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_130701,IEDB_136095,IEDB_137472,IEDB_144983,IEDB_147453,IEDB_149137,IEDB_152206,IEDB_190606,IEDB_885812,IEDB_983930,SB_44,SB_67,SB_72

• Article ID: 6765
  Haido RM, Silva MH, Ejzemberg R, Leitao EA, Hearn VM, Evans EG, Barreto Bergter E "Analysis of peptidogalactomannans from the mycelial surface of Aspergillus fumigatus" - Medical Mycology 36 (1998) 313-321
  

  Peptidogalactomannans (pGMs) from mycelium of two strains of Aspergillus fumigatus were fractionated by Cetavlon precipitation and size exclusion chromatography and theircarbohydrate structures analysed using methylation-fragmentation analysis, partial acetolysis and 13C-nuclear magnetic resonance spectroscopy. The most significant difference between the pGMs of the two strains was the degree of branching and the proportion of non-reducing ends of α-D-Manp) and β-D-Galf units. Methylation data showed that the pGM from AF 2109 contained α-D-Man p) and β-D-Galf non-reducing end units in a proportion of 3:1 while, in contrast, the proportion of these structures in pGM from AF 2140 was 7:1, resulting in a highly branched structure. The immunoreactivity of the pGM fractions was tested by indirect immunofluorescence. The fractions were also tested in an ELISA system with rabbit antiserum raised to whole cells of A. fumigatus NCPF 2140 and with serum from patients with either proven aspergilloma or ABPA. The carbohydrate moiety of the pGM appears to be responsible for the antigenicity. Periodate treatment, partial acid hydrolysis and β-elimination removed most of the antibody binding capacity.

  Aspergillus fumigatus, 13C-nuclear magnetic resonance, glycoprotein immunoreactivity, peptidogalactomannans

  Publication DOI: 10.1080/02681219880000491
  Journal NLM ID: 9815835
  Publisher: Oxford: Oxford University Press
  Correspondence: immgbel@microbio.ufrj.br
  Institutions: Instituto Biomédico, Universidade do Rio de Janeiro, Brasil, Instituto de Microbiologia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brasil, Mycology Reference Laboratory, University of Leeds, UK
  Methods: gel filtration, 13C NMR, 1H NMR, GC-MS, SDS-PAGE, ELISA, acid hydrolysis, periodate oxidation, methylation analysis, partial acetolysis, immunofluorescence, beta-elimination, phenol sulfuric acid method, Folin phenol reagent method
  
   
  
  Aspergillus fumigatus NCPF 2109, Aspergillus fumigatus AF 2109
  CSDB ID 40723 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: immunodominant epitope
Compound class: cell wall polysaccharide
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_137472,IEDB_137485,IEDB_144983,IEDB_147453,IEDB_149137,IEDB_152206,IEDB_190606,IEDB_885812,IEDB_983930,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 41244 (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_144983,IEDB_147453,IEDB_149137,IEDB_152206,IEDB_190606,IEDB_885812,IEDB_983930,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 42032 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure ; n=9-10
Compound class: O-polysaccharide, cell wall polysaccharide, 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_147453,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: 7329
  Latge JP, Kobayashi H, Debeaupuis JP, Diaquin M, Sarfati J, Wieruszeski JM, Parra E, Bouchara JP, Fournet B "Chemical and immunological characterization of the extracellular galactomannan of Aspergillus fumigatus" - Infection and Immunity 62(12) (1994) 5424-5433
  

