Show legend Show as text

Structure type: polymer chemical repeating unit
Trivial name: pustulan, β-1,6-glucan, β-(1,6)-glucan
Compound class: CPS, cell wall polysaccharide, glucan
Contained glycoepitopes: IEDB_135614,IEDB_141806,IEDB_142488,IEDB_146664,IEDB_241101,IEDB_983931,SB_192

• Article ID: 331
  Monteiro MA, Slavic D, St-Michael F, Brisson J, MacIinnes JI, Perry MB "The first description of a (1→6)-β-D-glucan in prokaryotes: (1→6)-β-D-glucan is a common component of Actinobacillus suis and is the basis for a serotyping system" - Carbohydrate Research 329(1) (2000) 121-130
  

  The chemical and antigenic properties of the cell-surface lipopolysaccharides (LPSs) and capsular polysaccharides (CPSs) of seven representative strains of Actinobacillus suis from healthy and diseased pigs were investigated. Four strains produced a linear (1→6)-β-D-glucan homopolymer, β-D-Glcp-(1-[→6)-β-D-Glcp-(1-]n →, as a LPS-O-chain (O1) and as a CPS (K1). Polyclonal antisera prepared against a (1→6)-β-D-glucan-containing strain showed a positive reaction against both LPSs and CPSs derived from the above strains (designated serotype O1/K1). One strain carried the (1→6)-β-D-glucan solely as a LPS-O-chain (serotype O1) and two strains did not express the (1→6)-β-D-glucan, but, instead, produced a different O-chain (designated serotype 02); these three strains expressed their own characteristic CPSs. (1→6)-β-D-Glucan structures are common cell wall components of yeast, fungi and lichens, but, to our knowledge, this is the first time a (1→6)-β-D-glucan has been described in a prokaryotic organism. Conformational and nuclear magnetic resonance analyses showed that the β-D-Glcp-(1→6)-β-D-Glcp linkage was flexible and two distinct glycosidic conformers are described. Cross-reactive antibodies to the A. suis (1→6)-β-D-glucan could be detected in sera from a variety of species and in sera from specific pathogen free pigs. This cross-reactivity may arise from immuno-stimulation of organisms present in the surrounding environment that contain (1→6)-β-D-glucan, which may also explain the high incidence of false positive results in previous serological tests for A. suis. In addition, these (1→6)-β-D-glucan background antibodies may be protective against A. suis infection. The characterization herein of (1→6)-β-D-glucan is the foundation for the development of a serotyping system for A. suis.

  Lipopolysaccharide, capsule, Actinobacillus suis, serotyping system, (1-6)-b-D-Glucan

  NCBI PubMed ID: 11086692
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: mario.monteiro@nrc.ca
  Institutions: Institute for Biological Sciences, National Research Council, 100 Sussex Dri6e, Ottawa, Ont., Canada K1A 0R6, Department of Pathobiology, Uni6ersity of Guelph, Guelph, Ont., Canada N1G 2W 1
  Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, sugar analysis, conformation analysis, GLC
  
   
  
  Actinobacillus suis O1
  CSDB ID 7724 (all data & tools)
• Article ID: 382
  Slavic D, Toffner TL, Monteiro MA, Perry MB, MacIinnes JI "Prevalence of O1/K1- and O2/K3-reactive Actinobacillus suis in healthy and diseased swine" - Journal of Clinical Microbiology 38(10) (2000) 3759-3762
  

