Show legend Show as text

Structure type: oligomer
Trivial name: GPI
Contained glycoepitopes: IEDB_130701,IEDB_1394182,IEDB_141793,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_983930,SB_198,SB_44,SB_67,SB_72

• Article ID: 4265
  Ferguson MA "The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research" - Journal of Cell Science 112(17) (1999) 2799-2809
  

  The discovery of glycosylphosphatidylinositol (GPI) membrane anchors has had a significant impact on several areas of eukaryote cell biology. Studies of the African trypanosome, which expresses a dense surface coat of GPI-anchored variant surface glycoprotein, have played important roles in establishing the general structure of GPI membrane anchors and in delineating the pathway of GPI biosynthesis. The major cell-surface molecules of related parasites are also rich in GPI-anchored glycoproteins and/or GPI-related glycophospholipids, and differences in substrate specificity between enzymes of trypanosomal and mammalian GPI biosynthesis may have potential for the development of anti-parasite therapies. Apart from providing stable membrane anchorage, GPI anchors have been implicated in the sequestration of GPI-anchored proteins into specialised membrane microdomains, known as lipid rafts, and in signal transduction events.

  Glycosylphosphatidylinositol, Trypanosome, Lipid raft

  NCBI PubMed ID: 10444375
  Journal NLM ID: 0052457
  Publisher: Cambridge: Company of Biologists
  Correspondence: majferguson@bad.dundee.ac.uk
  Institutions: Division of Molecular Parasitology and Biological Chemistry, Department of Biochemistry, The Wellcome Trust Building, University of Dundee, Dundee DD1 5EH, UK.
  
   
  
  (protista)
  CSDB ID 11499 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: GPI type 2
Contained glycoepitopes: IEDB_130701,IEDB_1394182,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_164174,IEDB_983930,SB_197,SB_44,SB_67,SB_72

• Article ID: 4265
  Ferguson MA "The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research" - Journal of Cell Science 112(17) (1999) 2799-2809
  

  The discovery of glycosylphosphatidylinositol (GPI) membrane anchors has had a significant impact on several areas of eukaryote cell biology. Studies of the African trypanosome, which expresses a dense surface coat of GPI-anchored variant surface glycoprotein, have played important roles in establishing the general structure of GPI membrane anchors and in delineating the pathway of GPI biosynthesis. The major cell-surface molecules of related parasites are also rich in GPI-anchored glycoproteins and/or GPI-related glycophospholipids, and differences in substrate specificity between enzymes of trypanosomal and mammalian GPI biosynthesis may have potential for the development of anti-parasite therapies. Apart from providing stable membrane anchorage, GPI anchors have been implicated in the sequestration of GPI-anchored proteins into specialised membrane microdomains, known as lipid rafts, and in signal transduction events.

  Glycosylphosphatidylinositol, Trypanosome, Lipid raft

  NCBI PubMed ID: 10444375
  Journal NLM ID: 0052457
  Publisher: Cambridge: Company of Biologists
  Correspondence: majferguson@bad.dundee.ac.uk
  Institutions: Division of Molecular Parasitology and Biological Chemistry, Department of Biochemistry, The Wellcome Trust Building, University of Dundee, Dundee DD1 5EH, UK.
  
   
  
  Tetrahymena, Leishmania, Endotrypanum, Leptomonas, Crithidia
  CSDB ID 14499 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: GPI hybrid
Contained glycoepitopes: IEDB_130701,IEDB_1394182,IEDB_141793,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_983930,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73

• Article ID: 4265
  Ferguson MA "The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research" - Journal of Cell Science 112(17) (1999) 2799-2809
  

  The discovery of glycosylphosphatidylinositol (GPI) membrane anchors has had a significant impact on several areas of eukaryote cell biology. Studies of the African trypanosome, which expresses a dense surface coat of GPI-anchored variant surface glycoprotein, have played important roles in establishing the general structure of GPI membrane anchors and in delineating the pathway of GPI biosynthesis. The major cell-surface molecules of related parasites are also rich in GPI-anchored glycoproteins and/or GPI-related glycophospholipids, and differences in substrate specificity between enzymes of trypanosomal and mammalian GPI biosynthesis may have potential for the development of anti-parasite therapies. Apart from providing stable membrane anchorage, GPI anchors have been implicated in the sequestration of GPI-anchored proteins into specialised membrane microdomains, known as lipid rafts, and in signal transduction events.