  The galactomannan (GM) produced extracellularly by Aspergillus fumigatus has been purified by a double sequential hydrazine-nitrous acid treatment of the ethanol precipitate of the culture filtrate. Nuclear magnetic resonance and gas-liquid chromatography-mass spectrometry analysis have been performed on intact GM, acid-hydrolyzed GM, and oligomers resulting from the acetolysis of the acid-hydrolyzed GM. Results show that A. fumigatus GM is composed of a linear mannan core with an α-(1-2)-linked mannotetraose repeating unit attached via α-(1-6) linkage. Side chains composed of an average of 4 to 5 β-(1-5)-galactofuranose units are linked to C-6 and C-3 positions of α-(1-2)-linked mannose units of the mannan. The immunoreactivity of GM and HCl- hydrolyzed GM was studied by use of human sera from aspergillosis patients and an antigalactofuran monoclonal antibody. The α-(1-2)(1-6)-mannan core is not antigenic. The immunogenic galactofuran is found amongst several exocellular glycoproteins. According to a direct enzyme-linked immunosorbent assay with GM as the detector antigen, only 26% of the serum samples from aspergilloma patients (all positive by immunodiffusion assays) give optical density values superior to a cutoff estimated as the mean ±3 standard deviations of values obtained with control sera.

  immunogenicity, Galactomannan, Aspergillus fumigatus, aspergilloma

  NCBI PubMed ID: 7960122
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Institutions: Unite de Mycologie, Institut Pasteur, Paris, France, Laboratoire de Chimie Biologie, Universite des Sciences et Technologies de Lille, d'Ascq Cedex, Angers, France, Laboratoire de Parasitologie-Mycologie, Centre Hospitalier Regional, Angers, France, Grupo de Carbohidratos, Instituto de Quimica Organica, Consejo Superior de Investigaciones Cientificas, Madrid, Spain
  Methods: gel filtration, 13C NMR, 1H NMR, methylation, GLC-MS, ELISA, acid hydrolysis, amino acid analysis, electrophoresis, HPLC, immunoblotting, extraction, periodate oxidation, acetylation, hydrazinolysis, reduction, cell growth, phenol-sulfuric acid assay, ethanol precipitation, ultrasonication, phosphate determination
  
   
  
  Aspergillus fumigatus CBS 143-89
  CSDB ID 44113 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: galactomannan
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_137472,IEDB_144983,IEDB_147453,IEDB_149137,IEDB_152206,IEDB_190606,IEDB_885812,IEDB_983930,SB_44,SB_67,SB_72

• Article ID: 7477
  Paulovičová E, Paulovičová L, Hrubiško M, Krylov VB, Argunov DA, Nifantiev NE "Immunobiological Activity of Synthetically Prepared Immunodominant Galactomannosides Structurally Mimicking Aspergillus Galactomannan" - Frontiers in Immunology 8 (2017) 1273
  

  The study is oriented at the in vitro evaluation of the immunobiological activity and efficacy of synthetically prepared isomeric pentasaccharides representing fragments of Aspergillus fumigatus cell-wall galactomannan and containing β-(1→5)-linked tetragalactofuranoside chain attached to O-6 (GM-1) or O-3 (GM-2) of a spacer-armed mannopyranoside residue. These compounds were studied as biotinylated conjugates which both demonstrated immunomodulatory activities on the RAW 264.7 cell line murine macrophages as in vitro innate immunity cell model. Immunobiological studies revealed time- and concentration-dependent efficient immunomodulation. The proliferation of RAW 264.7 macrophages was induced at higher concentration (100 µg/mL) of studied glycoconjugates and longer exposure (48 h), with more pronounced efficacy for GM-1. The increase of proliferation followed the previous increase of IL-2 production. The cytokine profile of the macrophages treated with the glycoconjugates was predominantly pro-inflammatory Th1 type with significant increase of TNFα, IL-6, and IL-12 release for both glycoconjugates. The RAW 264.7 macrophages production of free radicals was not significantly affected by glycoconjugates stimulation. The phagocytic activity of RAW 264.7 cells was reduced following GM-1 treatment and was significantly increased after 24 h stimulation with GM-2, contrary to 48 h stimulation. Moreover, the synthetically prepared galactomannoside derivatives have been evaluated as efficient serodiagnostic antigens recognized by specific Ig isotypes, and significant presence of specific IgM antibodies in serum of patients suffering from vulvovaginitis was observed.

