Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_135813,IEDB_137340,IEDB_141807,IEDB_144993,IEDB_144997,IEDB_151531,IEDB_534865

• Article ID: 4253
  De Libero G, Mori L "Self glycosphingolipids: new antigens recognized by autoreactive T lymphocytes" - News in Physiological Sciences 18 (2003) 71-76
  

  T cells may recognize glycolipids and lipids of bacterial and self origin associated with the CD1 antigen-presenting molecules. Understanding the mechanisms governing CD1-self glycolipid interaction will provide information on the molecular rules of glycolipid presentation and suggest new approaches to immunotherapy

  genetics, molecular, antigens, immunology, review, lipids, glycosphingolipids, glycolipids, models, CD1, glycosphingolipid, physiology, Animals, Humans, Autoantigens, Antigen-Presenting Cells, Autoimmune Diseases, Autoimmunity, Immunotherapy, Lymphocytes, T-Lymphocytes

  NCBI PubMed ID: 12644623
  Journal NLM ID: 8609378
  Publisher: Bethesda, MD: International Union of Physiological Sciences and the American Physiological Society
  Institutions: Experimental Immunology, Department of Research, University Hospital, Basel, CH-4031 Basel, Switzerland
  
   
  
  Mycobacterium tuberculosis
  CSDB ID 14506 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130701,IEDB_136104,IEDB_137340,IEDB_1394182,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141829,IEDB_141830,IEDB_141832,IEDB_143632,IEDB_144983,IEDB_144993,IEDB_144997,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_474450,IEDB_76933,IEDB_983930,SB_136,SB_191,SB_196,SB_198,SB_44,SB_67,SB_72

• Article ID: 6775
  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
  CSDB ID 40524 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130701,IEDB_136104,IEDB_140116,IEDB_140425,IEDB_140426,IEDB_141793,IEDB_141807,IEDB_141829,IEDB_141830,IEDB_141832,IEDB_143632,IEDB_144983,IEDB_144993,IEDB_144997,IEDB_145015,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_474450,IEDB_76933,IEDB_983930,SB_136,SB_191,SB_196,SB_198,SB_44,SB_67,SB_72

• Article ID: 7252
  Flury I, Benachour A, Conzelmann A "YLL031c belongs to a novel family of membrane proteins involved in the transfer of ethanolaminephosphate onto the core structure of glycosylphosphatidylinositol anchors in yeast" - Journal of Biological Chemistry 275(32) (2000) 24458-24465
  

  MCD4 and GPI7 are important for the addition of glycosylphosphatidylinositol (GPI) anchors to proteins in the yeast Saccharomyces cerevisiae. Mutations in these genes lead to a reduction of GPI anchoring and cell wall fragility. Gpi7 mutants accumulate a GPI lipid intermediate of the structure Manα1-2[NH2-(CH2)2-PO4]Man-α1-2Manα1-6[NH2-(CH2)2-PO4] Manα1-4GlcNα1-6 [acyl]inositol-PO4-lipid, which, in comparison with the complete GPI precursor lipid CP2, lacks an HF-sen-sitive side chain on the α1-6-linked mannose. In contrast, mcd4-174 accumulates only minor amounts of abnormal GPI intermediates. Here we investigate whether YLL031c, an open reading frame predicting a further homologue of GPI7 and MCD4, plays any role in GPI anchoring. YLL031c is an essential gene. Its depletion results in a reduction of GPI anchor addition to GPI proteins as well as to cell wall fragility. YLL031c-depleted cells accumulate GPI intermediates with the structures Manα1-2Manα1-2Manα1-6[NH2-(CH2)2-PO4]Manα1-4GlcNα1-6[a cyl]inositol-PO4-lipid and Manα1-2Manα1-2Manα1-6Manα1-4GlcNα1-6[acyl] inositol-PO4-lipid. Subcellular localization studies of a tagged version of YLL031c suggest that this protein is mainly in the ER, in contrast to Gpi7p, which is found at the cell surface. The data are compatible with the idea that YLL031c transfers the ethanolaminephosphate to the inner α1-2-linked mannose, i.e. the group that links the GPI lipid anchor to proteins, whereas Mcd4p and Gpi7p transfer ethanolaminephosphate onto the α1-4- and α1-6-linked mannoses of the GPI anchor, respectively.

  proteins, glycosylphosphatidylinositols, Saccharomyces cerevisiae, anchor biosynthesis