  Glycosylphosphatidylinositol, Trypanosome, Lipid raft

  NCBI PubMed ID: 10444375
  Journal NLM ID: 0052457
  Publisher: Cambridge: Company of Biologists
  Correspondence: majferguson@bad.dundee.ac.uk
  Institutions: Division of Molecular Parasitology and Biological Chemistry, Department of Biochemistry, The Wellcome Trust Building, University of Dundee, Dundee DD1 5EH, UK.
  
   
  
  Tetrahymena, Leishmania, Endotrypanum, Leptomonas, Crithidia
  CSDB ID 15499 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit ; n=12-13
Compound class: teichoic acid
Contained glycoepitopes: IEDB_114703,IEDB_136105,IEDB_153532,IEDB_225177,IEDB_591403,IEDB_885823

• Article ID: 4451
  Naumova IB, Shashkov AS "Anionic polymers in cell walls of Gram-positive bacteria" - Biochemistry (Moscow) 62(8) (1997) 809-840
  

  Information on the prevalence, compositions, and structures of anionic carbohydrate-containing polymers of cell walls of Gram-positive bacteria is summarized. The data suggest that these polymers are important for normal functioning of bacterial cells and require further studies. Structural data on teichoic acids found in the literature published over the last few years are discussed. This is a very diverse class of polymers whose structure-specific pathways of degradation were studied and NMR spectra were examined. Unique comprehensive tables of 13C-NMR spectroscopic data (mainly obtained by the authors) on these polymers are given in the Appendix. Other tables summarize data on teichuronic acids, sugar-phosphate polymers, acid polysaccharides, and structural variants of bonds between acid polysaccharides and peptidoglycans known from the literature. Functions of anionic polymers and their possible chemotaxonomic applications are discussed

  13C-NMR, NMR, structure, cell wall, composition, teichoic acid, teichuronic acid, Gram-positive, gram-positive bacteria, taxonomy

  NCBI PubMed ID: 9360295
  Journal NLM ID: 0376536
  Publisher: Nauka/Interperiodica
  Institutions: School of Biology, Lomonosov Moscow State University, Russia
  
   
  
  Agromyces fucosus ssp. hippuratus VKM Ac-1352, Agromyces fucosus ssp. hippuratus VKM Ac-1353
  CSDB ID 29068 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_130701,IEDB_1394182,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_164174,IEDB_983930,SB_197,SB_44,SB_67,SB_72

• Article ID: 6913
  Toledo MS, Levery SB, Straus AH, Takahashi HK "Sphingolipids of the mycopathogen Sporothrix schenckii: identification of a glycosylinositol phosphorylceramide with novel core GlcNH2-α1→2Ins motif" - FEBS Letters 493 (2001) 50-56
  

  Acidic glycosphingolipid components were extracted from the yeast form of the dimorphic mycopathogen Sporothrix schenckii. Two minor and the major fraction from the yeast form (Ss-Y1, -Y2, and -Y6, respectively) have been isolated. By a combination of 1- and 2-D 1H-nuclear magnetic resonance (NMR) spectroscopy, electrospray ionization mass spectrometry (ESI-MS), and gas chromatography/mass spectrometry (GC/MS), Ss-Y6 was determined to be triglycosylinositol phosphorylceramide with a novel glycan structure, Man-α1→3Man-α1→6GlcNH2-α1→2Ins1-P-1Cer (where Ins=myo-inositol, P=phosphodiester). While the GlcNH2-α1→6Ins1-P- motif is found widely distributed in eukaryotic GPI anchors, the linkage GlcNH2-α1→2Ins1-P- has not been previously observed in any glycolipid. Ss-Y1 and Ss-Y2 were both found to have the known glycan structure Man-α1→3Man-α1→2Ins1-P-1Cer. Together with the results of a prior study [Toledo et al. (2001) Biochem. Biophys. Res. Commun. 280, 19-24] which showed that the mycelium form expresses GIPCs with the structures Man-α1→6Ins1-P-1Cer and Man-α1→3Man-α1→6Ins1-P-1Cer, these results demonstrate that S. schenckii can synthesize glycosylinositol phosphorylceramides with at least three different core linkages.

