Show legend Show as text

Structure type: structural motif or average structure
Contained glycoepitopes: IEDB_115576,IEDB_128161,IEDB_130701,IEDB_133966,IEDB_134620,IEDB_134621,IEDB_135614,IEDB_136095,IEDB_136104,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_1394182,IEDB_1397514,IEDB_140116,IEDB_140628,IEDB_140629,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141806,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_142357,IEDB_142488,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_144998,IEDB_146664,IEDB_147452,IEDB_147453,IEDB_147454,IEDB_149137,IEDB_149176,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_153543,IEDB_153755,IEDB_153756,IEDB_1539315,IEDB_158538,IEDB_158555,IEDB_161166,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164479,IEDB_164480,IEDB_174840,IEDB_190606,IEDB_232584,IEDB_232585,IEDB_241101,IEDB_420417,IEDB_420418,IEDB_420419,IEDB_420420,IEDB_420421,IEDB_423115,IEDB_558866,IEDB_558867,IEDB_558868,IEDB_558869,IEDB_742521,IEDB_76933,IEDB_857742,IEDB_857743,IEDB_885812,IEDB_983930,IEDB_983931,SB_136,SB_191,SB_192,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72,SB_77

• Article ID: 6749
  Fontaine T, Simenel C, Dubreucq G, Adam O, Delepierre M, Lemoine J, Vorgias CE, Diaquin M, Latge JP "Molecular organization of the alkali-insoluble fraction of Aspergillus fumigatus cell wall" - Journal of Biological Chemistry 275 (2000) 27594-27607
  

  Physical and biological properties of the fungal cell wall are determined by the composition and arrangement of the structural polysaccharides. Cell wall polymers of fungi are classically divided into two groups depending on their solubility in hot alkali. We have analyzed the alkali-insoluble fraction of the Aspergillus fumigatus cell wall, which is the fraction believed to be responsible for fungal cell wall rigidity. Using enzymatic digestions with recombinant endo-β-1,3-glucanase and chitinase, fractionation by gel filtration, affinity chromatography with immobilized lectins, and high performance liquid chromatography, several fractions that contained specific interpolysaccharide covalent linkages were isolated. Unique features of the A. fumigatuscell wall are (i) the absence of β-1,6-glucan and (ii) the presence of a linear β-1,3/1,4-glucan, never previously described in fungi. Galactomannan, chitin, and β-1,3-glucan were also found in the alkali-insoluble fraction. The β-1,3-glucan is a branched polymer with 4% of β-1,6 branch points. Chitin, galactomannan, and the linear β-1,3/1,4-glucan were covalently linked to the nonreducing end of β-1,3-glucan side chains. As in Saccharomyces cerevisiae, chitin was linked via a β-1,4 linkage to β-1,3-glucan. The data obtained suggested that the branching of β-1,3-glucan is an early event in the construction of the cell wall, resulting in an increase of potential acceptor sites for chitin, galactomannan, and the linear β-1,3/1,4-glucan.

  Publication DOI: 10.1074/jbc.M909975199
  Journal NLM ID: 2985121R
  WWW link: http://www.jbc.org/content/275/36/27594.abstract
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: tfontain@pasteur.fr
  Institutions: Laboratoire des Aspergillus, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris cedex 15, France, Laboratoire de Résonance Magnétique Nucléaire, Institut Pasteur, 28 rue du Docteur Roux, 75724 Paris cedex 15, France, Laboratoire de Chimie Biologique, Universitédes Sciences et Technologie de Lille Flandres-Artois 59655 Villeneuve d'Ascq cedex, France, University of Athens, Department of Biology, Division of Biochemistry and Molecular Biology GR-15701, Athens, Greece
  Methods: gel filtration, 13C NMR, 1H NMR, GLC-MS, acid hydrolysis, GLC, mild acid hydrolysis, HPAEC, enzymatic digestion, 15N NMR, acetolysis, TOCSY, methylation analysis, DQF-COSY, MALDI-TOF-MS, phenol-sulfuric acid procedure, Johnson procedure, lectin affinity chromatography, gHSQC-TOCSY
  
   
  
  Aspergillus fumigatus CBS 144-89
  CSDB ID 40488 (all data & tools)
• Article ID: 6762
  Bernard M, Latge JP "Aspergillus fumigatus cell wall: composition and biosynthesis" - Medical Mycology 39 (2001) 9-17
  

  Analysis of the cell wall of Aspergillus fumigatus is guided by obvious biological reasons: the cell wall protects the fungus against the aggressive human defense reactions, it harbours most of the fungal antigens and it represents a potential drug target. This review will discuss our current understanding of the structural organization of the polysaccharides constitutive of the cell wall of A. fumigatus [α and β(1,3)-glucans, chitin, galactomannan, and β(1,3),(1,4)-glucan] and of the enzymes (synthases, transglycosidases, and glycosyl hydrolases) responsible for their biosynthesis and remodelling. Comparative analysis of the cell wall of the conidium and mycelium also provides insights on their respective roles during the pathogenic life of this fungal species.