  NCBI PubMed ID: 10823837
  Publication DOI: 10.1074/jbc.M003844200
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: andreas.conzelmann@unifr.ch
  Institutions: Institute of Biochemistry, University of Fribourg, Fribourg, Switzerland
  Methods: PCR, DNA techniques, dephosphorylation, TLC, Western blotting, paper chromatography, radiolabeling, radioactivity measurement, alkaline deacylation, enzymatic digestion, biosynthetic methods, extraction, acetylation, cell growth, hydrolysis
  
   
  
  Saccharomyces cerevisiae
  CSDB ID 43943 (all data & tools)
• Article ID: 7253
  Benachour A, Sipos G, Flury I, Reggiori F, Canivenc-Gansel E, Vionnet C, Conzelmann A, Benghezal M "Deletion of GPI7, a yeast gene required for addition of a side chain to the glycosylphosphatidylinositol (GPI) core structure, affects GPI protein transport, remodeling, and cell wall integrity" - Journal of Biological Chemistry 274(21) (1999) 15251-15261
  

  Gpi7 was isolated by screening for mutants defective in the surface expression of glycosylphosphatidylinositol (GPI) proteins. Gpi7 mutants are deficient in YJL062w, herein named GPI7. GPI7 is not essential, but its deletion renders cells hypersensitive to Calcofluor White, indicating cell wall fragility. Several aspects of GPI biosynthesis are disturbed in Δgpi7. The extent of anchor remodeling, i.e. replacement of the primary lipid moiety of GPI anchors by ceramide, is significantly reduced, and the transport of GPI proteins to the Golgi is delayed. Gpi7p is a highly glycosylated integral membrane protein with 9-11 predicted transmembrane domains in the C-terminal part and a large, hydrophilic N-terminal ectodomain. The bulk of Gpi7p is located at the plasma membrane, but a small amount is found in the endoplasmic reticulum. GPI7 has homologues in Saccharomyces cerevisiae, Caenorhabditis elegans, and man, but the precise biochemical function of this protein family is unknown. Based on the analysis of M4, an abnormal GPI lipid accumulating in gpi7, we propose that Gpi7p adds a side chain onto the GPI core structure. Indeed, when compared with complete GPI lipids, M4 lacks a previously unrecognized phosphodiester-linked side chain, possibly an ethanolamine phosphate. Gpi7p contains significant homology with phosphodiesterases suggesting that Gpi7p itself is the transferase adding a side chain to the α1,6-linked mannose of the GPI core structure.

  proteins, glycosylphosphatidylinositols, Saccharomyces cerevisiae, anchor biosynthesis

  NCBI PubMed ID: 10329735
  Publication DOI: 10.1074/jbc.274.21.15251
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: andreas.conzelmann@unifr.ch
  Institutions: Institute of Biochemistry, University of Fribourg, Fribourg, Switzerland, Lab. Microbiologie l'Environnement, IRBA, Université de Caen, Caen, France, c/o R.S. Fuller, Department of Biological Chemistry, University of Michigan Medical Center, Ann Arbor, USA, c/o H. Pelham, MRC, Laboratory of Molecular Biology, Cambridge, UK, Institute of Biochemistry, Fribourg, Switzerland, Plant Cell Biology, Res. School of Biological Sciences, Australian National University, Canberra, Australia
  Methods: PCR, DNA techniques, dephosphorylation, TLC, Western blotting, paper chromatography, radiolabeling, radioactivity measurement, alkaline deacylation, enzymatic digestion, biosynthetic methods, extraction, acetylation, cell growth, hydrolysis
  
   
  
  Saccharomyces cerevisiae
  CSDB ID 43944 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130701,IEDB_136104,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141829,IEDB_141830,IEDB_141832,IEDB_143632,IEDB_144983,IEDB_144993,IEDB_144997,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_474450,IEDB_76933,IEDB_983930,SB_136,SB_191,SB_196,SB_198,SB_44,SB_67,SB_72

• Article ID: 7254
  Imhof I, Flury I, Vionnet C, Roubaty C, Egger D, Conzelmann A "Glycosylphosphatidylinositol (GPI) proteins of saccharomyces cerevisiae contain ethanolamine phosphate groups on the α1,4-linked mannose of the GPI anchor" - Journal of Biological Chemistry 279(19) (2004) 19614-19627
  

