus ΔakuBKU80
  CSDB ID 40899 (all data & tools)
• Article ID: 9238
  Curto MA, Butassi E, Ribas JC, Svetaz LA, Cortés JCG "Natural products targeting the synthesis of β(1,3)-D-glucan and chitin of the fungal cell wall. Existing drugs and recent findings" - Phytomedicine 88 (2021) ID 153556
  

  Background: During the last three decades systemic fungal infections associated to immunosuppressive therapies have become a serious healthcare problem. Clinical development of new antifungals is an urgent requirement. Since fungal but not mammalian cells are encased in a carbohydrate-containing cell wall, which is required for the growth and viability of fungi, the inhibition of cell wall synthesizing machinery, such as β(1,3)-D-glucan synthases (GS) and chitin synthases (CS) that catalyze the synthesis of β(1-3)-D-glucan and chitin, respectively, represent an ideal mode of action of antifungal agents. Although the echinocandins anidulafungin, caspofungin and micafungin are clinically well-established GS inhibitors for the treatment of invasive fungal infections, much effort must still be made to identify inhibitors of other enzymes and processes involved in the synthesis of the fungal cell wall. Purpose: Since natural products (NPs) have been the source of several antifungals in clinical use and also have provided important scaffolds for the development of semisynthetic analogues, this review was devoted to investigate the advances made to date in the discovery of NPs from plants that showed capacity of inhibiting cell wall synthesis targets. The chemical characterization, specific target, discovery process, along with the stage of development are provided here. Methods: An extensive systematic search for NPs against the cell wall was performed considering all the articles published until the end of 2020 through the following scientific databases: NCBI PubMed, Scopus and Google Scholar and using the combination of the terms 'natural antifungals' and 'plant extracts' with 'fungal cell wall'. Results: The first part of this review introduces the state of the art of the structure and biosynthesis of the fungal cell wall and considers exclusively those naturally produced GS antifungals that have given rise to both existing semisynthetic approved drugs and those derivatives currently in clinical trials. According to their chemical structure, natural GS inhibitors can be classified as 1) cyclic lipopeptides, 2) glycolipids and 3) acidic terpenoids. We also included nikkomycins and polyoxins, NPs that inhibit the CS, which have traditionally been considered good candidates for antifungal drug development but have finally been discarded after enduring unsuccessful clinical trials. Finally, the review focuses in the most recent findings about the growing field of plant-derived molecules and extracts that exhibit activity against the fungal cell wall. Thus, this search yielded sixteen articles, nine of which deal with pure compounds and seven with plant extracts or fractions with proven activity against the fungal cell wall. Regarding the mechanism of action, seven (44%) produced GS inhibition while five (31%) inhibited CS. Some of them (56%) interfered with other components of the cell wall. Most of the analyzed articles refer to tests carried out in vitro and therefore are in early stages of development. Conclusion: This report delivers an overview about both existing natural antifungals targeting GS and CS activities and their mechanisms of action. It also presents recent discoveries on natural products that may be used as starting points for the development of potential selective and non-toxic antifungal drugs.

  Plant Extracts, chitin, fungal cell wall, antifungal drugs, bioactive natural products, cell wall synthases, systemic fungal infection

  NCBI PubMed ID: 33958276
  Publication DOI: 10.1016/j.phymed.2021.153556
  Journal NLM ID: 9438794
  Publisher: Stuttgart: Urban & Fischer Verlag
  Correspondence: Svetaz LA ; Cortés JCG
  Institutions: Instituto de Biología Funcional y Genómica and Departamento de Microbiología y Genética, Consejo Superior de Investigaciones Científicas (CSIC)/Universidad de Salamanca, Salamanca, Spain, Área Farmacognosia, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Argentina
  
   
  
  (fungi)
  CSDB ID 40906 (all data & tools)
• Article ID: 9348
  Ghassemi N, Poulhazan A, Deligey F, Mentink-Vigier F, Marcotte I, Wang T "Solid-State NMR Investigations of Extracellular Matrixes and Cell Walls of Algae, Bacteria, Fungi, and Plants" - Chemical Reviews 122(10) (2022) 10036-10086
  