  transferase, cell wall, synthase, hydrolase, Aspergillus fumigatus, conidium, mycelium

  Publication DOI: 10.1080/mmy.39.1.9.17
  Journal NLM ID: 9815835
  Publisher: Oxford: Oxford University Press
  Correspondence: jplatge@pasteur.fr
  Institutions: Unité des Aspergillus, Institut Pasteur, Paris, France
  
   
  
  Aspergillus fumigatus
  CSDB ID 40511 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_115576,IEDB_130701,IEDB_134620,IEDB_136095,IEDB_136104,IEDB_137472,IEDB_1394182,IEDB_1397514,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_142488,IEDB_143632,IEDB_144983,IEDB_146664,IEDB_147454,IEDB_152206,IEDB_153220,IEDB_153543,IEDB_153756,IEDB_153762,IEDB_153763,IEDB_158555,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164480,IEDB_174840,IEDB_190606,IEDB_241100,IEDB_76933,IEDB_983930,IEDB_983931,SB_136,SB_191,SB_192,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72,SB_77

• Article ID: 6749
  Fontaine T, Simenel C, Dubreucq G, Adam O, Delepierre M, Lemoine J, Vorgias CE, Diaquin M, Latge JP "Molecular organization of the alkali-insoluble fraction of Aspergillus fumigatus cell wall" - Journal of Biological Chemistry 275 (2000) 27594-27607
  

  Physical and biological properties of the fungal cell wall are determined by the composition and arrangement of the structural polysaccharides. Cell wall polymers of fungi are classically divided into two groups depending on their solubility in hot alkali. We have analyzed the alkali-insoluble fraction of the Aspergillus fumigatus cell wall, which is the fraction believed to be responsible for fungal cell wall rigidity. Using enzymatic digestions with recombinant endo-β-1,3-glucanase and chitinase, fractionation by gel filtration, affinity chromatography with immobilized lectins, and high performance liquid chromatography, several fractions that contained specific interpolysaccharide covalent linkages were isolated. Unique features of the A. fumigatuscell wall are (i) the absence of β-1,6-glucan and (ii) the presence of a linear β-1,3/1,4-glucan, never previously described in fungi. Galactomannan, chitin, and β-1,3-glucan were also found in the alkali-insoluble fraction. The β-1,3-glucan is a branched polymer with 4% of β-1,6 branch points. Chitin, galactomannan, and the linear β-1,3/1,4-glucan were covalently linked to the nonreducing end of β-1,3-glucan side chains. As in Saccharomyces cerevisiae, chitin was linked via a β-1,4 linkage to β-1,3-glucan. The data obtained suggested that the branching of β-1,3-glucan is an early event in the construction of the cell wall, resulting in an increase of potential acceptor sites for chitin, galactomannan, and the linear β-1,3/1,4-glucan.

  Publication DOI: 10.1074/jbc.M909975199
  Journal NLM ID: 2985121R
  WWW link: http://www.jbc.org/content/275/36/27594.abstract
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: tfontain@pasteur.fr
  Institutions: Laboratoire des Aspergillus, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris cedex 15, France, Laboratoire de Résonance Magnétique Nucléaire, Institut Pasteur, 28 rue du Docteur Roux, 75724 Paris cedex 15, France, Laboratoire de Chimie Biologique, Universitédes Sciences et Technologie de Lille Flandres-Artois 59655 Villeneuve d'Ascq cedex, France, University of Athens, Department of Biology, Division of Biochemistry and Molecular Biology GR-15701, Athens, Greece
  Methods: gel filtration, 13C NMR, 1H NMR, GLC-MS, acid hydrolysis, GLC, mild acid hydrolysis, HPAEC, enzymatic digestion, 15N NMR, acetolysis, TOCSY, methylation analysis, DQF-COSY, MALDI-TOF-MS, phenol-sulfuric acid procedure, Johnson procedure, lectin affinity chromatography, gHSQC-TOCSY
  
   
  
  Aspergillus fumigatus CBS 144-89
  CSDB ID 40706 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: cell wall polysaccharide
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_137472,IEDB_141793,IEDB_144983,IEDB_147452,IEDB_147454,IEDB_152206,IEDB_153220,IEDB_190606,IEDB_885812,IEDB_983930,SB_198,SB_44,SB_67,SB_72