  In humans and Saccharomyces cerevisiae the free glycosylphosphatidylinositol (GPI) lipid precursor contains several ethanolamine phosphate side chains, but these side chains had been found on the protein-bound GPI anchors only in humans, not yeast. Here we confirm that the ethanolamine phosphate side chain added by Mcd4p to the first mannose is a prerequisite for the addition of the third mannose to the GPI precursor lipid and demonstrate that, contrary to an earlier report, an ethanolamine phosphate can equally be found on the majority of yeast GPI protein anchors. Curiously, the stability of this substituent during preparation of anchors is much greater in gpi7A sec18 double mutants than in either single mutant or wild type cells, indicating that the lack of a substituent on the second mannose (caused by the deletion of GPI7) influences the stability of the one on the first mannose. The phosphodiester-linked substituent on the second mannose, probably a further ethanolamine phosphate, is added to GPI lipids by endoplasmic reticulum-derived microsomes in vitro but cannot be detected on GPI proteins of wild type cells and undergoes spontaneous hydrolysis in saline. Genetic manipulations to increase phosphatidylethanolamine levels in gpi7Δ cells by overexpression of PSD1 restore cell growth at 37 °C without restoring the addition of a substituent to Man2. The three putative ethanolamine-phosphate transferases Gpi13p, Gpi7p, and Mcd4p cannot replace each other even when overexpressed. Various models trying to explain how Gpi7p, a plasma membrane protein, directs the addition of ethanolamine phosphate to mannose 2 of the GPI core have been formulated and put to the test.

  proteins, glycosylphosphatidylinositols, Saccharomyces cerevisiae, anchor biosynthesis

  NCBI PubMed ID: 14985347
  Publication DOI: 10.1074/jbc.M401873200
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: andreas.conzelmann@unifr.ch
  Institutions: Department of Medicine, University of Fribourg, Fribourg, Switzerland, Division of Biochemistry, Fribourg, Switzerland
  Methods: PCR, DNA techniques, dephosphorylation, TLC, Western blotting, paper chromatography, radiolabeling, radioactivity measurement, alkaline deacylation, enzymatic digestion, biosynthetic methods, extraction, acetylation, cell growth, hydrolysis
  
   
  
  Saccharomyces cerevisiae
  CSDB ID 43945 (all data & tools)

Show legend Show as text

Structure type: oligomer ; 1160.2 [M+H]+
Aglycon: arabinogalactan protein (AGP)
Compound class: glycolipid, GPI-anchor
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130701,IEDB_134623,IEDB_136044,IEDB_136095,IEDB_136104,IEDB_137340,IEDB_137472,IEDB_140116,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141829,IEDB_143632,IEDB_144983,IEDB_144993,IEDB_144997,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_190606,IEDB_433717,IEDB_474450,IEDB_983930,SB_136,SB_165,SB_166,SB_187,SB_191,SB_195,SB_196,SB_198,SB_44,SB_67,SB_7,SB_72,SB_88

• Article ID: 11498
  Oxley D, Bacic A "Structure of the glycosylphosphatidylinositol anchor of an arabinogalactan protein from Pyrus communis suspension-cultured cells" - Proceedings of the National Academy of Sciences of the USA 96(25) (1999) 14246-14251
  

  Arabinogalactan proteins (AGPs) are proteoglycans of higher plants, which are implicated in growth and development. We recently have shown that two AGPs, NaAGP1 (from Nicotiana alata styles) and PcAGP1 (from Pyrus communis cell suspension culture), are modified by the addition of a glycosylphosphatidylinositol (GPI) anchor. However, paradoxically, both AGPs were buffer soluble rather than membrane associated. We now show that pear suspension cultured cells also contain membrane-bound GPI-anchored AGPs. This GPI anchor has the minimal core oligosaccharide structure, D-Manα(1-2)-D- Manα(1-6)-D-Manα(1-4)-D-GlcN-inositol, which is consistent with those found in animals, protozoa, and yeast, but with a partial β(1-4)-galactosyl substitution of the 6-linked Man residue, and has a phosphoceramide lipid composed primarily of phytosphingosine and tetracosanoic acid. The secreted form of PcAGP1 contains a truncated GPI lacking the phosphoceramide moiety, suggesting that it is released from the membrane by the action of a phospholipase D. The implications of these findings are discussed in relation to the potential mechanisms by which GPI-anchored AGPs may be involved in signal transduction pathways.

  proteoglycan, Glycosylphosphatidylinositol, arabinogalactan protein, Pyrus communis, GPI-anchor

  NCBI PubMed ID: 10588691
  Publication DOI: 10.1073/pnas.96.25.14246
  Journal NLM ID: 7505876
  Publisher: National Academy of Sciences
  Correspondence: Oxley D
  Institutions: Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Victoria 3010, Australia
  Methods: GC-MS, HF solvolysis, dephosphorylation, ESI-MS, alkaline hydrolysis, enzymatic digestion, periodate oxidation, hydrazinolysis, nitrous deamination, RP-HPLC, fluorescent labeling, trimethylsilylation, HCl methanolysis, permanganate oxidation
  
   
  
  Pyrus communis
  CSDB ID 63042 (all data & tools)