  Extracellular matrixes (ECMs), such as the cell walls and biofilms, are important for supporting cell integrity and function and regulating intercellular communication. These biomaterials are also of significant interest to the production of biofuels and the development of antimicrobial treatment. Solid-state nuclear magnetic resonance (ssNMR) and magic-angle spinning-dynamic nuclear polarization (MAS-DNP) are uniquely powerful for understanding the conformational structure, dynamical characteristics, and supramolecular assemblies of carbohydrates and other biomolecules in ECMs. This review highlights the recent high-resolution investigations of intact ECMs and native cells in many organisms spanning across plants, bacteria, fungi, and algae. We spotlight the structural principles identified in ECMs, discuss the current technical limitation and underexplored biochemical topics, and point out the promising opportunities enabled by the recent advances of the rapidly evolving ssNMR technology.

  bacteria, algae, Plants, fungi, ssNMR

  NCBI PubMed ID: 34878762
  Publication DOI: 10.1021/acs.chemrev.1c00669
  Journal NLM ID: 2985134R
  Publisher: Chem Rev
  Correspondence: T. Wang < tuowang@lsu.edu>
  Institutions: Department of Chemistry, Louisiana State University, Baton Rouge, Louisiana 70803, United States, Department of Chemistry, Universite du Quebec a Montreal, Montreal H2X 2J6, Canada, National High Magnetic Field Laboratory, Tallahassee, Florida 32310, United States
  
   
  
  Aspergillus fumigatus, Candida albicans
  CSDB ID 51623 (all data & tools)
• Article ID: 10541
  Schetz JA, Anderson PAV "Glycosylation patterns of membrane proteins of the jellyfish Cyanea capillata" - Cell and Tissue Research 279 (1994) 315-321
  

  Integral and membrane-associated proteins extracted from neuron-enriched perirhopalial tissue of the jellyfish Cyanea capillata were probed with a panel of lectins that recognize sugar epitopes of varying complexity. Of the 13 lectins tested, only concanavalin A, jacalin lectin and tomato lectin stained distinct bands on Western blots, indicating the presence of repeating α-1,6-mannoses, terminal Gal-α-1,6-GalNAc and repeating β-1,4-linked GlcNAc, respectively. In whole-mounted perirhopalial tissue, jacalin lectin stained several cell types, including neurons, muscle, cilia and mucus strands. Tomato lectin stained secretory cells intensely, and neurons in a punctate fashion. Concanavalin A stained cytoplasmic epitopes in both ecto-and endodermal cells, and ectodermal secretory cells and the mucus strands emanating from them. With the exception of tomato lectin's sugar epitope, the other sugar epitopes identified in this study are “non-complex.” This study suggests that while glycosylation of integral and membrane-associated proteins occurs in Cyanea, the sugars post-translationally linked to these proteins tend to be simple.

  carbohydrate, linkage, sugar, Scyphozoa, nerve, Cyanea capillata (Cnidaria)

  Publication DOI: 10.1007/BF00318487
  Journal NLM ID: 0417625
  Publisher: Springer
  Institutions: Whitney Laboratory, St. Augustine, FL, USA, Department of Neuroscience, University of Florida, Gainesville, FL, USA, Department of Physiology, University of Florida, Gainesville, FL, USA
  
   
  
  Jasminum officinale, Cyanea capillata
  CSDB ID 118702 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit
Compound class: cell wall polysaccharide
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_153212,IEDB_241099,IEDB_423114,IEDB_423150,SB_74,SB_85

• Article ID: 6230
  Gannesen AV, Ziganshin RH, Zdorovenko EL, Klimko AI, Ianutsevich EA, Danilova OA, Tereshina VM, Gorbachevskii MV, Ovcharova MA, Nevolina ED, Martyanov SV, Shashkov AS, Dmitrenok AS, Novikov AA, Zhurina MV, Botchkova EA, Toukach PV, Plakunov VK "Epinephrine extensively changes the biofilm matrix composition in Micrococcus luteus C01 isolated from human skin" - Frontiers in Microbiology 13 (2022) 1003942
  