• Article ID: 6813
  Fu M, Zhang G, Ning J "First synthesis of the immunodominant β-galactofuranose-containing tetrasaccharide present in the cell wall of Aspergillus fumigatus" - Carbohydrate Research 340(1) (2005) 25-30
  

  beta-Galf-(1-->5)-beta-Galf-(1-->6)-alpha-Manp-(1-->6)-alpha-Manp, the immunodominant epitope in the cell-wall galactomannan of Aspergillus fumigatus, was synthesized for the first time as its allyl glycoside. The key disaccharide glycosyl donor, 2,3,5,6-tetra-O-benzoyl-beta-D-galactofuranosyl-(1-->5)-2-O-acetyl-3,6-di-O-benzoyl-beta-D-galactofuranosyl trichloroacetimidate (10), was constructed by 5-O-glycosylation of 1,2-O-isopropylidene-3,6-di-O-benzoyl-alpha-D-galactofuranose (4) with 2,3,5,6-tetra-O-benzoyl-beta-D-galactofuranosyl trichloroacetimidate (5), followed by 1,2-O-deacetonation, acetylation, selective 1-O-deacetylation, and trichloroacetimidation. The target tetrasaccharide 16 was obtained by the condensation of allyl 2,3,4-tri-O-benzoyl-alpha-D-mannopyranosyl-(1-->6)-2,3,4-tri-O-benzoyl-alpha-D-mannopyranoside (14) as glycosyl acceptor with the disaccharide glycosyl donor 10, followed by deprotection.

  synthesis, oligosaccharide, galactofuranose

  NCBI PubMed ID: 15620663
  Publication DOI: 10.1016/j.carres.2004.10.019
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: jning@mail.rcees.ac.cn
  Institutions: Research Center for Eco-Environmental Sciences, Chinese Academy of Sciences, PO Box 2871, Beijing 100085, China
  Methods: 13C NMR, 1H NMR, TLC, ESI-MS, chemical synthesis, chemical methods, UV, glycosylation
  
   
  
  Aspergillus fumigatus
  CSDB ID 41243 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit ; n>10
Trivial name: galactomannan
Compound class: cell wall polysaccharide
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_136104,IEDB_137472,IEDB_140116,IEDB_141793,IEDB_141795,IEDB_141829,IEDB_141830,IEDB_141832,IEDB_141833,IEDB_143632,IEDB_144983,IEDB_147452,IEDB_147454,IEDB_152206,IEDB_153220,IEDB_164480,IEDB_190606,IEDB_76933,IEDB_885812,IEDB_983930,SB_136,SB_191,SB_196,SB_198,SB_44,SB_67,SB_72

• Article ID: 6813
  Fu M, Zhang G, Ning J "First synthesis of the immunodominant β-galactofuranose-containing tetrasaccharide present in the cell wall of Aspergillus fumigatus" - Carbohydrate Research 340(1) (2005) 25-30
  

  beta-Galf-(1-->5)-beta-Galf-(1-->6)-alpha-Manp-(1-->6)-alpha-Manp, the immunodominant epitope in the cell-wall galactomannan of Aspergillus fumigatus, was synthesized for the first time as its allyl glycoside. The key disaccharide glycosyl donor, 2,3,5,6-tetra-O-benzoyl-beta-D-galactofuranosyl-(1-->5)-2-O-acetyl-3,6-di-O-benzoyl-beta-D-galactofuranosyl trichloroacetimidate (10), was constructed by 5-O-glycosylation of 1,2-O-isopropylidene-3,6-di-O-benzoyl-alpha-D-galactofuranose (4) with 2,3,5,6-tetra-O-benzoyl-beta-D-galactofuranosyl trichloroacetimidate (5), followed by 1,2-O-deacetonation, acetylation, selective 1-O-deacetylation, and trichloroacetimidation. The target tetrasaccharide 16 was obtained by the condensation of allyl 2,3,4-tri-O-benzoyl-alpha-D-mannopyranosyl-(1-->6)-2,3,4-tri-O-benzoyl-alpha-D-mannopyranoside (14) as glycosyl acceptor with the disaccharide glycosyl donor 10, followed by deprotection.

  synthesis, oligosaccharide, galactofuranose

  NCBI PubMed ID: 15620663
  Publication DOI: 10.1016/j.carres.2004.10.019
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: jning@mail.rcees.ac.cn
  Institutions: Research Center for Eco-Environmental Sciences, Chinese Academy of Sciences, PO Box 2871, Beijing 100085, China
  Methods: 13C NMR, 1H NMR, TLC, ESI-MS, chemical synthesis, chemical methods, UV, glycosylation
  
   
  
  Aspergillus fumigatus
  CSDB ID 41245 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: (->3) Ser/Thr-peptide
Trivial name: O-glycan
Compound class: glycoprotein
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_137472,IEDB_137485,IEDB_1394182,IEDB_141793,IEDB_144983,IEDB_147454,IEDB_152206,IEDB_153220,IEDB_190606,IEDB_983930,SB_198,SB_44,SB_67,SB_72

• Article ID: 6953
  Goto M "Protein O-Glycosylation in Fungi: Diverse Structures and Multiple Functions" - Bioscience, Biotechnology, and Biochemistry 71(6) (2007) 1415-1427
  

  Protein glycosylation is essential for eukaryotic cells from yeasts to humans. When compared to N-glycosylation, O-glycosylation is variable in sugar components and the mode of linkages connecting the sugars. In fungi, secretory proteins are commonly mannosylated by protein O-mannosyltransferase (PMT) in the endoplasmic reticulum, and subsequently glycosylated by several glycosyltransferases in the Golgi apparatus to form glycoproteins with diverse O-glycan structures. Protein O-glycosylation has roles in modulating the function of secretory proteins by enhancing the stability and solubility of the proteins, by affording protection from protease degradation, and by acting as a sorting determinant in yeasts. In filamentous fungi, protein O-glycosylation contributes to proper maintenance of fungal morphology, hyphal development, and differentiation. This review describes recent studies of the structure and function of protein O-glycosylation in industrially and medically important fungi.

