Found 19 structures.
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1. Compound ID: 17190
Galf-(1-?)-Galf-(1-?)-Galf-(1-?)-b-Galf-(1-5)-Galf-(1-?)-+
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Man-(1-?)-Man-(1-?)-a-Man-(1-2)-a-Man-(1-2)-a-Man-(1-2)-+ |
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Galf-(1-?)-Galf-(1-?)-Galf-(1-?)-b-Galf-(1-5)-Galf-(1-?)-a-Man-(1-6)-a-Man-(1-2)-a-Man-(1-2)-Man-(1-6)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-b-Glc-(1-3)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-+
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b-GlcN-(1-4)-b-GlcN-(1-4)-b-GlcN-(1-4)-b-GlcN-(1-4)-b-GlcN-(1-4)-b-GlcN-(1-4)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-b-Glc-(1-3)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-+ |
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Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-+ | |
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Glc-(1-?)-Glc-(1-?)-b-Glc-(1-3)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-b-Glc-(1-6)-+ | |
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Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-+ | | |
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Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-b-Glc-(1-6)-+ | | |
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Glc-(1-?)-Glc-(1-?)-b-Glc-(1-3)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-+ | | | |
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Glc-(1-4)-b-Glc-(1-3)-b-Glc-(1-4)-b-Glc-(1-3)-b-Glc-(1-4)-b-Glc-(1-3)-b-Glc-(1-3)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-b-Glc-(1-3)-b-Glc-(1-3)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc |
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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
The structure is contained in the following publication(s):
- 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.M909975199Journal NLM ID: 2985121RWWW link: http://www.jbc.org/content/275/36/27594.abstractPublisher: 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
- 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.39.1.9.17Journal NLM ID: 9815835Publisher: Oxford: Oxford University Press
Correspondence: jplatge@pasteur.fr
Institutions: Unité des Aspergillus, Institut Pasteur, Paris, France
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2. Compound ID: 17356
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
The structure is contained in the following publication(s):
- 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: 15620663Publication DOI: 10.1016/j.carres.2004.10.019Journal NLM ID: 0043535Publisher: 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
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3. Compound ID: 17358
b-D-Galf-(1-5)-b-D-Galf-(1-6)-+
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b-D-Galf-(1-5)-b-D-Galf-(1-3)-+ |
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-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1- |
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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
The structure is contained in the following publication(s):
- 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: 15620663Publication DOI: 10.1016/j.carres.2004.10.019Journal NLM ID: 0043535Publisher: 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
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4. Compound ID: 17776
b-Galf-(1-5)-b-Galf-(1-6)-a-Manp-(1-6)-Manp-(1--/(->3) Ser/Thr-peptide/ |
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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
The structure is contained in the following publication(s):
- 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: 17587671Publication DOI: 10.1271/bbb.70080Journal NLM ID: 9205717Publisher: 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
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5. Compound ID: 17778
b-Galf-(1-5)-b-Galf-(1-5)-b-Galf-(1-6)-a-Manp-(1-6)-Manp-(1--/(->3) Ser/Thr-peptide/ |
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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
The structure is contained in the following publication(s):
- 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: 17587671Publication DOI: 10.1271/bbb.70080Journal NLM ID: 9205717Publisher: 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
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6. Compound ID: 18875
b-D-Galf-(1-5)-b-D-Galf-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1--/(->3) L-Ser/L-Thr (protein)/ |
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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
The structure is contained in the following publication(s):
- 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: 28876853Publication DOI: 10.1101/glycobiology.3e.023WWW 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
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7. Compound ID: 18876
b-D-Galf-(1-5)-b-D-Galf-(1-5)-b-D-Galf-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1--/(->3) L-Ser/L-Thr (protein)/ |
Show graphically |
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
The structure is contained in the following publication(s):
- 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: 28876853Publication DOI: 10.1101/glycobiology.3e.023WWW 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
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8. Compound ID: 19023
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
The structure is contained in the following publication(s):