  A cell surface antigen-typing system was devised for the swine pathogen Actinobacillus suis and used to examine the prevalence of different lipopolysaccharide (O) types in healthy and diseased pigs. The strains examined in this study were isolated from a variety of locations in Canada and from Kansas. Lipopolysaccharide preparations of 151 isolates of A. suis were characterized by immunoblotting using polyclonal antisera generated to strains SO4 (O1/K1), H89-1173 (O2/K3), and VSB 3714, a rough strain. Approximately 54% (62 of 114) of A. suis isolates from diseased pigs, all (11 of 11) isolates from healthy pigs, and all (4 of 4) reference strains reacted with O1/K1 antiserum. More than 80% (18 of 22) of A. suis strains used for bacterin production and approximately 41% (47 of 114) of isolates from diseased pigs bound O2/K3 antiserum. One isolate appeared to be rough, and five were untypeable. O1/K1- and O2/K3-reactive strains were equally prevalent in Kansas, whereas O2/K3-reactive strains were more common in Quebec and western Canada and O1/K1 strains were most common in Ontario. The fact that virtually all of the strains submitted for bacterin production were O2/K3-reactive strains is consistent with the notion that these strains may be more virulent than O1/K1 strains; alternatively, this may reflect geographic or other biases. In addition, we observed cross-reactivity between A. suis cell surface antigens and swine antisera to several other important pathogens. This finding may explain why previous attempts to develop a simple serodiagnostic test for A. suis have been unsuccessful.

  serotype, Actinobacillus suis, Actinobacillus, Prevalence

  NCBI PubMed ID: 11015398
  Journal NLM ID: 7505564
  Publisher: American Society for Microbiology
  Correspondence: macinnes@uoguelph.ca
  Institutions: Department of Pathobiology, University of Guelph, Guelph, Ontario, Canada N1G 2W1, Institute for Biological Sciences, National Research Council, Ottawa, Ontario, Canada K1A 0R6
  Methods: serological methods
  
   
  
  Actinobacillus suis
  CSDB ID 8325 (all data & tools)
• Article ID: 7001
  Latge JP, Mouyna I, Tekaia F, Beauvais A, Debeaupuis JP, Nierman W "Specific molecular features in the organization and biosynthesis of the cell wall of Aspergillus fumigatus" - Medical Mycology (2005) S15-S22
  

  The cell wall of Aspergillus fumigatus is composed of a branched PI,3 glucan covalently bound to chitin, β-1,3, β-1,4 glucans, and galactomannan, that is embedded in an amorphous cement composed of α-1,3 glucan, galactomannan and polygalactosamin. The mycelial cell wall of A. fumigatus is very different from the yeast Saccharomyces cerevisiae cell wall, and in particular lacks 01,6 glucans and proteins covalently bound to cell wall polysaccharides. The differences in cell wall composition between the mould A. fumigatus and the yeast S. cerevisiae are also reflected at the genomic level where unique features have been identified in A. fumigatus. A single gene codes for the glucan synthase catalytic subumit; this finding has lead to the development of a RNAi methodology for the disruption of essential genes in A. fumigatus. In contrast to the glucan synthase, multiple genes have been found in the chitin synthase and the α-glucan synthase families; in spite of homologous sequences, each gene in each family have very different function. Similarly homologous mannosyltransferase genes are found in yeast and moulds but they lead to the synthesis of very different N-mannan structures. This chemo-genomic comparative analysis has also suggested that GPI-anchored proteins do not have a role of linker in the three dimensional organization of the fungal cell wall.

  cell wall, mannan, glucan, GPI, chitin

  Publication DOI: 10.1080/13693780400029155
  Journal NLM ID: 9815835
  Publisher: Oxford: Oxford University Press
  Correspondence: jplatge@pasteur.fr
  Institutions: Le Reseau International des Instituts Pasteur (RIIP), Aspergillus Unit, 25 Rue Dr Roux, F-75724 Paris, France, The Institute for Genomic Research, Rockville, MD, USA
  
   
  
  Saccharomyces cerevisiae
  CSDB ID 42140 (all data & tools)
• Article ID: 7333
  Tanabe Y, Oda M "Molecular characterization of endo-1,3-β-glucanase from Cellulosimicrobium cellulans: effects of carbohydrate-binding module on enzymatic function and stability" - Biochimica et Biophysica Acta 1814(12) (2011) 1713-1719
  