  mannan, Galactomannan, cytokines, Candida, Aspergillus, RAW 264.7

  NCBI PubMed ID: 29081774
  Publication DOI: 10.3389/fimmu.2017.01273
  Journal NLM ID: 101560960
  Publisher: Lausanne: Frontiers Research Foundation
  Correspondence: Paulovičová E ; Nifantiev NE
  Institutions: N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, Department of Immunochemistry of Glycoconjugates, Center for Glycomics, Institute of Chemistry, Slovak Academy of Sciences, Bratislava, Slovakia, Department of Clinical Immunology and Allergy, Oncology Institute of St. Elisabeth, Bratislava, Slovakia
  
   
  
  Aspergillus fumigatus
  CSDB ID 43025 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure ; n=16, 29000
Compound class: EPS, galactomannan
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_136104,IEDB_137472,IEDB_140116,IEDB_141793,IEDB_141795,IEDB_141830,IEDB_141834,IEDB_143632,IEDB_144983,IEDB_147453,IEDB_149137,IEDB_152206,IEDB_153220,IEDB_164480,IEDB_190606,IEDB_76933,IEDB_885812,IEDB_983930,SB_136,SB_196,SB_198,SB_44,SB_67,SB_72

• Article ID: 5307
  Liu J, Wang X, Pu H, Liu S, Kan J, Jin C "Recent advances in endophytic exopolysaccharides: Production, structural characterization, physiological role and biological activity" - Carbohydrate Polymers 157 (2017) 1113-1124
  

  Endophytes are microorganisms that colonize living, internal tissues of plants without causing any immediate, overt negative effects. In recent years, both endophytic bacteria and fungi have been demonstrated to be excellent exopolysaccharides (EPS) producers. This review focuses on the recent advances in EPS produced by endophytes, including its production, isolation and purification, structural characterization, physiological role and biological activity. In general, EPS production is influenced by media components and cultivation conditions. The structures of purified EPS range from linear homopolysaccharides to highly branched heteropolysaccharides. These structurally novel EPS not only play important roles in plant-endophyte interactions; but also exhibit several biological functions, such as antioxidant, antitumor, anti-inflammatory, anti-allergic and prebiotic activities. In order to utilize endophytic EPS on an industrial scale, both yield and productivity enhancement strategies are required at several levels. Besides, the exact mechanisms on the physiological roles and biological functions of EPS should be elucidated in future.

  exopolysaccharides, biological activity, Structural characterization, endophytes, physiological role

  NCBI PubMed ID: 27987813
  Publication DOI: 10.1016/j.carbpol.2016.10.084
  Journal NLM ID: 8307156
  Publisher: Elsevier
  Correspondence: junliu@yzu.edu.cn
  Institutions: College of Food Science and Engineering, Yangzhou University, Yangzhou, China
  
   
  
  Aspergillus ochraceus
  CSDB ID 43158 (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 ; 1257 (Hex5HexNAc2), 1419 (Hex6HexNAc2), 1581 (Hex7HexNAc2), 1743 (Hex8HexNAc2), 1905 (Hex9HexNAc2), 2067 (Hex10HexNAc2), 2229 (Hex11HexNAc2)
Compound class: N-glycan, galactomannan
Contained glycoepitopes: IEDB_123886,IEDB_130701,IEDB_135813,IEDB_136095,IEDB_136104,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141795,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_143632,IEDB_144983,IEDB_147453,IEDB_149137,IEDB_149176,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153220,IEDB_164174,IEDB_164480,IEDB_187201,IEDB_190606,IEDB_423157,IEDB_429156,IEDB_548907,IEDB_76933,IEDB_857734,IEDB_885812,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_33,SB_44,SB_53,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85

• Article ID: 7555
  Morelle W, Bernard M, Debeaupuis JP, Buitrago M, Tabouret M, Latge JP "Galactomannoproteins of Aspergillus fumigatus" - Eukaryotic Cell 4(7) (2005) 1308-1316
  