  O-glycosylation, Aspergillus, protein O-mannosyltransferase

  NCBI PubMed ID: 17587671
  Publication DOI: 10.1271/bbb.70080
  Journal NLM ID: 9205717
  Publisher: Japan Society for Bioscience, Biotechnology, and Agrochemistry
  Correspondence: m_goto@agr.kyushu-u.ac.jp
  Institutions: Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University, Japan
  
   
  
  Aspergillus fumigatus
  CSDB ID 42030 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: (->3) Ser/Thr-peptide
Trivial name: O-glycan
Compound class: glycoprotein
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_137472,IEDB_137485,IEDB_1394182,IEDB_141793,IEDB_144983,IEDB_147452,IEDB_147454,IEDB_152206,IEDB_153220,IEDB_190606,IEDB_885812,IEDB_983930,SB_198,SB_44,SB_67,SB_72

• Article ID: 6953
  Goto M "Protein O-Glycosylation in Fungi: Diverse Structures and Multiple Functions" - Bioscience, Biotechnology, and Biochemistry 71(6) (2007) 1415-1427
  

  Protein glycosylation is essential for eukaryotic cells from yeasts to humans. When compared to N-glycosylation, O-glycosylation is variable in sugar components and the mode of linkages connecting the sugars. In fungi, secretory proteins are commonly mannosylated by protein O-mannosyltransferase (PMT) in the endoplasmic reticulum, and subsequently glycosylated by several glycosyltransferases in the Golgi apparatus to form glycoproteins with diverse O-glycan structures. Protein O-glycosylation has roles in modulating the function of secretory proteins by enhancing the stability and solubility of the proteins, by affording protection from protease degradation, and by acting as a sorting determinant in yeasts. In filamentous fungi, protein O-glycosylation contributes to proper maintenance of fungal morphology, hyphal development, and differentiation. This review describes recent studies of the structure and function of protein O-glycosylation in industrially and medically important fungi.

  O-glycosylation, Aspergillus, protein O-mannosyltransferase

  NCBI PubMed ID: 17587671
  Publication DOI: 10.1271/bbb.70080
  Journal NLM ID: 9205717
  Publisher: Japan Society for Bioscience, Biotechnology, and Agrochemistry
  Correspondence: m_goto@agr.kyushu-u.ac.jp
  Institutions: Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University, Japan
  
   
  
  Aspergillus fumigatus
  CSDB ID 42031 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: (->3) Ser/Thr-peptide
Trivial name: O-glycan
Compound class: glycoprotein
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_137472,IEDB_137485,IEDB_1394182,IEDB_141793,IEDB_144983,IEDB_147452,IEDB_147454,IEDB_152206,IEDB_153220,IEDB_190606,IEDB_885812,IEDB_983930,SB_198,SB_44,SB_67,SB_72

• Article ID: 6953
  Goto M "Protein O-Glycosylation in Fungi: Diverse Structures and Multiple Functions" - Bioscience, Biotechnology, and Biochemistry 71(6) (2007) 1415-1427
  

  Protein glycosylation is essential for eukaryotic cells from yeasts to humans. When compared to N-glycosylation, O-glycosylation is variable in sugar components and the mode of linkages connecting the sugars. In fungi, secretory proteins are commonly mannosylated by protein O-mannosyltransferase (PMT) in the endoplasmic reticulum, and subsequently glycosylated by several glycosyltransferases in the Golgi apparatus to form glycoproteins with diverse O-glycan structures. Protein O-glycosylation has roles in modulating the function of secretory proteins by enhancing the stability and solubility of the proteins, by affording protection from protease degradation, and by acting as a sorting determinant in yeasts. In filamentous fungi, protein O-glycosylation contributes to proper maintenance of fungal morphology, hyphal development, and differentiation. This review describes recent studies of the structure and function of protein O-glycosylation in industrially and medically important fungi.