  An endo-1,3-β-glucanase was purified from Tunicase®, a crude enzyme preparation from Cellulosimicrobium cellulans DK-1, and determined to be a 383-residue protein (Ala1-Leu383), comprising a catalytic domain of the glycoside hydrolase family 16 and a C-terminal carbohydrate-binding module family 13. The Escherichia coli expression system of the catalytic domain (Ala1-Thr256) was constructed, and the protein with N-terminal polyhistidine tag was purified using a Ni-nitrilotriacetic acid column. We analyzed enzymatic properties of the recombinant catalytic domain, its variants, and the Tunicase®-derived full-length endo-1,3-β-glucanase. Substitution of Glu119 with Ala and deletion of Met123, both of the residues are located in the catalytic motif, resulted in the loss of hydrolytic activity. In comparison between the full-length enzyme and isolated catalytic domain, their hydrolytic activities for soluble substrates such as laminarin and laminarioligosaccharides were similar. In contrast, the hydrolytic activity of the full-length enzyme for insoluble substrates such as curdlan and yeast-glucan was significantly higher than that of the catalytic domain. It should be noted that the acid stabilities for the hydrolysis of laminarin were clearly different. Secondary structure analysis using circular dichroism showed that the full-length enzyme was more acid stable than was the catalytic domain, possibly because of domain interactions between the catalytic domain and the carbohydrate-binding module.

  Catalytic Domain, β-1, Carbohydrate-binding module, Enzymatic activity, 3 glucan, Acid tolerance

  NCBI PubMed ID: 21979581
  Publication DOI: 10.1016/j.bbapap.2011.09.004
  Journal NLM ID: 0217513
  Publisher: Elsevier
  Correspondence: Oda M
  Institutions: Graduate School of Life and Environmental Sciences, Kyoto Prefectural University, Kyoto, Japan
  Methods: enzymatic activity assay
  
   
  
  Umbilicaria papulosa
  CSDB ID 45578 (all data & tools)
• Article ID: 7911
  Bzducha-Wróbel A, Kieliszek M, Błażejak S "Chemical composition of the cell wall of probiotic and brewer’s yeast in response to cultivation medium with glycerol as a carbon source" - European Food Research and Technology 237(4) (2013) 489-499
  

  The structure of cell wall of yeasts (genus Saccharomyces) is one of the factors that determine their health-promoting properties connected to the presence of b-glucans and mannoprotein. The aim of the study was to determine the influence of glycerol as a carbon source on structural polymers of cell wall (b-glucan and mannoprotein) of probiotic yeasts Saccharomyces cerevisiae var. boulardii and brewer’s yeasts S. cerevisiae R9. Significant increase of the percentage of polysaccharide content in the cell wall dry weight of S. cerevisiae R9 brewer’s yeasts was noted (in the range of 10–20 %) after cultivation in medium containing glycerol at a concentration of 2–5 % and pH 4.0. The highest content of carbohydrates in probiotic yeasts’ cell wall (58 %) was observed after cultivation in medium containing 3 % of glycerol and pH 5.0. The cell wall of probiotic yeasts was characterized by higher content of mannoprotein comparing with cell wall preparation of brewer’s yeasts S. cerevisiae R9 composed mainly of b-glucans. After cultivation in mediums with 2 and 3 % of glycerol, the cell of brewer’s yeasts contained the highest amount of b(1,3/1,6)-glucan in dry weight of the cell wall (about 36 %). Glycerol at a concentration of 3 and 5 % also intensified mannoprotein biosynthesis in cell wall of S. cerevisiae R9, approximating their content to those noted in the cells of probiotic yeasts (about 29 % (w/w) of dry weight of the cell wall) after cultivation in a medium of pH 5.0 containing 3 % of glycerol.

  cell wall, β-glucan, Saccharomyces cerevisiae, mannoprotein, probiotic yeast

  Publication DOI: 10.1007/s00217-013-2016-8
  Journal NLM ID: 100957634
  Publisher: Berlin: Springer
  Correspondence: anna_bzducha_wrobel@sggw.pl
  Institutions: Department of Biotechnology, Microbiology and Food Evaluation, Faculty of Food Sciences, Warsaw University of Life Sciences - SGGW, Warsaw, Poland
  Methods: enzymatic hydrolysis, statistical analysis, hydrolysis, dialysis, autolysis
  
   
  