  Galactofuranose-containing molecules have been repeatedly shown to be important antigens among human fungal pathogens, including Aspergillus fumigatus. Immunogenic galactofuran determinants have been poorly characterized chemically, however. We reported here the characterization of two glycoproteins of A. fumigatus with an N-glycan containing galactofuranose. These proteins are a phospholipase C and a phytase. Chemical characterization of the N-glycan indicates that it is a mixture of Hex(5-13)HexNAc(2) oligosaccharides, the major molecular species corresponding to Hex(6-8)HexNAc(2). The N-glycan contained one galactofuranose unit that was in a terminal nonreducing position attached to the 2 position of Man. This single terminal nonreducing galactofuranose is essential for the immunoreactivity of the N-glycans assessed either with a monoclonal antibody that recognizes a tetra-β-1,5-galactofuran chain of galactomannan or with Aspergillus-infected patient sera.

  NCBI PubMed ID: 16002656
  Publication DOI: 10.1128/EC.4.7.1308-1316.2005
  Journal NLM ID: 101130731
  Publisher: American Society for Microbiology
  Correspondence: jplatge@pasteur.fr
  Institutions: Unité des Aspergillus, Institut Pasteur, Paris, France, Bio-Rad, Clinical Microbiology Division, Steenvoorde, France
  Methods: GC-MS, GLC, methylation analysis, TFA hydrolysis, MALD-MS
  
   
  
  Aspergillus fumigatus CBS 144-89
  CSDB ID 44556 (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)

Show legend Show as text

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

• 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: 25643073
  Publication DOI: 10.1039/c4ob02634a
  Journal NLM ID: 101154995
  Publisher: 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
  
   
  
  Aspergillus fumigatus
  CSDB ID 42336 (all data & tools)

Show legend Show as text

Structure type: oligomer ; 886.3396 [M+H]+
C₃₃H₅₈NO₂₆
Compound class: galactomannan
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_137472,IEDB_144983,IEDB_147453,IEDB_149137,IEDB_152206,IEDB_190606,IEDB_885812,IEDB_983930,SB_44,SB_67,SB_72

• 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: 25643073
  Publication DOI: 10.1039/c4ob02634a
  Journal NLM ID: 101154995
  Publisher: 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
  
   
  
  Aspergillus fumigatus
  CSDB ID 42337 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure ; 29000, n=16
Compound class: galactomannan
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_136104,IEDB_137472,IEDB_140116,IEDB_141793,IEDB_141795,IEDB_141830,IEDB_141834,IEDB_143632,IEDB_144983,IEDB_147453,IEDB_149137,IEDB_152206,IEDB_153220,IEDB_164480,IEDB_190606,IEDB_76933,IEDB_885812,IEDB_983930,SB_136,SB_196,SB_198,SB_44,SB_67,SB_72

• Article ID: 8002
  Guo S, Mao W, Yan M, Zhao C, Li N, Shan J, Lin C, Liu X, Guo T, Wang S "Galactomannan with novel structure produced by the coral endophytic fungus Aspergillus ochraceus" - Carbohydrate Polymers 105 (2014) 325–333
  

  The homogeneous extracellular polysaccharide, AW1, was obtained from the fermented broth of the fungus Aspergillus ochraceus derived from coral Dichotella gemmacea. AW1 was a galactomannan with a molar ratio of mannose and galactose of 2.16:1.00 and a molecular weight of about 29.0kDa. The structure of AW1 was investigated by chemical and spectroscopic methods, including methylation analysis, one- and two-dimensional nuclear magnetic resonance (1D, 2D NMR) and electrospray mass spectrometry with collision-induced dissociation (ES-CID MS/MS) spectroscopic analyses. The results showed that the backbone of AW1 consisted of (1⟶2)-linked α-d-mannopyranose residues. The mannopyranose residues in the backbone were substituted at C-6 by the (1⟶)-linked α-d-mannopyranose units and (1⟶5)-linked β-D-galactofuranose oligosaccharides with different degrees of polymerization. The investigation demonstrated that AW1 was a novel galactomannan with different structural characteristics from other fungal galactomannans, and could be a potential resource of the (1⟶5)-linked β-D-galactofuranose oligosaccharides.