  O-glycosylation, Aspergillus, protein O-mannosyltransferase

  NCBI PubMed ID: 17587671
  Publication DOI: 10.1271/bbb.70080
  Journal NLM ID: 9205717
  Publisher: Japan Society for Bioscience, Biotechnology, and Agrochemistry
  Correspondence: m_goto@agr.kyushu-u.ac.jp
  Institutions: Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University, Japan
  
   
  
  Aspergillus fumigatus
  CSDB ID 42204 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Aglycon: (->4) Asn (protein)
Compound class: cell wall glucan
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_137472,IEDB_141793,IEDB_142488,IEDB_144983,IEDB_144998,IEDB_146664,IEDB_147454,IEDB_152206,IEDB_153220,IEDB_190606,IEDB_983930,IEDB_983931,SB_192,SB_198,SB_44,SB_67,SB_72

• Article ID: 7121
  Shibata N, Okawa Y "Chemical structure of β-galactofuranose-containing polysaccharide and O-linked oligosaccharides obtained from the cell wall of pathogenic dematiaceous fungus Fonsecaea pedrosoi" - Glycobiology 21(1) (2011) 69-81
  

  Fonsecaea pedrosoi is the main etiologic agent of chromoblastomycosis, usually occurring in tropical and subtropical areas. The cell wall components of pathogenic microorganisms behave as an antigen and/or ligand of the innate immune response. The cells of F. pedrosoi reacted with the α-galactopyranose-binding lectin (Griffonia simplicifolia lectin 1B4 isolectin, GSL 1B4), as well as the α-mannose-binding lectin, concanavalin A. The cell wall glycoprotein was isolated from conidial cells of F. pedrosoi, and its structure was analyzed by (1)H-nuclear magnetic resonance (NMR) and (13)C-NMR experiments. The N-linked polysaccharide moiety consists of a backbone β-1,6-linked galactofuranose and α-1,6-linked mannose polymers, both of which are substituted with α-1,2-linked glucose side-chains. Furthermore, the glycoprotein contained a large amount of O-linked oligosaccharides, especially a hexaose that constituted approximately 20% of the glycoprotein. Unexpectedly, the hexaose had a highly branched structure which consisted of galactofuranose, galactopyranose, glucose and mannose residues as follows: aDGlcp(1-2)bDGalf(1-6)[aDGalp(1-3),aDGalp(1-2)]aDManp(1-2)?DManp. An anti-F. pedrosoi antibody specifically reacted with the cells of F. pedrosoi, whereas other fungal cells that contain galactofuranose residues did not react. The reactivity of the antibody was strongly inhibited by the branched hexaose, suggesting that the characteristic structure of the O-linked hexaose involves the antigenic specificity of the cells.

  oligosaccharide, polysaccharide, NMR spectroscopy, Galactomannan, β-elimination

  NCBI PubMed ID: 20833653
  Publication DOI: 10.1093/glycob/cwq132
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Correspondence: Shibata N
  Institutions: Department of Infection and Host Defense, Tohoku Pharmaceutical University, Sendai, Japan
  Methods: 13C NMR, 1H NMR, NMR-2D, methylation, GC-MS, ELISA, acid hydrolysis, HPLC, ion-exchange chromatography, extraction, acetolysis, ROESY, TOCSY, methylation analysis, reduction, column chromatography, GS-MS, flow cytometry analysis, DQF-COSY, HMBC, DEPT
  
   
  
  Fonsecaea pedrosoi NBRC 6733
  CSDB ID 43542 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: (->3) L-Ser/L-Thr (protein)
Compound class: O-linked glycoprotein
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_137472,IEDB_141793,IEDB_144983,IEDB_147452,IEDB_147454,IEDB_152206,IEDB_153220,IEDB_190606,IEDB_885812,IEDB_983930,SB_198,SB_44,SB_67,SB_72

• Article ID: 7461
  Doering TL, Cummings RD, Aebi M "Fungi" - Book: Essentials of Glycobiology [Internet]. 3rd edition. (2017) Vol. 1, Chapter 23,
  

  Fungi are a fascinating group of predominantly multicellular organisms. Fungal species, such as Saccharomyces cerevisiae, have been instrumental in defining the fundamental processes of glycosylation, but their glycobiology is significantly different from animal or plant systems. This chapter describes the glycan structures that compose the fungal cell wall, offers some insights into novel glycobiology revealed through studying fungal systems, addresses the use of fungi as experimental and synthetic systems, and delineates the relationships of several important glycoconjugates to fungal biology and pathogenesis.

  NCBI PubMed ID: 28876853
  Publication DOI: 10.1101/glycobiology.3e.023
  WWW link: https://www.ncbi.nlm.nih.gov/books/NBK453054/
  Publisher: Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press
  Editors: Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M, Darvill AG, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL, Seeberger RH
  Institutions: Complex Carbohydrate Research Center, University of Georgia, Athens, USA, Laboratory of Immunoglycobiology, WPI Immunology Frontier Research Center, Osaka University, Osaka, Japan, Distinguished Professor of Medicine and Cellular & Molecular Medicine, Co-Director, Glycobiology Research and Training Center, University of California, San Diego, USA, National Center for Functional Glycomics, Harvard Medical School, Cambridge, USA, Glycobiology Research and Training Center, University of California, San Diego, USA, Albert Einstein College of Medicine, New York, NY, USA, Johns Hopkins University, Baltimore, USA, ETH Zürich, Zürich, Switzerland, Macquarie University and Institute for Glycomics, Griffith University, Sydney, Australia, University of Georgia, Athens, Georgia, USA, Max-Planck-Institute of Colloids and Interfaces, Potsdam, Germany
  
   
  
