Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_135614,IEDB_141806,IEDB_142488,IEDB_146664,IEDB_153543,IEDB_241101,IEDB_983931,SB_192

• Article ID: 6867
  Magnelli P, Cipollo JF, Abeijon C "A refined method for the determination of Saccharomyces cerevisiae cell wall composition and beta-1,6-glucan fine structure" - Analytical Biochemistry 301 (2002) 136-150
  

  In yeast and other fungi, cell division, cell shape, and growth depend on the coordinated synthesis and degradation of cell wall polymers. We have developed a reliable and efficient micro method to determine Saccharomyces cerevisiae cell wall composition that distinguishes between β1,3- and β1,6-glucan. The method is based on the sequential treatment of cell walls with specific hydrolytic enzymes followed by dialysis. The low molecular weight (MW) products thus separated account for each particular cell wall polymer. The method can be applied to as little as 50-100 mg (wet wt) of radioactively labeled cells. A combination of chitinase and recombinant β-1,3-glucanase is initially used, releasing all of the chitin and 60-65% of the β1,3-glucan from the cell walls. Next, recombinant endo-β-1,6-glucanase from Trichoderma harzianum is utilized to release all the β-1,6-glucan present in the wall. The chromatographic pattern of endoglucanase digested β-1,6-glucan provides a characteristic 'fingerprint' of β-1,6-glucan and the fine structure of the oligosaccharides in this pattern was determined by 1H NMR and electrospray ionization mass spectroscopy. The final enzymatic step uses laminarinase and β-glucosidase to release the remaining β-1,3-glucan. The cell wall mannan remains as a high MW fraction at the end of the fractionation procedure. Good sensitivity and correlation with cell wall composition determined by traditional methods were observed for wild-type and several cell wall mutants.

  yeast cell wall, glycosydic linkage, beta-1, 6-glucan branch point

  Publication DOI: 10.1006/abio.2001.5473
  Journal NLM ID: 0370535
  Publisher: Academic Press
  Institutions: Department of Molecular and Cell Biology, Boston University Goldman School of Dental Medicine, Boston, Massachusetts 02118, USA
  Methods: 1H NMR, TLC, ESI-MS, acid hydrolysis, radiolabeling, enzymatic digestion, methylation analysis, gel filtration chromatography, DQF-COSY, ion exchange chromatography, alkali extraction, acid extraction
  
   
  
  Saccharomyces cerevisiae SEY6210
  CSDB ID 40567 (all data & tools)

Show legend Show as text

Structure type: homopolymer
Trivial name: R-glucan
Contained glycoepitopes: IEDB_135614,IEDB_1397514,IEDB_140628,IEDB_141806,IEDB_142488,IEDB_146664,IEDB_153543,IEDB_158555,IEDB_161166,IEDB_2278476,IEDB_2278477,IEDB_241101,IEDB_558869,IEDB_857743,IEDB_983931,SB_192

• Article ID: 6918
  Bartnicki-García S "Glucans, walls, and morphogenesis: On the contributions of J. G. H. Wessels to the golden decades of fungal physiology and beyond" - Fungal Genetics and Biology 27 (1999) 119-127
  

  This is a collection of impressions on the career of J. G. H. Wessels and his work in the areas of cell wall metabolism and apical morphogenesis. It highlights the finding of massive cell wall glucan metabolism during differentiation, the discovery of covalent linkages between wall polymers, the changes in chemical and physical properties of the wall at the fungal apex, and the steady-state model for tip growth. A tandem VSC-SS model for hyphal morphogenesis is proposed that combines the spatial control of wall synthesis provided by the vesicle supply center model with the temporal regulation intrinsic in Wessels's steady-state model.

  Publication DOI: 10.1006/fgbi.1999.1144
  Journal NLM ID: 9607601
  Publisher: Orlando, FL : Academic Press / Elsevier
  Correspondence: bart@citrus.ucr.edu
  Institutions: Department of Plant Pathology, University of California, Riverside, California 92521-0122, USA
  
   
  