  Saccharomyces cerevisiae R9, Saccharomyces cerevisiae var. boulardii
  CSDB ID 44888 (all data & tools)
• Article ID: 7930
  Cabib E, Arroyo J "How carbohydrates sculpt cells: chemical control of morphogenesis in the yeast cell wall" - Nature Reviews Microbiology 11(9) (2013) 648-655
  

  In budding yeast, the neck that connects the mother and daughter cell is the site of essential functions such as organelle trafficking, septum formation and cytokinesis. Therefore, the morphology of this region, which depends on the surrounding cell wall, must be maintained throughout the cell cycle. Growth at the neck is prevented, redundantly, by a septin ring inside the cell membrane and a chitin ring in the cell wall. Here, we describe recent work supporting the hypothesis that attachment of the chitin ring, which forms at the mother–bud neck during budding, to β-1,3-glucan in the cell wall is necessary to stop growth at the neck. Thus, in this scenario, chemistry controls morphogenesis.

  NCBI PubMed ID: 23949603
  Publication DOI: 10.1038/nrmicro3090
  Journal NLM ID: 101190261
  Publisher: London, UK: Nature Publishing Group
  Correspondence: Cabib E
  Institutions: Laboratory of Biochemistry and Genetics, National institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Department of Health and Human Services, Bethesda, USA, the Departamento de Microbiología II, Facultad de Farmacia, Universidad Complutense de Madrid and Instituto Ramón y Cajal de Investigaciones Sanitarias, Madrid, Spain
  
   
  
  Saccharomyces cerevisiae
  CSDB ID 44927 (all data & tools)
• Article ID: 7932
  de Groot PW, Bader O, de Boer AD, Weig M, Chauhan N "Adhesins in human fungal pathogens: glue with plenty of stick" - Eukaryotic Cell 12(4) (2013) 470-481
  

  Understanding the pathogenesis of an infectious disease is critical for developing new methods to prevent infection and diagnose or cure disease. Adherence of microorganisms to host tissue is a prerequisite for tissue invasion and infection. Fungal cell wall adhesins involved in adherence to host tissue or abiotic medical devices are critical for colonization leading to invasion and damage of host tissue. Here, with a main focus on pathogenic Candida species, we summarize recent progress made in the field of adhesins in human fungal pathogens and underscore the importance of these proteins in establishment of fungal diseases.

  NCBI PubMed ID: 23397570
  Publication DOI: 10.1128/EC.00364-12
  Journal NLM ID: 101130731
  Publisher: American Society for Microbiology
  Correspondence: chauhan1@umdnj.edu
  Institutions: Regional Center for Biomedical Research, Albacete Science and Technology Park, University of Castilla—La Mancha, Albacete, Spaina, Institute for Medical Microbiology and German National Reference Center for Systemic Mycoses, University Medical Center Göttingen, Göttingen, Germany, Public Health Research Institutec and Department of Microbiology and Molecular Genetics, New Jersey Medical School, University of Medicine and Dentistry of New Jersey, Newark, New Jersey, USA
  
   
  
  Candida
  CSDB ID 44939 (all data & tools)
• Article ID: 8094
  Ao J, Chinnici JL, Maddi A, Free SJ "The N-linked outer chain mannans and the Dfg5p and Dcw1p endo-α-1,6-mannanases are needed for incorporation of Candida albicans glycoproteins into the cell wall" - Eukaryotic Cell 14(8) (2015) 792-903
  

  A biochemical pathway for the incorporation of cell wall protein into the cell wall of Neurospora crassa was recently proposed. In this pathway, the DFG-5 and DCW-1 endo-α-1,6-mannanases function to covalently cross-link cell wall protein-associated N-linked galactomannans, which are structurally related to the yeast outer chain mannans, into the cell wall glucan-chitin matrix. In this report, we demonstrate that the mannosyltransferase enzyme Och1p, which is needed for the synthesis of the N-linked outer chain mannan, is essential for the incorporation of cell wall glycoproteins into the Candida albicans cell wall. Using endoglycosidases, we show that C. albicans cell wall proteins are cross-linked into the cell wall via their N-linked outer chain mannans. We further demonstrate that the Dfg5p and Dcw1p α-1,6-mannanases are needed for the incorporation of cell wall glycoproteins into the C. albicans cell wall. Our results support the hypothesis that the Dfg5p and Dcw1p α-1,6-mannanases incorporate cell wall glycoproteins into the C. albicans cell wall by cross-linking outer chain mannans into the cell wall glucan-chitin matrix.