  Aspergillus
  CSDB ID 42955 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: (->3) L-Ser/L-Thr (protein)
Compound class: O-linked glycoprotein
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_137472,IEDB_141793,IEDB_144983,IEDB_147452,IEDB_147454,IEDB_152206,IEDB_153220,IEDB_190606,IEDB_885812,IEDB_983930,SB_198,SB_44,SB_67,SB_72

• Article ID: 7461
  Doering TL, Cummings RD, Aebi M "Fungi" - Book: Essentials of Glycobiology [Internet]. 3rd edition. (2017) Vol. 1, Chapter 23,
  

  Fungi are a fascinating group of predominantly multicellular organisms. Fungal species, such as Saccharomyces cerevisiae, have been instrumental in defining the fundamental processes of glycosylation, but their glycobiology is significantly different from animal or plant systems. This chapter describes the glycan structures that compose the fungal cell wall, offers some insights into novel glycobiology revealed through studying fungal systems, addresses the use of fungi as experimental and synthetic systems, and delineates the relationships of several important glycoconjugates to fungal biology and pathogenesis.

  NCBI PubMed ID: 28876853
  Publication DOI: 10.1101/glycobiology.3e.023
  WWW link: https://www.ncbi.nlm.nih.gov/books/NBK453054/
  Publisher: Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press
  Editors: Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M, Darvill AG, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL, Seeberger RH
  Institutions: Complex Carbohydrate Research Center, University of Georgia, Athens, USA, Laboratory of Immunoglycobiology, WPI Immunology Frontier Research Center, Osaka University, Osaka, Japan, Distinguished Professor of Medicine and Cellular & Molecular Medicine, Co-Director, Glycobiology Research and Training Center, University of California, San Diego, USA, National Center for Functional Glycomics, Harvard Medical School, Cambridge, USA, Glycobiology Research and Training Center, University of California, San Diego, USA, Albert Einstein College of Medicine, New York, NY, USA, Johns Hopkins University, Baltimore, USA, ETH Zürich, Zürich, Switzerland, Macquarie University and Institute for Glycomics, Griffith University, Sydney, Australia, University of Georgia, Athens, Georgia, USA, Max-Planck-Institute of Colloids and Interfaces, Potsdam, Germany
  
   
  
  Aspergillus
  CSDB ID 42956 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure ; n=15, 40000
Compound class: EPS, cell wall polysaccharide
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_136104,IEDB_137472,IEDB_141793,IEDB_141836,IEDB_142488,IEDB_143632,IEDB_144983,IEDB_144998,IEDB_146664,IEDB_147454,IEDB_149176,IEDB_152206,IEDB_153220,IEDB_158538,IEDB_164174,IEDB_190606,IEDB_983930,IEDB_983931,SB_136,SB_192,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72

• Article ID: 7475
  Li H, Yu H, Zhu H "Structure Studies of the Extracellular Polysaccharide from Trichoderma sp. KK19L1 and Its Antitumor Effect via Cell Cycle Arrest and Apoptosis" - Applied Biochemistry and Biotechnology 182 (2017) 128-141
  

  An extracellular polysaccharide TP1A was purified from the fermented broth of Trichoderma sp. KK19L1 by combination of Q Sepharose fast flow and Sephacryl S-300 chromatography. TP1A was composed of Man, Gal, and Glc in a molar ratio of about 3.0:5.1:8.1. The molar mass of TP1A was about 40.0 kDa. Methylation and NMR analysis indicated that the probable structure of TP1A was [→4,6)-α-D-Glcp(1→6)-β-D-Galf(1→6)-β-D-Galf(1→2,6)-β-D-Galf(1→2,6)-β-D-Galf(1→2,6)-β-D-Galf(1→2,6)-α-D-Manp(1→2,6)-α-D-Manp(1→] with [α-D-Glcp(1→] and [α-D-Manp(1→6)-α-D-Glcp(1→6)-α-D-Glcp(1→] as branches. The antitumor study showed that TP1A was able to inhibit the cell viability of HeLa and MCF-7 cells. TP1A could arrest HeLa cells in G2/M phase and induce HeLa cell apoptosis. These findings suggest that fungal polysaccharides could be a potential source for antitumor agents.

  structure, extracellular polysaccharide, antitumor activity, Trichoderma sp. KK19L1

  NCBI PubMed ID: 27854039
  Publication DOI: 10.1007/s12010-016-2315-1
  Journal NLM ID: 8208561
  Publisher: Humana Press
  Correspondence: Li H ; Zhu H
  Institutions: Key Laboratory of Medicinal Chemistry and Molecular Diagnosis, Ministry of Education, Baoding, China, College of Chemistry and Environment Science, Hebei University, Baoding, China, College of Pharmaceutical Science, Hebei University, Baoding, China
  Methods: 13C NMR, 1H NMR, methylation, HPLC, UV, acetylation, TOCSY, NaBD4 reduction, GS-MS, trifluoroacetic acid solvolysis, HPGPC, HMBC, DEPT, NOESY, HSQC, FT-IR
  
   
  