  Schizophyllum commune
  CSDB ID 40853 (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: oligomer
Contained glycoepitopes: IEDB_115576,IEDB_130701,IEDB_134620,IEDB_136095,IEDB_136104,IEDB_137472,IEDB_1394182,IEDB_1397514,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_142488,IEDB_143632,IEDB_144983,IEDB_146664,IEDB_147454,IEDB_152206,IEDB_153220,IEDB_153543,IEDB_153756,IEDB_153762,IEDB_153763,IEDB_158555,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164480,IEDB_174840,IEDB_190606,IEDB_2278476,IEDB_241100,IEDB_76933,IEDB_983930,IEDB_983931,SB_136,SB_191,SB_192,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72,SB_77

• Article ID: 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 40706 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Contained glycoepitopes: IEDB_114708,IEDB_1397514,IEDB_141806,IEDB_142488,IEDB_146664,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 40707 (all data & tools)

Show legend Show as text

Structure type: homopolymer
Contained glycoepitopes: IEDB_135614,IEDB_141806,IEDB_142488,IEDB_146664,IEDB_241101,IEDB_983931,SB_192

• Article ID: 6944
  Klis FM, de Groot P, Hellingwerf K "Molecular organization of the cell wall of Candida albicans" - Medical Mycology 39 (2001) 1-8
  

  We have recently presented a molecular model of the cell wall of Saccharomyces cerevisiae. Here we discuss the evidence that a similar model is also valid for Candida albicans. We further discuss how cell-wall proteins are linked to the skeletal layer of the wall, and their potential functions. We emphasize that the composition and structure of the cell wall depends on growth conditions. Finally, cell-wall damage seems to activate a salvage mechanism resulting in restructuring of the cell wall.

  cell-wall dynamics, GPI proteins, Pir proteins

  Publication DOI: 10.1080/mmy.39.1.1.8-0
  Journal NLM ID: 9815835
  Publisher: Oxford: Oxford University Press
  Correspondence: klis@science.uva.nl
  Institutions: Swammerdam Institute for Life Sciences, University of Amsterdam, Nieuwe Achtergracht 166, 1018 WV Amsterdam, The Netherlands
  
   
  
  Candida albicans, Saccharomyces cerevisiae
  CSDB ID 40515 (all data & tools)
• Article ID: 6953
  Richard M, de Groot P, Courtin O, Poulain D, Klis F, Gaillardin C "GPI7 affects cell-wall protein anchorage in Saccharomyces cerevisiae and Candida albicans" - Microbiology 148 (2002) 2125-2133
  

  Glycosylphosphatidylinositol (GPI)-anchoring represents a mechanism for attaching proteins to the cell surface of all eukaryotic cells. Two localizations of GPI proteins have been observed in the yeasts Saccharomyces cerevisiae and Candida albicans: plasma membrane and cell wall. The signals and the mechanisms involved in this differential targeting are presently not well understood. Here several cell-wall-related phenotypes of a gpi7/las21 deletion are described, where GPI7/LAS21 encodes a GPI-anchor-modifying activity. In both organisms, the structure and composition of the cell wall was modified, with a clear increase in chitin deposition. Cell-wall-targeted proteins accumulated in the growth medium, whereas the protein content of the cell wall decreased significantly, suggesting inefficiency of the covalent linkage. The level of plasma-membrane-targeted GPI proteins was not affected. Sequence analyses revealed that gene families involved in the addition of phosphoethanolamines to the core GPI anchor are highly conserved between eukaryotes, with the exception of the Gpi7 family which seems to be fungus-specific. These data are compatible with the notion that the phosphoethanolamine added by Gpi7 protein to the GPI anchor is a key factor in the covalent linkage of cell-wall proteins to fungal cell-wall components.

  Glycosylphosphatidylinositol, Pir proteins, Als proteins

  Journal NLM ID: 0376646
  WWW link: http://mic.sgmjournals.org/content/148/7/2125.abstract
  Publisher: Washington, DC: Kluwer Academic/Plenum Publishers
  Correspondence: richard@grignon.inra.fr
  Institutions: Laboratoire de Génétique Moléculaire et Cellulaire, Institut National Agronomique Paris-Grignon, UMR-INRA216, URA-CNRS1925, BP01, 78850 Thiverval-Grignon, France, Fungal Research Group, Swammerdam Institute for Life Sciences, University of Amsterdam, Nieuwe Achtergracht 166, 1018 WV Amsterdam, The Netherlands, Aventis Pharma, Romainville, France, Laboratoire de Mycologie Fondamentale et Appliquée, INSERM EPI 9915, Université de Lille II, Faculté de Médecine H. Warembourg, Pôle Recherche, Place Verdun, 59037 Lille Cedex, France
  Methods: acid hydrolysis, PAGE, Western blot, enzyme sensitivity assays, SDS hypersensitivity test, ioc-exchange chromatography
  