- 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: 28883999Publication DOI: 10.4155/fsoa-2017-0030Journal NLM ID: 101665030Publisher: 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
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9. Compound ID: 19044
D-Galf-(1-?)-D-Galf-(1-?)-D-Galf-(1-?)-b-D-Galf-(1-5)-D-Galf-(1-?)-+
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D-Galf-(1-?)-D-Galf-(1-?)-D-Galf-(1-?)-b-D-Galf-(1-5)-D-Galf-(1-?)-+ |
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D-Manp-(1-?)-D-Manp-(1-?)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-D-Manp-(1-6)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-b-D-Glcp-(1-3)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-+
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b-D-GlcpN-(1-4)-b-D-GlcpN-(1-4)-b-D-GlcpN-(1-4)-b-D-GlcpN-(1-4)-b-D-GlcpN-(1-4)-b-D-GlcpN-(1-4)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-b-D-Glcp-(1-3)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-+ |
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D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-+ | |
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D-Glcp-(1-?)-D-Glcp-(1-?)-b-D-Glcp-(1-3)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-b-D-Glcp-(1-6)-+ | |
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D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-+ | | |
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D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-b-D-Glcp-(1-6)-+ | | |
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D-Glcp-(1-?)-D-Glcp-(1-?)-b-D-Glcp-(1-3)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-+ | | | |
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D-Glcp-(1-4)-b-D-Glcp-(1-3)-b-D-Glcp-(1-4)-b-D-Glcp-(1-3)-b-D-Glcp-(1-4)-b-D-Glcp-(1-3)-b-D-Glcp-(1-3)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-b-D-Glcp-(1-3)-b-D-Glcp-(1-3)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp-(1-?)-D-Glcp |
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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
The structure is contained in the following publication(s):
- 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: 28513415Publication DOI: 10.1128/microbiolspec.FUNK-0035-2016Journal NLM ID: 101634614Publisher: 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
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10. Compound ID: 19173
{{{-b-Galf-(1-5)-}}}b-Galf-(1-6)-+
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{{{-b-Galf-(1-5)-}}}b-Galf-(1-6)-+ |
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-2)-a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1-2)-a-D-Manp-(1- |
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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
The structure is contained in the following publication(s):
- 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: 18686165Publication DOI: 10.1080/13693780802258832Journal NLM ID: 9815835Publisher: Oxford: Oxford University Press
Correspondence: jplatge@pasteur.fr
Institutions: Institut Pasteur, Aspergillus Unit, Paris, France
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11. Compound ID: 19532
{{{-b-Galf-(1-5)-}}}?%b-Galf-(1-?)-+
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{{{-b-Galf-(1-5)-}}}?%b-Galf-(1-?)-+ |
| |
{{{-b-Galf-(1-5)-}}}?%b-Galf-(1-?)-+ | |
| | |
{{{-b-Galf-(1-5)-}}}?%b-Galf-(1-?)-+ | | |
| | | |
-2)-a-D-Manp-(1-6)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1- |
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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
The structure is contained in the following publication(s):
- 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: 23419716Publication DOI: 10.1016/B978-0-12-407677-8.00002-6Journal NLM ID: 0370421Publisher: 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
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12. Compound ID: 19963
{{{-b-D-Galf-(1-5)-}}}/n=3-4/-?%b-D-Galf-(1-?)-+
|
-?)-a-D-Manp-(1- |
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Structure type: structural motif or average structure
Compound class: galactomannan
Contained glycoepitopes: IEDB_115576,IEDB_130701,IEDB_134620,IEDB_136095,IEDB_136104,IEDB_137472,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_143632,IEDB_144983,IEDB_147452,IEDB_147453,IEDB_147454,IEDB_149137,IEDB_152206,IEDB_153220,IEDB_153756,IEDB_153762,IEDB_153763,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164480,IEDB_174840,IEDB_190606,IEDB_241100,IEDB_76933,IEDB_885812,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72,SB_77
The structure is contained in the following publication(s):
- Article ID: 7923
Argunov DA, Krylov VB, Nifantiev NE "Convergent synthesis of isomeric heterosaccharides related to the fragments of galactomannan from Aspergillus fumigatus" -
Organic and Biomolecular Chemistry 13(11) (2015) 3255-3267
Aspergillus fumigatus is a very common fungus with high pathogenic potential for immunosuppressed hospital patients. A. fumigatus galactomannan, being the part of its cell wall, is considered as a promising candidate for vaccine and diagnostic test-systems. In this article we report the convergent synthesis of pentasaccharide fragments of the galactomannan containing the β-(1→5)-linked galactofuranoside chain attached to O-3 or O-6 of a spacer-armed mannopyranoside residue. The synthesis of selectively protected galactofuranoside precursors has been performed using recently developed pyranoside-into-furanoside (PIF) rearrangement. For assembling the target galactomannan structures the [1 + 2 + 2]-scheme was applied. This strategy was shown to be highly efficient and can easily be extended to the synthesis of longer fragments of the galactomannan.