  Trichoderma sp. KK19L1
  CSDB ID 43022 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: galactomannan
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_137472,IEDB_141793,IEDB_144983,IEDB_147452,IEDB_147454,IEDB_152206,IEDB_153220,IEDB_190606,IEDB_885812,IEDB_983930,SB_198,SB_44,SB_67,SB_72

• Article ID: 5306
  Marino C, Rinflerch A, de Lederkremer RM "Galactofuranose antigens, a target for diagnosis of fungal infections in humans" - Future Science OA 3(3) (2017) FSO199
  

  The use of biomarkers for the detection of fungal infections is of interest to complement histopathological and culture methods. Since the production of antibodies in immunocompromised patients is scarce, detection of a specific antigen could be effective for early diagnosis. D-Galactofuranose (Galf) is the antigenic epitope in glycoconjugates of several pathogenic fungi. Since Galf is not biosynthesized by mammals, it is an attractive candidate for diagnosis of infection. A monoclonal antibody that recognizes Galf is commercialized for detection of aspergillosis. The linkage of Galf in the natural glycans and the chemical structures of the synthesized Galf-containing oligosaccharides are described in this paper. The oligosaccharides could be used for the synthesis of artificial carbohydrate-based antigens, not enough exploited for diagnosis.

  galactofuranose, immune response, diagnosis, biomarkers, fungal infections, synthetic haptens

  NCBI PubMed ID: 28883999
  Publication DOI: 10.4155/fsoa-2017-0030
  Journal NLM ID: 101665030
  Publisher: London: Future Science Group
  Correspondence: Marino C ; de Lederkremer RM
  Institutions: Universidad de Buenos Aires, Consejo Nacional de Investigaciones Científicas y Técnicas, Centro de Investigaciones en Hidratos de Carbono (CIHIDECAR), Departamento de Química Orgánica, Facultad de Ciencias Exactas y Naturales, Pabellón II, Ciudad Universitaria, Buenos Aires, Argentina, Servicio de Dermatología, Dermatología Experimental, Hospital Italiano de Buenos Aires, Buenos Aires, Argentina
  
   
  
  Aspergillus fumigatus
  CSDB ID 43129 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Compound class: cell wall polysaccharide, galactoglucomannan
Contained glycoepitopes: IEDB_115576,IEDB_128161,IEDB_130701,IEDB_133966,IEDB_134620,IEDB_134621,IEDB_135614,IEDB_136095,IEDB_136104,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_1397514,IEDB_140116,IEDB_140628,IEDB_140629,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141806,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_142357,IEDB_142488,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_144998,IEDB_146664,IEDB_147452,IEDB_147453,IEDB_147454,IEDB_149137,IEDB_149176,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_153543,IEDB_153755,IEDB_153756,IEDB_1539315,IEDB_158538,IEDB_158555,IEDB_161166,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164479,IEDB_164480,IEDB_174840,IEDB_190606,IEDB_232584,IEDB_232585,IEDB_241101,IEDB_420417,IEDB_420418,IEDB_420419,IEDB_420420,IEDB_420421,IEDB_423115,IEDB_558866,IEDB_558867,IEDB_558868,IEDB_558869,IEDB_742521,IEDB_76933,IEDB_857742,IEDB_857743,IEDB_885812,IEDB_983930,IEDB_983931,SB_136,SB_191,SB_192,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72,SB_77

• Article ID: 7500
  Gow NAR, Latge JP, Munro CA "The fungal cell wall: structure, biosynthesis, and function" - Microbiology Spectrum 5(3) (2017) FUNK-0035
  

  The molecular composition of the cell wall is critical for the biology and ecology of each fungal species. Fungal walls are composed of matrix components that are embedded and linked to scaffolds of fibrous load-bearing polysaccharides. Most of the major cell wall components of fungal pathogens are not represented in humans, other mammals, or plants, and therefore the immune systems of animals and plants have evolved to recognize many of the conserved elements of fungal walls. For similar reasons the enzymes that assemble fungal cell wall components are excellent targets for antifungal chemotherapies and fungicides. However, for fungal pathogens, the cell wall is often disguised since key signature molecules for immune recognition are sometimes masked by immunologically inert molecules. Cell wall damage leads to the activation of sophisticated fail-safe mechanisms that shore up and repair walls to avoid catastrophic breaching of the integrity of the surface. The frontiers of research on fungal cell walls are moving from a descriptive phase defining the underlying genes and component parts of fungal walls to more dynamic analyses of how the various components are assembled, cross-linked, and modified in response to environmental signals. This review therefore discusses recent advances in research investigating the composition, synthesis, and regulation of cell walls and how the cell wall is targeted by immune recognition systems and the design of antifungal diagnostics and therapeutics.