   
  
  Saccharomyces cerevisiae, Candida albicans
  CSDB ID 40757 (all data & tools)
• Article ID: 6954
  Chaffin WL, López-Ribot JL, Casanova M, Gozalbo D, Martínez JP "Cell wall and secreted proteins of Candida albicans: identification, function, and expression" - Microbiology and Molecular Biology Reviews: MMBR 62 (1998) 130-180
  

  The cell wall is essential to nearly every aspect of the biology and pathogenicity of Candida albicans. Although it was initially considered an almost inert cellular structure that protected the protoplast against osmotic offense, more recent studies have demonstrated that it is a dynamic organelle. The major components of the cell wall are glucan and chitin, which are associated with structural rigidity, and mannoproteins. The protein component, including both mannoprotein and nonmannoproteins, comprises some 40 or more moieties. Wall proteins may differ in their expression, secretion, or topological location within the wall structure. Proteins may be modified by glycosylation (primarily addition of mannose residues), phosphorylation, and ubiquitination. Among the secreted enzymes are those that are postulated to have substrates within the cell wall and those that find substrates in the extracellular environment. Cell wall proteins have been implicated in adhesion to host tissues and ligands. Fibrinogen, complement fragments, and several extracellular matrix components are among the host proteins bound by cell wall proteins. Proteins related to the hsp70 and hsp90 families of conserved stress proteins and some glycolytic enzyme proteins are also found in the cell wall, apparently as bona fide components. In addition, the expression of some proteins is associated with the morphological growth form of the fungus and may play a role in morphogenesis. Finally, surface mannoproteins are strong immunogens that trigger and modulate the host immune response during candidiasis

  Journal NLM ID: 9706653
  WWW link: http://mmbr.asm.org/content/62/1/130.long
  Publisher: Washington, DC: American Society for Microbiology
  Correspondence: micwlc@ttuhsc.edu
  Institutions: Department of Microbiology and Immunology, Texas Tech University Health Sciences Center, Lubbock, USA, Department of Medicine, University of Texas Health Science Center at San Antonio, San Antonio, Texas, USA, Departamento de Microbiologı́a y Ecologı́a, Facultad de Farmacia, Universitat de Valencia, Valencia, Spain
  
   
  
  Candida albicans
  CSDB ID 40759 (all data & tools)
• 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 40799 (all data & tools)

Show legend Show as text

Structure type: monomer ; 734.5 [M+Na]+
Trivial name: neogala sphingolipid, NGL1
Compound class: glycosphingolipid
Contained glycoepitopes: IEDB_137339,IEDB_142488,IEDB_146664,IEDB_983931,SB_192,SB_5

• Article ID: 7054
  Tani Y, Funatsu T, Ashida H, Ito M, Itonori S, Sugita M, Yamamoto K "Novel neogala-series glycosphingolipids with terminal mannose and glucose residues from Hirsutella rhossiliensis, an aureobasidin A-resistant ascomycete fungus" - Glycobiology 20(4) (2010) 433-441
  

  Hirsutella rhossiliensis, a nematophagous fungus belonging to the Ascomycota, is resistant to aureobasidin A (AbA). In this fungus, the biosynthetic pathway leading to mannosylinositolphosphoceramides, which is inhibited by AbA, was not detected. Instead, this fungus contains neutral complex glycosphingolipids (GSLs) and monoglycosylceramides. Except for monoglycosylceramides, neutral GSLs share a neogala-series core structure, Galβ1-6Galβ1-Cer. Among the GSLs of H. rhossiliensis, three novel GSLs with terminal Man and Glc residues on the sugar chain were elucidated. We analyzed GSL structure using compositional sugar, fatty acid, and sphingoid analyses, methylation analysis, matrix-assisted laser desorption ionization time-of-flight/mass spectrometry (MALDI-TOF MS), and (1)H nuclear magnetic resonance spectroscopy (NMR). The following structures were determined: Manα1-3Galβ1-6Galβ1-6Galβ1-Cer; Glcα1-2Galβ1-6Galβ1-6Galβ1-Cer; and Manα1-3Galβ1-6(Glcα1-4)Galβ1-6Galβ1-Cer. In the ceramides, the fatty acids were predominantly saturated h24:0-acids and the sphingoids were predominately t18:0- or t18:1-sphingoids. In contrast, the ceramides of Glcβ1-Cer contained d18:2- and d19:2-sphingoids. These findings indicate the presence of a novel biosynthetic pathway of neogala-series GSLs in fungi.