  cell wall, mannan, N-glycans, endo-mannanases

  NCBI PubMed ID: 26048011
  Publication DOI: 10.1128/EC.00032-154
  Journal NLM ID: 101130731
  Publisher: American Society for Microbiology
  Correspondence: free@buffalo.edu
  Institutions: Department of Biological Sciences, SUNY University at Buffalo, Buffalo, NY, USA, School of Dental Medicine, Periodontics and Endodontics, SUNY University at Buffalo Dental School, Buffalo, NY, USA
  
   
  
  Candida albicans, Saccharomyces cerevisiae
  CSDB ID 42316 (all data & tools)
• Article ID: 8097
  Blanco N, Sanz AB, Rodríguez-Peña JM, Nombela C, Farkaš V, Hurtado-Guerrero R, Arroyo J "Structural and functional analysis of yeast Crh1 and Crh2 transglycosylases" - FEBS Journal 282(4) (2015) 715-731
  

  Covalent cross-links between chitin and glucan at the yeast cell wall are created by the transglycosylase activity of redundant proteins Crh1 and Crh2, with cleavage of β-1,4 linkages of the chitin backbone and transfer of the generated molecule containing newly created reducing end onto the glucan acceptor. A three-dimensional structure of Crh1 was generated by homology modeling based on the crystal structure of bacterial 1,3-1,4-β-D-glucanase, followed by site-directed mutagenesis to obtain molecular insights into how these enzymes achieve catalysis. The residues of both proteins that are involved in their catalytic and binding activities have been characterized by measuring the ability of yeast cells expressing different versions of these proteins to transglycosylate oligosaccharides derived from β-1,3-glucan, β-1,6-glucan and chitin to the chitin at the cell wall. Within the catalytic site, residues E134 and E138 of Crh1, as well as E166 and E170 of Crh2, corresponding to the nucleophile and general acid/base, and also the auxiliary D136 and D168 of Crh1 and Crh2, respectively, are shown to be essential for catalysis. Mutations of aromatic residues F152, Y160 and W219, located within the carbohydrate-binding cleft of the Crh1 model, also affect the transglycosylase activity. Unlike Crh1, Crh2 contains a putative carbohydrate-binding module (CBM18) of unknown function. Modeling and functional analysis of site-directed mutant residues of this CBM identified essential amino acids for protein folding and stability, as well as residues that tune the catalytic activity of Crh2.

  cell wall, glucan, glycoside hydrolase, chitin, transglycosylation, computer modelling, carbohydrate binding module

  NCBI PubMed ID: 25495733
  Publication DOI: 10.1111/febs.13176
  Journal NLM ID: 101229646
  Publisher: Blackwell Publishing
  Correspondence: Arroyo J ; Hurtado-Guerrero R
  Institutions: Departamento de Microbiología II, Facultad de Farmacia, Universidad Complutense de Madrid, IRYCIS, Madrid, Spain, Institute of Chemistry, Center for Glycomics, Department of Glycobiology, Slovak Academy of Sciences, Bratislava, Slovakia, Institute of Biocomputation and Physics of Complex Systems (BIFI), University of Zaragoza, Zaragoza, Spain, BIFI-IQFR (CSIC), Zaragoza, Spain, Fundacion ARAID, Zaragoza, Spain
  
   
  
  Saccharomyces cerevisiae
  CSDB ID 42327 (all data & tools)
• Article ID: 8111
  Ene IV, Walker LA, Schiavone M, Lee KK, Martin-Yken H, Dague E, Gow NA, Munro CA, Brown AJ "Cell wall remodeling enzymes modulate fungal cell wall elasticity and osmotic stress resistance" - mBio 6(4) (2015) e00986 (1-15)
  