  mass spectrometry, nuclear magnetic resonance, glycolipid, sphingolipid, dimorphism, mycopathogen

  Publication DOI: 10.1016/S0014-5793(01)02275-X
  Journal NLM ID: 0155157
  Publisher: Elsevier
  Correspondence: leverysb@ccrc.uga.ed
  Institutions: Department of Biochemistry, Universidade Federal de São Paulo/Escola Paulista de Medicina, Rua Botucatu 862, 04023-900 São Paulo, SP, Brazil, Department of Biochemistry and Molecular Biology, and The Complex Carbohydrate Research Center, University of Georgia, 220 Riverbend Road, Athens, GA 30602, USA
  Methods: 1H NMR, GC-MS, ESI-MS, HPLC, ESI-CID-MS, TOCSY, CC, NOESY, acetylation analysis
  
   
  
  Sporothrix schenckii 65
  CSDB ID 40468 (all data & tools)

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_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_2278476,IEDB_2278477,IEDB_2278480,IEDB_232584,IEDB_232585,IEDB_2346541,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_4

• Article ID: 6927
  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: Thierry Fontaine
  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: 13C NMR, 1H NMR, GLC-MS, gel filtration, 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: 6940
  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_135813,IEDB_137340,IEDB_1397514,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_153543,IEDB_158555,IEDB_2278476,IEDB_983931,SB_192

• Article ID: 6927
  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: Thierry Fontaine
  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: 13C NMR, 1H NMR, GLC-MS, gel filtration, 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 40704 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_1397514,IEDB_141806,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_153543,IEDB_158555,IEDB_161166,IEDB_2278476,IEDB_2278477,IEDB_241101,IEDB_558869,IEDB_857743,IEDB_983931,SB_192

• Article ID: 6927
  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: Thierry Fontaine
  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: 13C NMR, 1H NMR, GLC-MS, gel filtration, 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 40705 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Compound class: N-glycan
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531

• Article ID: 6941
  Cutler JE "N-glycosylation of yeast, with emphasis on Candida albicans" - Medical Mycology 39 (2001) 75-86
  

  Fungal cell wall N-linked glycans have been studied most extensively in Saccharomyces cerevisiae and in Candida albicans. The glycans are located on the fungal cell surface in the form of phosphomannoprotein complexes and the amount of glycosylation is influenced both by genetics and environmental factors. The glycans, which are comprised mostly of mannan, are important in fungal-host interactions, as they make first contact with the immune system. Initial N-linked glycosylation events take place in the endoplasmic reticulum and are conserved throughout all eukaryotes, but yeasts are capable of additional glycosylation that may result in a glycan comprised of more than 200 mannose units. In C. albicans, the glycan can be delineated into an inner mannan core, which is similar to mammalian glycoproteins, an α-linked mannan backbone with α-oligomannosyl side chains, and β(1,2)-oligomannosides which are phosphodiester linked to the α-mannan. Both the β-oligomannosides, which make up the acid-labile part of the phosphomannan complex, and α-oligomannosides, which make up the acid-stable part of the complex, serve as adhesins in the attachment of C. albicans yeast cells to host splenic and lymph node macrophages. The β-oligomannosides can induce release of tumour necrosis factor (TNF)-α, and antibodies specific to certain β-oligomannosides enhance host resistance to various forms of candidiasis. The importance of the N-linked glycans in fungal-host interactions provides rationale for further studies, which may well lead to effective immunotherapeutic strategies for prevention and, possibly, treatment of disease.

  antibodies, vaccines, cell walls, fungi, N-glycans, mannoproteins, phosphomannoproteins

  Publication DOI: 10.1080/mmy.39.1.75.86
  Journal NLM ID: 9815835
  Publisher: Oxford: Oxford University Press
  Correspondence: jcutler@montana.edu
  Institutions: Department of Microbiology, Montana State University, Bozeman 59717, USA.
  