  The importance of the impact of human hormones on commensal microbiota and microbial biofilms is established in lots of studies. In the present investigation, we continued and extended the research of epinephrine effects on the skin commensal Micrococcus luteus C01 and its biofilms, and also the matrix changes during the biofilm growth. Epinephrine in concentration 4.9 × 10-9 M which is close to normal blood plasma level increased the amount of polysaccharides and extracellular DNA in the matrix, changed extensively its protein, lipid and polysaccharide composition. The Ef-Tu factor was one of the most abundant proteins in the matrix and its amount increased in the presence of the hormone. One of the glucose-mannose polysaccharide was absent in the matrix in presence of epinephrine after 24 h of incubation. The matrix phospholipids were also eradicated by the addition of the hormone. Hence, epinephrine has a great impact on the M. luteus biofilms and their matrix composition, and this fact opens wide perspectives for the future research.

  NMR, mass spectrometry, biofilms, biofilm matrix, Micrococcus luteus, epinephrine, host-microbiota interactions, human skin microbiota

  NCBI PubMed ID: 36204611
  Publication DOI: 10.3389/fmicb.2022.1003942
  Journal NLM ID: 101548977
  Publisher: Lausanne: Frontiers Research Foundation
  Correspondence: A.V. Gannesen
  Institutions: N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, Faculty of Biology, Lomonosov Moscow State University, Moscow, Russia, Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia, Winogradsky Institute of Microbiology, Federal Research Center 'Fundamentals of Biotechnology' of Russian Academy of Sciences, Moscow, Russia, Faculty of Chemical and Environmental Engineering, Gubkin University, Moscow, Russia
  Methods: 13C NMR, 1H NMR, NMR-2D, GLC, anion-exchange chromatography, Smith degradation, chemical methods, GPC, extraction, statistical analysis, biofilm assays, TEM, Orbitrap MS, surface-enhanced Raman scattering (SERS), proteomics analysis, NMR analysis by GODDESS and GRASS
  
   
  
  Micrococcus luteus C01
  CSDB ID 20941 (all data & tools)

Show legend Show as text

Structure type: homopolymer ; n is large
Trivial name: chitin
Compound class: chitin
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_153212,IEDB_241099,IEDB_423114,IEDB_423150,SB_74,SB_85

• Article ID: 6493
  Elorza MV, Sentandreu R, Ruiz-Herrera J "Isolation and characterization of yeast monomorphic mutants of Candida albicans" - Journal of Bacteriology 176 (1994) 2318-2325
  

  A method was devised for the isolation of yeast monomorphic (LEV) mutants of Candida albicans. By this procedure, about 20 stable yeast-like mutants were isolated after mutagenesis with ethyl methane sulfonate. The growth rate of the mutants in different carbon sources, both fermentable and not, was indistinguishable from that of the parental strain, but they were unable to grow as mycelial forms after application of any of the common effective inducers, i.e., heat shock, pH alterations, proline addition, or use of GlcNAc as the carbon source. Studies performed with one selected strain demonstrated that it had severe alterations in the chemical composition of the cell wall, mainly in the levels of chitin and glucans, and in specific mannoproteins, some of them recognizable by specific polyclonal and monoclonal antibodies. It is suggested that these structural alterations hinder the construction of a normal hyphal wall.