  NCBI PubMed ID: 28513415
  Publication DOI: 10.1128/microbiolspec.FUNK-0035-2016
  Journal NLM ID: 101634614
  Publisher: Washington, DC: ASM Press
  Correspondence: n.gow@abdn.ac.uk
  Institutions: Unité des Aspergillus, Institut Pasteur, Paris, France, Aberdeen Fungal Group, Institute of Medical Sciences, University of Aberdeen, Aberdeen, UK
  
   
  
  Aspergillus fumigatus
  CSDB ID 43192 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Compound class: galactomananan
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_136104,IEDB_137472,IEDB_140116,IEDB_141793,IEDB_141795,IEDB_141829,IEDB_141830,IEDB_141832,IEDB_141833,IEDB_143632,IEDB_144983,IEDB_147452,IEDB_147453,IEDB_147454,IEDB_149137,IEDB_152206,IEDB_153220,IEDB_164480,IEDB_190606,IEDB_76933,IEDB_885812,IEDB_983930,SB_136,SB_191,SB_196,SB_198,SB_44,SB_67,SB_72

• Article ID: 7554
  Latge JP "Galactofuranose containing molecules in Aspergillus fumigatus" - Medical Mycology 47 (2009) S104-S109
  

  Galactofuranose is a major carbohydrate in Aspergillus fumigatus. It became famous in medical mycology as being part of the galactomannan which was shown 30 years ago to be the major antigen circulating in the body fluid of patients suffering from invasive aspergillosis. Four different molecules contain galactofuranose in A. fumigatus: (i) the galactomannan present in the alkali soluble and insoluble fraction of the cell wall (ii) N- and O glycan moieties of secreted glycoproteins (iii) a GPI- anchored lipophosphogalactomannan and (iv) several sphingolipids also anchored to the membrane by an inositol phosphoceramide.

  genetics, cell wall, glycobiology, Aspergillus, aspergillosis

  NCBI PubMed ID: 18686165
  Publication DOI: 10.1080/13693780802258832
  Journal NLM ID: 9815835
  Publisher: Oxford: Oxford University Press
  Correspondence: jplatge@pasteur.fr
  Institutions: Institut Pasteur, Aspergillus Unit, Paris, France
  
   
  
  Aspergillus fumigatus
  CSDB ID 44542 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Trivial name: galactomannan
Compound class: galactomannan
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_136104,IEDB_137472,IEDB_140116,IEDB_141793,IEDB_141795,IEDB_141829,IEDB_141830,IEDB_141832,IEDB_141833,IEDB_143632,IEDB_144983,IEDB_147452,IEDB_147453,IEDB_147454,IEDB_149137,IEDB_152206,IEDB_153220,IEDB_164480,IEDB_190606,IEDB_76933,IEDB_885812,IEDB_983930,SB_136,SB_191,SB_196,SB_198,SB_44,SB_67,SB_72

• Article ID: 7724
  Free SJ "Fungal cell wall organization and biosynthesis" - Advances in Genetics 81 (2013) 33-82
  

  The composition and organization of the cell walls from Saccharomyces cerevisiae, Candida albicans, Aspergillus fumigatus, Schizosaccharomyces pombe, Neurospora crassa, and Cryptococcus neoformans are compared and contrasted. These cell walls contain chitin, chitosan, β-1,3-glucan, β-1,6-glucan, mixed β-1,3-/β-1,4-glucan, α-1,3-glucan, melanin, and glycoproteins as major constituents. A comparison of these cell walls shows that there is a great deal of variability in fungal cell wall composition and organization. However, in all cases, the cell wall components are cross-linked together to generate a cell wall matrix. The biosynthesis and properties of each of the major cell wall components are discussed. The chitin and glucans are synthesized and extruded into the cell wall space by plasma membrane-associated chitin synthases and glucan synthases. The glycoproteins are synthesized by ER-associated ribosomes and pass through the canonical secretory pathway. Over half of the major cell wall proteins are modified by the addition of a glycosylphosphatidylinositol anchor. The cell wall glycoproteins are also modified by the addition of O-linked oligosaccharides, and their N-linked oligosaccharides are extensively modified during their passage through the secretory pathway. These cell wall glycoprotein posttranslational modifications are essential for cross-linking the proteins into the cell wall matrix. Cross-linking the cell wall components together is essential for cell wall integrity. The activities of four groups of cross-linking enzymes are discussed. Cell wall proteins function as cross-linking enzymes, structural elements, adhesins, and environmental stress sensors and protect the cell from environmental changes.

  Candida albicans, Aspergillus fumigatus, Saccharomyces cerevisiae, fungal cell wall, Schizosaccharomyces pombe, Neurospora crassa, cell wall biogenesis, glucan; chitin, Cryptococcus neoformas

  NCBI PubMed ID: 23419716
  Publication DOI: 10.1016/B978-0-12-407677-8.00002-6
  Journal NLM ID: 0370421
  Publisher: San Diego, CA: Academic Press
  Correspondence: free@buffalo.edu
  Institutions: Department of Biological Sciences, SUNY University at Buffalo, Buffalo, NY, USA
  Methods: MS, electrophoresis, enzymatic digestion, microscopy
  
   
  
  Aspergillus fumigatus
  CSDB ID 44866 (all data & tools)