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Structure type: oligomer
Trivial name: lipid IV A
Compound class: glycolipid
Contained glycoepitopes: IEDB_135394,IEDB_137340,IEDB_141807,IEDB_151531

• Article ID: 5617
  Stead C, Tran A, Ferguson D Jr, McGrath S, Cotter R, Trent S "A novel 3-deoxy-D-manno-octulosonic acid (Kdo) hydrolase that removes the outer Kdo sugar of Helicobacter pylori lipopolysaccharide" - Journal of Bacteriology 187(10) (2005) 3374-3383
  

  The lipid A domain anchors lipopolysaccharide (LPS) to the outer membrane and is typically a disaccharide of glucosamine that is both acylated and phosphorylated. The core and O-antigen carbohydrate domains are linked to the lipid A moiety through the eight-carbon sugar 3-deoxy-D-manno-octulosonic acid known as Kdo. Helicobacter pylori LPS has been characterized as having a single Kdo residue attached to lipid A, predicting in vivo a monofunctional Kdo transferase (WaaA). However, using an in vitro assay system we demonstrate that H. pylori WaaA is a bifunctional enzyme transferring two Kdo sugars to the tetra-acylated lipid A precursor lipid IV(A). In the present work we report the discovery of a Kdo hydrolase in membranes of H. pylori capable of removing the outer Kdo sugar from Kdo2-lipid A. Enzymatic removal of the Kdo group was dependent upon prior removal of the 1-phosphate group from the lipid A domain, and mass spectrometric analysis of the reaction product confirmed the enzymatic removal of a single Kdo residue by the Kdo-trimming enzyme. This is the first characterization of a Kdo hydrolase involved in the modification of gram-negative bacterial LPS

  lipid A, Helicobacter pylori, Kdo hydrolase

  NCBI PubMed ID: 15866922
  Publication DOI: 10.1128/JB.187.10.3374-3383.2005
  Journal NLM ID: 2985120R
  Publisher: American Society for Microbiology
  Correspondence: trentms@mail.etsu.edu
  Institutions: Department of Pharmacology and Molecular Sciences, The Johns Hopkins University School of Medicine, Baltimore, USA, Department of Microbiology, J. H. Quillen College of Medicine, Johnson City, USA, East Tennessee State University Laboratory of Clinical Microbiology, Johnson City, USA
  Methods: PCR, DNA techniques, MALDI-TOF MS, biological assays, radiolabeling, radioactivity measurement, enzymatic digestion, cell growth, enzymatic assay, centrifugation
  
   
  
  Helicobacter pylori J99 ATCC 700824, Helicobacter pylori 26695 ATCC 700392
  CSDB ID 47787 (all data & tools)

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Structure type: monomer
Contained glycoepitopes: IEDB_130701,IEDB_1394182,IEDB_144983,IEDB_144993,IEDB_152206,IEDB_983930,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
  CSDB ID 40677 (all data & tools)