  NCBI PubMed ID: 8157600
  Journal NLM ID: 2985120R
  Publisher: American Society for Microbiology
  Institutions: Sección de Microbiología, Facultat de Farmacia, Universitat de Valencia, Spain
  Methods: SDS-PAGE, ELISA, autoradiography, immunodetection
  
   
  
  Candida albicans ATCC 26555, Candida albicans LAT1, Candida albicans LEV1, Candida albicans LEV7
  CSDB ID 131817 (all data & tools)
• Article ID: 6499
  Kreger DR "On the nature and formation of the fibrillar nets produced by protoplasts of Saccharomyces cerevisiae in liquid media: An electronmicroscopic, X-ray diffraction and chemical study" - Journal of General Microbiology 92 (1975) 207-220
  
  Journal NLM ID: 0375371
  
   
  
  Saccharomyces cerevisiae
  CSDB ID 139821 (all data & tools)
• Article ID: 6525
  Arlorio M, Ludwig A, Boller T, Bonfante P "Inhibition of fungal growth by plant chitinases and b-1,3-glucanases" - Protoplasma 171 (1992) 34-43
  
  Journal NLM ID: 9806853
  Publisher: Springer
  
   
  
  Trichoderma longibrachiatum
  CSDB ID 147987 (all data & tools)
• Article ID: 6577
  da-Silva MM, Polizeli MLTM, Jorge JA, Terenzi HF "Cell wall deficiency in 'slime' strains of Neurospora crassa: osmotic inhibition of cell wall synthesis and b-D-glucan synthase activity" - Brazilian Journal of Medical and Biological Research = Revista brasileira de pesquisas médicas e biológicas 27 (1994) 2843-2857
  

  1. The RCP-3 S/H mutant of Neurospora crassa was obtained by vegetative selection in medium of high osmolarity of a mycelial form of an fz, sg, os-1 ("slime"-like) segregant. The mutant exhibits spheroplast-hyphal dimorphism conditioned by the osmolarity of the culture medium (Pietro et al. (1990). Journal of General Microbiology, 136: 121-129). The carbohydrate composition of the cell wall of the mutant was different from that of the wild type in the absence of an alkali-soluble galactosaminoglycan polymer. Furthermore the mutant cell wall had a somewhat lower content of β-glucan relative to that of chitin. 2. Increasing concentrations of sorbitol in the culture medium of the mutant inhibited by 10-fold the formation of cell wall relative to total biomass. The cell wall of the mutant cultured in the presence of sorbitol lacked mannose- and galactose-containing polymers, and also showed progressively lower amounts of β-glucan relative to chitin. 3. The activity of membrane-bound (1-3)-β-D-glucan synthase from the mutant grown in the absence of sorbitol shared several properties with the wild type enzyme (i.e., Km app., Vmax, stability at 30 degrees C, activation by GTP gamma S, and dissociability by treatment with NaCl and Tergitol NP-40 into a membrane-bound catalytic center and a GTP-binding activating protein). On the other hand, the enzyme from the mutant but not that from the wild type was inactivated by about 15% by treatment with NaCl and detergent. 4. At high concentrations of sorbitol (1.0 M) the RCP-3 S/H mutant exclusively produced spheroplasts devoid of (1-3)-β-D-glucan synthase activity. The defect was at the level of the membrane-bound catalytic center. The activity of the GTP-binding activating factor was apparently normal in these cells. 5. These results suggest that the definitive loss of cell wall in the N. crassa "slime" RCP-3 S/H mutant was due to a defect in (1-3)-β-D-glucan synthase activity which was exaggerated in the presence of high osmolyte concentrations.

  NCBI PubMed ID: 7550004
  Journal NLM ID: 8112917
  Publisher: SP, Brasil: Associação Brasileira de Divulgação Científica
  Institutions: Departamento de Biologia, Faculdade de Filosofia, Universidade de São Paulo, Brasil
  
   
  
  Neurospora crassa RCP-3 S/H, Neurospora crassa
  CSDB ID 111874 (all data & tools)
• Article ID: 6582
  Bobichon H, Gache D, Bouchet P "Ultrarapid cryofixation of Candida albicans: Evidence for a fibrillar reticulated external layer and mannan channels within the cell wall" - Cryo Letters 15 (1994) 161-172
  
  Journal NLM ID: 9891832
  
   
  