  NMR, extracellular polysaccharide, Aspergillus ochraceus, ES-CID MS/MS, galacto-oligosaccharide

  NCBI PubMed ID: 24708987
  Publication DOI: 10.1016/j.carbpol.2014.01.079
  Journal NLM ID: 8307156
  Publisher: Elsevier
  Correspondence: Mao W
  Institutions: Key Laboratory of Marine Drugs, Ministry of Education, School of Medicine and Pharmacy, Ocean University of China, Qingdao, China, Key Laboratory of Atherosclerosis in Universities of Shandong Province, Institute of Atherosclerosis, Taishan Medical University, Taian, Shandong, China
  Methods: 13C NMR, 1H NMR, IR, GC-MS, ESI-MS/MS, GC, HPLC, FPLC, methylation analysis, reduction with NaBH4, HPGPC, phenol-sulfuric acid assay, HMBC, Bradford method, HMQC, DEPT, COSY, NOESY, HCl hydrolysis, ES-MS, TFA hydrolysis, ES-CID MS/MS, HP-TLC, Hakamori method
  
   
  
  Aspergillus ochraceus
  CSDB ID 47455 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_137472,IEDB_144983,IEDB_147453,IEDB_149137,IEDB_152206,IEDB_190606,IEDB_885812,IEDB_983930,SB_44,SB_67,SB_72

• Article ID: 8227
  Kudoh A, Okawa Y, Shibata N "Significant structural change in both O- and N-linked carbohydrate moieties of the antigenic galactomannan from Aspergillus fumigatus grown under different culture conditions" - Glycobiology 25(1) (2015) 74-87
  

  Invasive aspergillosis is an important cause of morbidity and mortality in immunocompromised patients. Diagnosis of this infection frequently employs detection of the circulating galactomannan in the patient serum using enzyme immunoassay (EIA), a highly sensitive and specific system. Although there are many structural studies of the galactomannan of Aspergillus fumigatus, some inconsistencies are present in these results. In this study, to clarify the relationship between the growth conditions and structure of the galactomannans, we cultured A. fumigatus using two distinct yeast/fungal cultivation media, i.e. the yeast extract-peptone-dextrose (YPD) medium and yeast nitrogen base (YNB) medium. Galactomannans prepared from the resulting culture supernatants were structurally characterized by 1H and 13C nuclear magnetic resonance, methylation analysis, acetolysis and α-mannosidase degradation. These assays revealed that the galactomannan from the YPD cultivation had short β-1,5-linked galactofuranose (Galf) oligosaccharide chains in both the O- and N-linked carbohydrate moieties, while the galactomannan from the YNB cultivation incorporated long Galf oligosaccharide chains. The galactomannans derived from the two culture conditions significantly differed in reactivity based on the EIA diagnostic system. We also demonstrated the presence of a novel Galf-containing branched oligosaccharide in the O-linked moiety

  NMR, antigen, oligosaccharide, Galactomannan, Aspergillus

  NCBI PubMed ID: 25187160
  Publication DOI: 10.1093/glycob/cwu091
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Correspondence: nshibata@tohoku-pharm.ac.jp
  Institutions: Department of Infection and Host Defense, Tohoku Pharmaceutical University, Sendai, Japan, The Sendai Open Hospital, Sendai, Japan
  Methods: 13C NMR, 1H NMR, NMR-2D, GC-MS, enzyme immunoassay, acid hydrolysis, alkaline hydrolysis, enzymatic digestion, acetylation, acetolysis, methylation analysis, reduction, column chromatography, gel permeation chromatography, cell growth, dialysis, enzymatic assay, precipitation, evaporation, DEPT
  
   
  
  Aspergillus fumigatus NBRC 33022
  CSDB ID 48318 (all data & tools)