   
  
  Candida albicans
  CSDB ID 40721 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_137340,IEDB_137485,IEDB_1394182,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_983930,SB_197,SB_44,SB_67,SB_72

• Article ID: 6951
  Murakami K, Takeuchi K, Beppu T, Horinouchi S "Structure of asparagine-linked oligosaccharides of an aspartic proteinase from the zygomycete fungus Rhizomucor pusillus" - Microbiology 144 (1998) 1369-1374
  

  The zygomycete fungus Rhizomucor pusillus (previously called Mucor pusillus) secretes an aspartic proteinase containing two asparagine-linked, high-mannose type oligosaccharide chains at Asn79 and Asn188. For structural elucidation of the carbohydrate moieties, the protein was divided into two portions, an N-terminal portion containing Asn79 and a C-terminal portion containing Asn188, by a specific autocatalytic cleavage under alkaline conditions. Each of the asparagine-linked oligosaccharides was then released by peptide-N-glycosidase F digestion and pyridylaminated with a fluorescent reagent, 2-aminopyridine, at the reducing end. High-performance liquid chromatography analyses showed that the structure of the asparagine-linked oligosaccharide chain attached to residue Asn79 was Man5 GlcNAc2, and that bound to residue Asn188 was Man5 GlcNAc2 and Man5GlcNAc2. These observations suggest that the processing of mannose residues in asparagine-linked oligosaccharides in the Golgi apparatus of Rhizomucor resembles that in mammalian cells.

  asparagine-linked oligosaccharide, Rhizomucor pusillus, zygomycete, aspartic proteinase

  Publication DOI: 10.1099/00221287-144-5-1369
  Journal NLM ID: 0376646
  Publisher: Washington, DC: Kluwer Academic/Plenum Publishers
  Correspondence: asuhori@hongo.ecc.u-tokyo.ac.jp
  Institutions: Department of Biotechnology, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113, Japan
  Methods: acid hydrolysis, HPLC, pyridylamination, automated Edman degradation
  
   
  
  Rhizomucor pusillus IFO4578, Rhizomucor pusillus F27
  CSDB ID 40522 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_137340,IEDB_137485,IEDB_1394182,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_144983,IEDB_149158,IEDB_151531,IEDB_152206,IEDB_164174,IEDB_983930,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73,SB_77

• Article ID: 6951
  Murakami K, Takeuchi K, Beppu T, Horinouchi S "Structure of asparagine-linked oligosaccharides of an aspartic proteinase from the zygomycete fungus Rhizomucor pusillus" - Microbiology 144 (1998) 1369-1374
  

  The zygomycete fungus Rhizomucor pusillus (previously called Mucor pusillus) secretes an aspartic proteinase containing two asparagine-linked, high-mannose type oligosaccharide chains at Asn79 and Asn188. For structural elucidation of the carbohydrate moieties, the protein was divided into two portions, an N-terminal portion containing Asn79 and a C-terminal portion containing Asn188, by a specific autocatalytic cleavage under alkaline conditions. Each of the asparagine-linked oligosaccharides was then released by peptide-N-glycosidase F digestion and pyridylaminated with a fluorescent reagent, 2-aminopyridine, at the reducing end. High-performance liquid chromatography analyses showed that the structure of the asparagine-linked oligosaccharide chain attached to residue Asn79 was Man5 GlcNAc2, and that bound to residue Asn188 was Man5 GlcNAc2 and Man5GlcNAc2. These observations suggest that the processing of mannose residues in asparagine-linked oligosaccharides in the Golgi apparatus of Rhizomucor resembles that in mammalian cells.

  asparagine-linked oligosaccharide, Rhizomucor pusillus, zygomycete, aspartic proteinase

  Publication DOI: 10.1099/00221287-144-5-1369
  Journal NLM ID: 0376646
  Publisher: Washington, DC: Kluwer Academic/Plenum Publishers
  Correspondence: asuhori@hongo.ecc.u-tokyo.ac.jp
  Institutions: Department of Biotechnology, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113, Japan
  Methods: acid hydrolysis, HPLC, pyridylamination, automated Edman degradation
  
   
  
  Rhizomucor pusillus IFO4578, Rhizomucor pusillus F27
  CSDB ID 40753 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_1394182,IEDB_140116,IEDB_141807,IEDB_143632,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_983930,SB_136,SB_196,SB_197,SB_44,SB_67,SB_72