  Candida albicans
  CSDB ID 121703 (all data & tools)
• Article ID: 6603
  Ruiz-Herrera J, Mormeneo S, Vanaclocha P, Font-de-mora J, Iranzo M, Puertes I, Sentandreu R "Structural organization of the components of the cell wall from Candida albicans" - Microbiology 140 (1994) 1513-1523
  

  The organization of the components of the cell wall from Candida albicans was studied by means of sequential treatment with hot SDS, anhydrous ethylenediamine (EDA) and lytic enzymes, followed by chemical and microscopic analyses of the different separated fractions. The EDA-insoluble fraction retained the original morphology of the wall, which was destroyed by β-glucanase, but not by chitinase treatments. Staining with fluorescent lectins revealed distinct distributions of mannoproteins, glucans and chitin in the wall. Amino acid analysis of SDS-extracted walls, and the EDA-soluble and -resistant fractions gave similar results, with seven amino acids making up about 70% of the total protein weight. Treatment of the EDA-insoluble fraction with Zymolyase or chitinase released fragments of variable size whose susceptibility to these and other hydrolases suggests that they are made of glucan, chitin and mannan oligomers associated with proteins. Treatment of the Zymolyase-insoluble residue with chitinase released a series of low-molecular-mass oligomers made of neutral sugars, GlcNAc and amino acids, mainly lysine. It is suggested that they represent fragments of the core making up the scaffold of the cell wall of the fungus.

  NCBI PubMed ID: 8075794
  Journal NLM ID: 0376646
  Publisher: Washington, DC: Kluwer Academic/Plenum Publishers
  Institutions: Departamento de Genética y Biología Molecular, Unidad Irapuato, Centro de Investigación y de Estudios Avanzados del IPN, Gto., México
  Methods: gel filtration, enzymatic digestion, light microscopy, HCl hydrolysis
  
   
  
  Candida albicans ATCC 26555
  CSDB ID 143656 (all data & tools)
• Article ID: 6623
  Hartland RP, Vermeulen CA, Klis FM, Sietsma JH, Wessels JGH "The linkage of (1-3)-b-glucan to chitin during cell wall assembly in Saccharomyces cerevisiae" - Yeast 10 (1994) 1591-1599
  

  Pulse-chase experiments with [14C]glucose demonstrated that in the cell wall of wild-type Saccharomyces cerevisiae alkali-soluble (1-3)-β-glucan serves as a precursor for alkali-insoluble (1-3)-β-glucan. The following observations support the notion that the insolubilization of the glucan is caused by linkage to chitin: (i) degradation of chitin by chitinase completely dissolved the glucan, and (ii) disruption of the gene for chitin synthase 3 prevented the formation of alkali-insoluble glucan. These cells, unable to form a glucan-chitin complex, were highly vulnerable to hypo-osmotic shock indicating that the linkage of the two polymers significantly contributes to the mechanical strength of the cell wall. Conversion of alkali-soluble glucan into alkali-insoluble glucan occurred both early and late during budding and also in the ts-mutant cdc24-1 in the absence of bud formation.

  NCBI PubMed ID: 7725794
  Publication DOI: 10.1002/yea.320101208
  Journal NLM ID: 8607637
  Publisher: Chichester, Wiley
  Institutions: Department of Plant Biology, University of Groningen, Haren, The Netherlands
  
   
  
  Saccharomyces cerevisiae
  CSDB ID 149876 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit
Trivial name: chitin
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_153212,IEDB_241099,IEDB_423114,IEDB_423150,SB_74,SB_85

• Article ID: 6776
  Chaffin WL, López-Ribot JL, Casanova M, Gozalbo D, Martínez JP "Cell wall and secreted proteins of Candida albicans: identification, function, and expression" - Microbiology and Molecular Biology Reviews: MMBR 62 (1998) 130-180
  