cell wall, Galactomannan, Aspergilus, antifungal drug target
NCBI PubMed ID: 25643073Publication DOI: 10.1039/c4ob02634aJournal NLM ID: 101154995Publisher: The Royal Society of Chemistry
Correspondence: Nifantiev NE
Institutions: Laboratory of Glycoconjugate Chemistry, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, Laboratory of Glycoconjugate Chemistry, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Leninsky prospect 47, Moscow, Russia
Methods: 1H NMR, GC, optical rotation measurement, ROESY, TOCSY, HMBC, COSY, NOESY, HSQC, HSQC-TOCSY, optical rotation, 13N MNR, HMRS
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13. Compound ID: 19996
?%b-D-Galf-(1-5)-b-D-Galf-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1--/(->3) L-Thr/L-Ser (Glucoamylase 1)/ |
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Structure type: oligomer
Aglycon: (->3) L-Thr/L-Ser (Glucoamylase 1)
Compound class: O-glycan
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
The structure is contained in the following publication(s):
- Article ID: 7939
Deshpande N, Wilkins MR, Packer N, Nevalainen H "Protein glycosylation pathways in filamentous fungi" -
Glycobiology 18(8) (2008) 626–637
Glycosylation of proteins is important for protein stability, secretion, and localization. In this study, we have investigated the glycan synthesis pathways of 12 filamentous fungi including those of medical/agricultural/industrial importance for which genomes have been recently sequenced. We have adopted a systems biology approach to combine the results from comparative genomics techniques with high confidence information on the enzymes and fungal glycan structures, reported in the literature. From this, we have developed a composite representation of the glycan synthesis pathways in filamentous fungi (both N- and O-linked). The N-glycosylation pathway in the cytoplasm and endoplasmic reticulum was found to be highly conserved evolutionarily across all the filamentous fungi considered in the study. In the final stages of N-glycan synthesis in the Golgi, filamentous fungi follow the high mannose pathway as in Saccharomyces cerevisiae, but the level of glycan mannosylation is reduced. Highly specialized N-glycan structures with galactofuranose residues, phosphodiesters, and other insufficiently trimmed structures have also been identified in the filamentous fungi. O-Linked glycosylation in filamentous fungi was seen to be highly conserved with many mannosyltransferases that are similar to those in S. cerevisiae. However, highly variable and diverse O-linked glycans also exist. We have developed a web resource for presenting the compiled data with user-friendly query options, which can be accessed at www.fungalglycans.org. This resource can assist attempts to remodel glycosylation of recombinant proteins expressed in filamentous fungal hosts.
synthesis, glycan, Recombinant Proteins, filamentous fungi, comparative genomics, systems biology
NCBI PubMed ID: 18504293Publication DOI: 10.1093/glycob/cwn044Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: ndeshpan@els.mq.edu.au
Institutions: Department of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, Australia, School of Biotechnology and Biomolecular Sciences, University of New South Wales, Australia
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14. Compound ID: 20628
{{{-b-D-Galf-(1-5)-}}}/n=0-3/-b-D-Galf-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1--/(->3) L-Thr/L-Ser (protein)/ |
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Structure type: oligomer
Aglycon: (->3) L-Thr/L-Ser (protein)
Compound class: O-glycan
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_137472,IEDB_141793,IEDB_144983,IEDB_147452,IEDB_147453,IEDB_147454,IEDB_149137,IEDB_152206,IEDB_153220,IEDB_190606,IEDB_885812,IEDB_983930,SB_198,SB_44,SB_67,SB_72
The structure is contained in the following publication(s):
- Article ID: 8258
Oka T, Futagami T, Goto M "Cell wall biosynthesis in filamentous fungi" -
Book: Stress Biology of Yeasts and Fungi (2015) Chapter 10, 151-168
The cell wall provides physical strength to cells and defines the morphology of fungi. During hyphal development of filamentous fungi, the apical region and the branching sites of the cell are remodeled to support hyphal extension and formation of a new hypha. The cell wall has contact with the environment and thus is the place of first contact with external stresses originating outside of the cells. The cell wall also acts as a matrix for various extracellular proteins such as enzymes and sensor proteins. Budding yeast (Saccharomyces cerevisiae) and filamentous fungi (Aspergillus species) are industrially and medically important fungi belonging to the Ascomycota. These fungi share similar composition in the cell wall although they are morphologically different. Fungal cell walls are usually composed of glucose, mannose, N-acetyl-D-glucosamine, proteins, and lipids. Some glycans composed of galactofuranose or N-acetyl-D-galactosamine are found characteristically in the cell wall of Aspergillus species. In this chapter, we present an overview of current knowledge on cell wall biogenesis and wall-stress sensing in fungi, particularly focusing on recent findings in filamentous fungi