  The fungal cell wall confers cell morphology and protection against environmental insults. For fungal pathogens, the cell wall is a key immunological modulator and an ideal therapeutic target. Yeast cell walls possess an inner matrix of interlinked β-glucan and chitin that is thought to provide tensile strength and rigidity. Yeast cells remodel their walls over time in response to environmental change, a process controlled by evolutionarily conserved stress (Hog1) and cell integrity (Mkc1, Cek1) signaling pathways. These mitogen-activated protein kinase (MAPK) pathways modulate cell wall gene expression, leading to the construction of a new, modified cell wall. We show that the cell wall is not rigid but elastic, displaying rapid structural realignments that impact survival following osmotic shock. Lactate-grown Candida albicans cells are more resistant to hyperosmotic shock than glucose-grown cells. We show that this elevated resistance is not dependent on Hog1 or Mkc1 signaling and that most cell death occurs within 10 min of osmotic shock. Sudden decreases in cell volume drive rapid increases in cell wall thickness. The elevated stress resistance of lactate-grown cells correlates with reduced cell wall elasticity, reflected in slower changes in cell volume following hyperosmotic shock. The cell wall elasticity of lactate-grown cells is increased by a triple mutation that inactivates the Crh family of cell wall cross-linking enzymes, leading to increased sensitivity to hyperosmotic shock. Overexpressing Crh family members in glucose-grown cells reduces cell wall elasticity, providing partial protection against hyperosmotic shock. These changes correlate with structural realignment of the cell wall and with the ability of cells to withstand osmotic shock.

  cell wall, glycosyltransferases, Microscopy

  NCBI PubMed ID: 26220968
  Publication DOI: 10.1128/mBio.00986-15
  Journal NLM ID: 101519231
  Publisher: Washington, DC: American Society for Microbiology
  Correspondence: al.brown@abdn.ac.uk
  Institutions: Université de Toulouse, CNRS, UMR5504, Toulouse, France, School of Medical Sciences, University of Aberdeen, Institute of Medical Sciences, Aberdeen, UK, INSA, UPS, INP, LISBP, Toulouse, France, INRA, UMR792 Ingénierie des Systèmes Biologiques et des Procédés, Toulouse, France, CNRS, LAAS, Toulouse, France, Université de Toulouse, LAAS, Toulouse, France, School of Medical Sciences, University of Aberdeen, Institute of Medical Sciences, Foresterhill, Aberdeen, United Kingdom
  Methods: AFM, HPF-TEM
  
   
  
  Candida albicans
  CSDB ID 48507 (all data & tools)
• Article ID: 8118
  Fesel PH, Zuccaro A "β-glucan: Crucial component of the fungal cell wall and elusive MAMP in plants" - Fungal Genetics and Biology 90 (2016) 53-60
  

  Plant innate immunity relies in first place on the detection of invading microbes. Thus, plants evolved receptors to sense unique molecules of the microbe, the so called microbe-associated molecular patterns or MAMPs. The best studied fungal MAMP is chitin, an important structural building block of the fungal cell wall. Over the past years several plant receptors for chitin have been characterized as well as different strategies adopted by fungi to evade chitin recognition. Despite its strong activity as an elicitor of plant defense chitin represents only a small percentage of the cell wall of most fungi compared to other complex sugars. β-glucan, the most abundant fungal cell wall polysaccharide, also serves as a MAMP, but the mechanisms of β-glucan perception and signaling in plants are largely unknown. In contrast to that the β-glucan recognition and signaling machineries are well characterized in mammals. The C-type lectin receptor Dectin-1 is a key component of these machineries. In this review we describe valuable knowledge about the existence of at least one β-glucan receptor in plants and about the hindrances in β-glucan research. Additionally we discuss possible future perspectives of glucan research and the possibility to transfer the gathered knowledge from mammalian systems to plants.