  glycosphingolipid, Aureobasidin A, Ascomycota, Hirsutella rhossiliensis, neogalatriaosylceramide

  NCBI PubMed ID: 20007186
  Publication DOI: 10.1093/glycob/cwp190
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Correspondence: yasu-t@lif.kyoto-u.ac.jp
  Institutions: Graduate School of Biostudies, Kyoto University, Kyoto, Japan, Department of Bioscience and Bioinformatics, Ritsumeikan University, Kusatsu, Shiga 525-8577, and Faculty of Liberal Arts and Education, Shiga University, Otsu, Japan
  Methods: 1H NMR, GC-MS, sugar analysis, TLC, GC, MALDI-TOF MS, enzymatic digestion, mild alkaline hydrolysis, methylation analysis
  
   
  
  Hirsutella rhossiliensis JCM 23109
  CSDB ID 41719 (all data & tools)

Show legend Show as text

Structure type: monomer ; 748.5 [M+Na]+
Trivial name: neogala sphingolipid, NGL1
Compound class: glycosphingolipid
Contained glycoepitopes: IEDB_137339,IEDB_142488,IEDB_146664,IEDB_983931,SB_192,SB_5

• Article ID: 7054
  Tani Y, Funatsu T, Ashida H, Ito M, Itonori S, Sugita M, Yamamoto K "Novel neogala-series glycosphingolipids with terminal mannose and glucose residues from Hirsutella rhossiliensis, an aureobasidin A-resistant ascomycete fungus" - Glycobiology 20(4) (2010) 433-441
  

  Hirsutella rhossiliensis, a nematophagous fungus belonging to the Ascomycota, is resistant to aureobasidin A (AbA). In this fungus, the biosynthetic pathway leading to mannosylinositolphosphoceramides, which is inhibited by AbA, was not detected. Instead, this fungus contains neutral complex glycosphingolipids (GSLs) and monoglycosylceramides. Except for monoglycosylceramides, neutral GSLs share a neogala-series core structure, Galβ1-6Galβ1-Cer. Among the GSLs of H. rhossiliensis, three novel GSLs with terminal Man and Glc residues on the sugar chain were elucidated. We analyzed GSL structure using compositional sugar, fatty acid, and sphingoid analyses, methylation analysis, matrix-assisted laser desorption ionization time-of-flight/mass spectrometry (MALDI-TOF MS), and (1)H nuclear magnetic resonance spectroscopy (NMR). The following structures were determined: Manα1-3Galβ1-6Galβ1-6Galβ1-Cer; Glcα1-2Galβ1-6Galβ1-6Galβ1-Cer; and Manα1-3Galβ1-6(Glcα1-4)Galβ1-6Galβ1-Cer. In the ceramides, the fatty acids were predominantly saturated h24:0-acids and the sphingoids were predominately t18:0- or t18:1-sphingoids. In contrast, the ceramides of Glcβ1-Cer contained d18:2- and d19:2-sphingoids. These findings indicate the presence of a novel biosynthetic pathway of neogala-series GSLs in fungi.

  glycosphingolipid, Aureobasidin A, Ascomycota, Hirsutella rhossiliensis, neogalatriaosylceramide

  NCBI PubMed ID: 20007186
  Publication DOI: 10.1093/glycob/cwp190
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Correspondence: yasu-t@lif.kyoto-u.ac.jp
  Institutions: Graduate School of Biostudies, Kyoto University, Kyoto, Japan, Department of Bioscience and Bioinformatics, Ritsumeikan University, Kusatsu, Shiga 525-8577, and Faculty of Liberal Arts and Education, Shiga University, Otsu, Japan
  Methods: 1H NMR, GC-MS, sugar analysis, TLC, GC, MALDI-TOF MS, enzymatic digestion, mild alkaline hydrolysis, methylation analysis
  
   
  
  Hirsutella rhossiliensis JCM 23109
  CSDB ID 42149 (all data & tools)