cell wall, glycosylation, Glucans, Aspergillus, fungi, GPI anchor, Saccharomyces, cell wall integrity, stress response
Publication DOI: 10.1007/978-4-431-55248-2_10Publisher: Springer, Tokyo
Correspondence: mgoto@brs.kyushu-u.ac.jp
Editors: Takagi H, Kitagaki H
Institutions: Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University, Fukuoka, Japan, Department of Applied Microbial Technology, Faculty of Biotechnology and Life Science, Sojo University, Kumamoto, Japan, Education and Research Center for Fermentation Studies, Faculty of Agriculture, Kagoshima University, Kagoshima, Japan
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15. Compound ID: 20795
?%b-D-Galf-(1-5)-b-D-Galf-(1-5)-84%b-D-Galf-(1-?)-+
|
-?)-a-D-Manp-(1- |
Show graphically |
Structure type: structural motif or average structure
Compound class: galactomannan
Contained glycoepitopes: IEDB_115576,IEDB_130701,IEDB_134620,IEDB_136095,IEDB_136104,IEDB_137472,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_143632,IEDB_144983,IEDB_147452,IEDB_147454,IEDB_152206,IEDB_153220,IEDB_153756,IEDB_153762,IEDB_153763,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164480,IEDB_174840,IEDB_190606,IEDB_241100,IEDB_76933,IEDB_885812,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72,SB_77
The structure is contained in the following publication(s):
- Article ID: 8362
Chen J, Robb CS, Unfried F, Kappelmann L, Markert S, Song T, Harder J, Avcı B, Becher D, Xie P, Amann RI, Hehemann JH, Schweder T, Teeling H "Alpha- and beta-mannan utilization by marine Bacteroidetes" -
Environmental Microbiology 20(11) (2018) 4127-4140
Marine microscopic algae carry out about half of the global carbon dioxide fixation into organic matter. They provide organic substrates for marine microbes such as members of the Bacteroidetes that degrade algal polysaccharides using carbohydrate-active enzymes (CAZymes). In Bacteroidetes genomes CAZyme encoding genes are mostly grouped in distinct regions termed polysaccharide utilization loci (PULs). While some studies have shown involvement of PULs in the degradation of algal polysaccharides, the specific substrates are for the most part still unknown. We investigated four marine Bacteroidetes isolated from the southern North Sea that harbour putative mannan-specific PULs. These PULs are similarly organized as PULs in human gut Bacteroides that digest α- and β-mannans from yeasts and plants respectively. Using proteomics and defined growth experiments with polysaccharides as sole carbon sources we could show that the investigated marine Bacteroidetes express the predicted functional proteins required for α- and β-mannan degradation. Our data suggest that algal mannans play an as yet unknown important role in the marine carbon cycle, and that biochemical principles established for gut or terrestrial microbes also apply to marine bacteria, even though their PULs are evolutionarily distant.
mannan, Galactomannan, Proteomics, glycobiology, Bacteroidetes, carbohydrate-active enzymes, marine polysaccharide utilization, Flavobacteriia
NCBI PubMed ID: 30246424Publication DOI: 10.1111/1462-2920.14414Journal NLM ID: 100883692Publisher: Blackwell Publishing
Correspondence: Teeling H
; Schweder T
Institutions: University of Chinese Academy of Sciences, Beijing, China, Max Planck Institute for Marine Microbiology, Bremen, Germany, Donghu Experimental Station of Lake Ecosystems, State Key Laboratory of Freshwater Ecology and Biotechnology of China, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan, China, College of Ocean, Hebei Agricultural University, Qinhuangdao, China, MARUM, Center for Marine Environmental Sciences, University of Bremen, Bremen, Germany, Pharmaceutical Biotechnology, Institute of Pharmacy, University Greifswald, Greifswald, Germany, Institute of Marine Biotechnology, Greifswald, Germany, Institute of Microbiology, University Greifswald, Greifswald, Germany
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Next 15 structure(s)
Total list of structure IDs on all result pages of the current query:
Total list of corresponding CSDB IDs (record IDs):
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