  The cell wall is essential to nearly every aspect of the biology and pathogenicity of Candida albicans. Although it was initially considered an almost inert cellular structure that protected the protoplast against osmotic offense, more recent studies have demonstrated that it is a dynamic organelle. The major components of the cell wall are glucan and chitin, which are associated with structural rigidity, and mannoproteins. The protein component, including both mannoprotein and nonmannoproteins, comprises some 40 or more moieties. Wall proteins may differ in their expression, secretion, or topological location within the wall structure. Proteins may be modified by glycosylation (primarily addition of mannose residues), phosphorylation, and ubiquitination. Among the secreted enzymes are those that are postulated to have substrates within the cell wall and those that find substrates in the extracellular environment. Cell wall proteins have been implicated in adhesion to host tissues and ligands. Fibrinogen, complement fragments, and several extracellular matrix components are among the host proteins bound by cell wall proteins. Proteins related to the hsp70 and hsp90 families of conserved stress proteins and some glycolytic enzyme proteins are also found in the cell wall, apparently as bona fide components. In addition, the expression of some proteins is associated with the morphological growth form of the fungus and may play a role in morphogenesis. Finally, surface mannoproteins are strong immunogens that trigger and modulate the host immune response during candidiasis

  Journal NLM ID: 9706653
  WWW link: http://mmbr.asm.org/content/62/1/130.long
  Publisher: Washington, DC: American Society for Microbiology
  Correspondence: micwlc@ttuhsc.edu
  Institutions: Department of Microbiology and Immunology, Texas Tech University Health Sciences Center, Lubbock, USA, Department of Medicine, University of Texas Health Science Center at San Antonio, San Antonio, Texas, USA, Departamento de Microbiologı́a y Ecologı́a, Facultad de Farmacia, Universitat de Valencia, Valencia, Spain
  
   
  
  Candida albicans
  CSDB ID 40760 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit
Trivial name: chitin
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_153212,IEDB_241099,IEDB_423114,IEDB_423150,SB_74,SB_85

• Article ID: 6785
  Hochstenbach F, Klis FM, van den Ende H, van Donselaar E, Peters PJ, Klausner RD "Identification of a putative alpha-glucan synthase essential for cell wall construction and morphogenesis in fission yeast" - Proceedings of the National Academy of Sciences of the USA 95 (1998) 9161-9166
  

  The cell wall protects fungi against lysis and determines their cell shape. Alpha-glucan is a major carbohydrate component of the fungal cell wall, but its function is unknown and its synthase has remained elusive. Here, we describe a fission yeast gene, ags1+, which encodes a putative alpha-glucan synthase. In contrast to the structure of other carbohydrate polymer synthases, the predicted Ags1 protein consists of two probable catalytic domains for alpha-glucan assembly, namely an intracellular domain for alpha-glucan synthesis and an extracellular domain speculated to cross-link or remodel alpha-glucan. In addition, the predicted Ags1 protein contains a multipass transmembrane domain that might contribute to transport of alpha-glucan across the membrane. Loss of Ags1p function in a temperature-sensitive mutant results in cell lysis, whereas mutant cells grown at the semipermissive temperature contain decreased levels of cell wall alpha-glucan and fail to maintain rod shapes, causing rounding of the cells. These findings demonstrate that alpha-glucan is essential for fission yeast morphogenesis.

  Journal NLM ID: 7505876
  WWW link: http://www.pnas.org/content/95/16/9161.abstract
  Publisher: National Academy of Sciences
  Correspondence: hochstenbach@bio.uva.nl
  Institutions: Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA, Institute for Molecular Cell Biology, BioCentrum Amsterdam, University of Amsterdam, Kruislaan 318, 1098 SM Amsterdam, The Netherlands, Department of Cell Biology, Faculty of Medicine and Institute of Biomembranes, Utrecht University, 3584 CX Utrecht, The Netherlands
  Methods: electron microscopy, enzymatic digestion, cloning, sequence analysis
  
   
  
  Schizosaccharomyces pombe
  CSDB ID 40800 (all data & tools)

Show legend Show as text

Structure type: homopolymer ; n=2000
Trivial name: chitin
Compound class: cell wall polysaccharide
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_153212,IEDB_241099,IEDB_423114,IEDB_423150,SB_74,SB_85