• Article ID: 6951
  Murakami K, Takeuchi K, Beppu T, Horinouchi S "Structure of asparagine-linked oligosaccharides of an aspartic proteinase from the zygomycete fungus Rhizomucor pusillus" - Microbiology 144 (1998) 1369-1374
  

  The zygomycete fungus Rhizomucor pusillus (previously called Mucor pusillus) secretes an aspartic proteinase containing two asparagine-linked, high-mannose type oligosaccharide chains at Asn79 and Asn188. For structural elucidation of the carbohydrate moieties, the protein was divided into two portions, an N-terminal portion containing Asn79 and a C-terminal portion containing Asn188, by a specific autocatalytic cleavage under alkaline conditions. Each of the asparagine-linked oligosaccharides was then released by peptide-N-glycosidase F digestion and pyridylaminated with a fluorescent reagent, 2-aminopyridine, at the reducing end. High-performance liquid chromatography analyses showed that the structure of the asparagine-linked oligosaccharide chain attached to residue Asn79 was Man5 GlcNAc2, and that bound to residue Asn188 was Man5 GlcNAc2 and Man5GlcNAc2. These observations suggest that the processing of mannose residues in asparagine-linked oligosaccharides in the Golgi apparatus of Rhizomucor resembles that in mammalian cells.

  asparagine-linked oligosaccharide, Rhizomucor pusillus, zygomycete, aspartic proteinase

  Publication DOI: 10.1099/00221287-144-5-1369
  Journal NLM ID: 0376646
  Publisher: Washington, DC: Kluwer Academic/Plenum Publishers
  Correspondence: asuhori@hongo.ecc.u-tokyo.ac.jp
  Institutions: Department of Biotechnology, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113, Japan
  Methods: acid hydrolysis, HPLC, pyridylamination, automated Edman degradation
  
   
  
  Rhizomucor pusillus IFO4578, Rhizomucor pusillus F27
  CSDB ID 40754 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_1394182,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_143632,IEDB_144983,IEDB_149158,IEDB_151531,IEDB_152206,IEDB_164174,IEDB_983930,SB_136,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73,SB_77

• Article ID: 6951
  Murakami K, Takeuchi K, Beppu T, Horinouchi S "Structure of asparagine-linked oligosaccharides of an aspartic proteinase from the zygomycete fungus Rhizomucor pusillus" - Microbiology 144 (1998) 1369-1374
  

  The zygomycete fungus Rhizomucor pusillus (previously called Mucor pusillus) secretes an aspartic proteinase containing two asparagine-linked, high-mannose type oligosaccharide chains at Asn79 and Asn188. For structural elucidation of the carbohydrate moieties, the protein was divided into two portions, an N-terminal portion containing Asn79 and a C-terminal portion containing Asn188, by a specific autocatalytic cleavage under alkaline conditions. Each of the asparagine-linked oligosaccharides was then released by peptide-N-glycosidase F digestion and pyridylaminated with a fluorescent reagent, 2-aminopyridine, at the reducing end. High-performance liquid chromatography analyses showed that the structure of the asparagine-linked oligosaccharide chain attached to residue Asn79 was Man5 GlcNAc2, and that bound to residue Asn188 was Man5 GlcNAc2 and Man5GlcNAc2. These observations suggest that the processing of mannose residues in asparagine-linked oligosaccharides in the Golgi apparatus of Rhizomucor resembles that in mammalian cells.

  asparagine-linked oligosaccharide, Rhizomucor pusillus, zygomycete, aspartic proteinase

  Publication DOI: 10.1099/00221287-144-5-1369
  Journal NLM ID: 0376646
  Publisher: Washington, DC: Kluwer Academic/Plenum Publishers
  Correspondence: asuhori@hongo.ecc.u-tokyo.ac.jp
  Institutions: Department of Biotechnology, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113, Japan
  Methods: acid hydrolysis, HPLC, pyridylamination, automated Edman degradation
  
   
  
  Rhizomucor pusillus IFO4578, Rhizomucor pusillus F27
  CSDB ID 40755 (all data & tools)

Show legend Show as text

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

• Article ID: 6963
  Hochstenbach F, Klis FM, van den Ende H, van Donselaar E, Peters PJ, Klausner RD "Identification of a putative alpha-glucan synthase essential for cell wall construction and morphogenesis in fission yeast" - Proceedings of the National Academy of Sciences of the USA 95 (1998) 9161-9166
  