  β-glucan, chitin, Dectin-1, fungal MAMPs, pattern recognition receptor, plant immune system

  NCBI PubMed ID: 26688467
  Publication DOI: 10.1016/j.fgb.2015.12.004
  Journal NLM ID: 9607601
  Publisher: Orlando, FL : Academic Press / Elsevier
  Correspondence: azuccaro@uni-koeln.de
  Institutions: Botanical Institute, Cluster of Excellence on Plant Sciences (CEPLAS), University of Cologne, Cologne, Germany
  
   
  
  (fungi), Phytophthora, Pythium
  CSDB ID 42402 (all data & tools)
• Article ID: 8570
  Komath SS, Singh SL, Pratyusha VA, Sah SK "Generating anchors only to lose them: The unusual story of glycosylphosphatidylinositol anchor biosynthesis and remodeling in yeast and fungi" - International Union of Biochemistry and Molecular Biology life 70(5) (2018) 355-383
  

  Glycosylphosphatidylinositol (GPI)-anchored proteins (GPI-APs) are present ubiquitously at the cell surface in all eukaryotes. They play a crucial role in the interaction of the cell with its external environment, allowing the cell to receive signals, respond to challenges, and mediate adhesion. In yeast and fungi, they also participate in the structural integrity of the cell wall and are often essential for survival. Roughly four decades after the discovery of the first GPI-APs, this review provides an overview of the insights gained from studies of the GPI biosynthetic pathway and the future challenges in the field. In particular, we focus on the biosynthetic pathway in Saccharomyces cerevisiae, which has for long been studied as a model organism. Where available, we also provide information about the GPI biosynthetic steps in other yeast/ fungi. Although the core structure of the GPI anchor is conserved across organisms, several variations are built into the biosynthetic pathway. The present Review specifically highlights these variations and their implications. There is growing evidence to suggest that several phenotypes are common to GPI deficiency and should be expected in GPI biosynthetic mutants. However, it appears that several phenotypes are unique to a specific step in the pathway and may even be species-specific. These could suggest the points at which the GPI biosynthetic pathway intersects with other important cellular pathways and could be points of regulation. They could be of particular significance in the study of pathogenic fungi and in identification of new and specific antifungal drugs/ drug targets.

  cell wall, Candida albicans, Saccharomyces cerevisiae, GPI anchor biosynthesis, antifungal drug target

  NCBI PubMed ID: 29679465
  Publication DOI: 10.1002/iub.1734
  Journal NLM ID: 100888706
  Publisher: London; Philadelphia, PA: International Union of Biochemistry and Molecular Biology by Taylor & Francis
  Correspondence: Komath SS ; Komath SS
  Institutions: School of Life Sciences, Jawaharlal Nehru University, New Delhi, India
  
   
  
  Saccharomyces cerevisiae, Aspergillus fumigatus
  CSDB ID 48753 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130650,IEDB_136044,IEDB_137472,IEDB_137779,IEDB_138949,IEDB_139428,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_7,SB_88

• Article ID: 4025
  Ganeshapillai J, Boncheff AG, Slavic D, Macinnes J, Monteiro MA "The lipopolysaccharide core of Actinobacillus suis and its relationship to those of Actinobacillus pleuropneumoniae" - Biochemistry and Cell Biology 89(3) (2011) 351-358
  

  The Gram-negative bacteria Actinobacillus suis colonizes the upper respiratory and genital tracts of swine. Along with capsular polysaccharides, lipopolysaccharides (O-chain→core→lipid A~cell) are a main cell-surface component of A. suis. In this study, we determined that A. suis lipopolysaccharide incorporates a conserved core that shares some structural features with several core types of A. pleuropneumoniae . These common core structural features likely account for the observed serological cross-reactivity between A. suis and A. pleuropneumoniae, and the data suggest that the structural epitopes responsible for immunogenicity are those in the outer core domain.

  Lipopolysaccharide, core, Actinobacillus suis, Actinobacillus pleuropneumoniae

  NCBI PubMed ID: 21639829
  Publication DOI: 10.1139/o11-003
  Journal NLM ID: 8606068
  Publisher: Ottawa: National Research Council of Canada
  Correspondence: M.A. Monteiro
  Institutions: Department of Chemistry, University of Guelph, Canada
  Methods: 13C NMR, 1H NMR, NMR-2D, sugar analysis, ESI-MS, MS/MS, NMR-1D, immunoblotting
  
   
  
  Actinobacillus suis
  CSDB ID 26206 (all data & tools)