• Article ID: 6979
  Ruiz-Herrera J, Elorza MV, Valentin E, Sentandreu R "Molecular organization of the cell wall of Candida albicans and its relation to pathogenicity" - FEMS Yeast Research 6(1) (2006) 14-29
  

  Candida albicans is one of the most important opportunistic pathogenic fungi. Weakening of the defense mechanisms of the host, and the ability of the microorganism to adapt to the environment prevailing in the host tissues, turn the fungus from a rather harmless saprophyte into an aggressive pathogen. The disease, candidiasis, ranges from light superficial infections to deep processes that endanger the life of the patient. In the establishment of the pathogenic process, the cell wall of C. albicans (as in other pathogenic fungi) plays an important role. It is the outer structure that protects the fungus from the host defense mechanisms and initiates the direct contact with the host cells by adhering to their surface. The wall also contains important antigens and other compounds that affect the homeostatic equilibrium of the host in favor of the parasite. In this review, we discuss our present knowledge of the structure of the cell wall of C. albicans, the synthesis of its different components, and the mechanisms involved in their organization to give rise to a coherent composite. Furthermore, special emphasis has been placed on two further aspects: how the composition and structure of C. albicans cell wall compare with those from other fungi, and establishing the role of some specific wall components in pathogenesis. From the data presented here, it becomes clear that the composition, structure and synthesis of the cell wall of C. albicans display both subtle and important differences with the wall of different saprophytic fungi, and that some of these differences are of utmost importance for its pathogenic behavior.

  Pathogenesis, cell wall, glycoproteins, Glucans, Candida albicans, chitin

  NCBI PubMed ID: 16423067
  Publication DOI: 10.1111/j.1567-1364.2005.00017.x
  Journal NLM ID: 101085384
  Publisher: Oxford University Press
  Correspondence: Ruiz-Herrera J
  Institutions: Departamento de Ingeniería Genética, Unidad Irapuato, Centro de Investigación y de Estudios Avanzados del IPN, Irapuato, Mexico, Departament de Microbiología i Ecología, Facultat de Farmacia, Universitat de València, Burjassot, Spain
  
   
  
  Candida albicans
  CSDB ID 41831 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure ; 4300
Trivial name: polyglucosamine
Compound class: O-polysaccharide
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_153212,IEDB_241099,IEDB_423114,IEDB_423150,SB_74,SB_85

• Article ID: 7415
  Ben-Josef AM, Platt D, Zomer E "Cationic polysaccharides in the treatment of pathogenic Candida infections" - ACS Symposium Series 1102 (2012) 219-231
  

  A heat stable complex polysaccharide (molecular weight of 4300 Da) purified from the cell wall of the fungus Mucor rouxii (CPM) and a cationic polysaccharide from crab chitin (CPP) are potent antifungal agents both in vitro and in vivo. These compounds possess several highly desirable characteristics for the next generation of antifungal agents. First, being novel compounds, unrelated to the existing antifungal drugs, there is no cross resistance between the compounds and the currently used antifungal agents. Second is the importance of the rapidity of action, low MIC (Minimum Inhibitory Concentration) values and the lethal effect of these compounds against a wide spectrum of pathogenic yeasts. This will help reduce treatment duration and the development of untoward effects. Third, these compounds are heat and light-stable, making them promising to use for topical applications as was proven by the in vivo experiments with CPP. Fourth, being a large molecule with highly charged residues, these compounds are acting on external targets of the cell membrane. Thus, it is unlikely to develop resistance to CPM by the efflux mechanism that is a major cause of drug resistance in microorganisms including fungi.

  cytology, Mucor rouxii, antifungal agents, cell membranes, candidiasis

  Publication DOI: 10.1021/bk-2012-1102.ch008
  Journal NLM ID: 100961485
  Publisher: American Chemical Society
  Correspondence: zomer@galectintherapeutics.com
  Institutions: Pro-Pharmaceuticals, Newton, USA
  Methods: biological assays
  
   
  
  Mucor rouxii
  CSDB ID 44408 (all data & tools)