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

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

Show legend Show as text

Structure type: oligomer
Aglycon: 2-aminopyridine
Trivial name: N-linked oligosaccharide
Contained glycoepitopes: IEDB_123886,IEDB_130701,IEDB_135813,IEDB_136104,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_1394182,IEDB_140116,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141830,IEDB_143632,IEDB_144983,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_190606,IEDB_540671,IEDB_548907,IEDB_983930,SB_136,SB_196,SB_197,SB_198,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85

• Article ID: 7045
  Ohashi T, Nakakita S, Sumiyoshi W, Takegawa K "Production of heterologous glycoproteins by a glycosylation-defective alg3och1 mutant of Schizosaccharomyces pombe" - Journal of Biotechnology 150(3) (2010) 348-356
  

  The early stages of N-linked glycosylation are highly conserved between fungal and mammalian cells. Such N-linked oligosaccharides are synthesized through the ordered assembly of a dolichyl pyrophosphate (Dol-PP)-linked Glc(3)Man(9)GlcNAc(2) structure by the sequential actions of several glycosyltransferases located in the endoplasmic reticulum (ER). Of the glycosyltransferase genes, Saccharomyces cerevisiae ALG3 has been identified to encode the Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol α1,3-mannosyltransferase, and an alg3 mutant has been shown to accumulate an Endo H-resistant M5B (Manα1,2-Manα1,2-Manα1,3(Manα1,6-)-Manβ1,4-GlcNAcβ1,4-GlcNAc) structure. Although Schizosaccharomyces pombe contains a homolog of the ALG3 gene (SPAC7D4.06c), the role of this gene in oligosaccharide biosynthesis is not at all clear. In this study, we deleted the alg3(+) gene in the och1Δ mutant and analyzed the detailed oligosaccharide structures in alg3Δoch1Δ double mutant. The oligosaccharides were prepared from cell-surface glycoproteins by hydrazinolysis and fluorescent labeling with 2-aminopyridine. The labeled oligosaccharides were analyzed by high performance liquid chromatography, in combination with sequential glycosidase digestion and methylation analysis. These analyses revealed that the N-linked oligosaccharides of S. pombe alg3Δoch1Δ cells mainly consisted of two or three α-galactose-capped M5B structures. Finally, western blot analysis of recombinant human transferrin suggested that heterologously expressed glycoproteins in alg3Δoch1Δ cells have Endo H-resistant N-linked oligosaccharide structures similar to those of alg3Δoch1Δ cell-surface glycoproteins.

  Schizosaccharomyces pombe, Alg3, Och1, N-Linked oligosaccharide, Galactosylation

  NCBI PubMed ID: 20854854
  Publication DOI: 10.1016/j.jbiotec.2010.09.942
  Journal NLM ID: 8411927
  Publisher: Amsterdam: Elsevier
  Correspondence: takegawa@agr.kyushu-u.ac.jp
  Institutions: Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University, Fukuoka, Japan, ASPEX Division, Research Center, Asahi Glass Co., Ltd., Yokohama, Japan, Division of Functional Glycomics, Life Science Research Center, Institute of Research Promotion, Kagawa University, Miki-cho, Japan, Division of Glyco-Bioindustry, Life Science Research Center, Institute of Research Promotion, Kagawa University, Miki-cho, Japan, Division of Functional Glycomics, Life Science Research Center, Institute of Research Promotion, Kagawa University, Kagawa, Japan, Division of Glyco-Bioindustry, Life Science Research Center, Institute of Research Promotion, Kagawa University, Kagawa, Japan, ASPEX Division, Research Center, Asahi Glass Co. Ltd., Yokohama, Japan
  Methods: methylation, SDS-PAGE, Western blotting, genetic methods, HPLC, enzymatic digestion, microscopy, N-acetylation, hydrazinolysis, cell growth, fluorescence microscopy, derivatization, evaporation, single-step gene disruption, fluorescent labeling with 2-aminopyridine
  
   
  
  Schizosaccharomyces pombe ARC039
  CSDB ID 41708 (all data & tools)