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Structure type: oligomer
Aglycon: lipid A
Compound class: LOS, LPS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_175430,IEDB_2189047,IEDB_226300,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_983931,SB_192

• Article ID: 107
  Tong YH, Reinhold V, Reinhold B, Brandt B, Stein DC "Structural and immunochemical characterization of the lipooligosaccharides expressed by Neisseria subflava 44" - Journal of Bacteriology 183(3) (2001) 942-950
  

  Neisserial lipooligosaccharides (LOSs) are a family of complex cell surface glycolipids. We used mass spectrometry techniques (electrospray ionization, collision-induced dissociation, and multiple step), combined with fluorophore-assisted carbohydrate electrophoresis monosaccharide composition analysis, to determine the structure of the two low-molecular-mass LOS molecules (LOSI and LOSII) expressed by Neisseria subflava 44. We determined that LOSI contains one glucose on both the alpha and beta chains. LOSII is structurally related to LOSI and differs from it by the addition of a hexose (either glucose or galactose) on the alpha chain. LOSI and LOSII were able to bind monoclonal antibody (MAb) 25-1-LC1 when analyzed by Western blotting experiments. We used a set of genetically defined Neisseria gonorrhoeae mutants that expressed single defined LOS epitopes and a group of Neisseria meningitidis strains that expresses chemically defined LOS components to determine the structures recognized by MAb 25-1-LC1. We found that extensions onto the beta-chain glucose of LOSI block the recognition by this MAb, as does further elongation from the LOSII alpha chain. The LOSI structure was determined to be the minimum structure that is recognized by MAb 25-1-LC1.

  Lipooligosaccharide, Neisseria, structural, characterization, immunochemical, lipooligosaccharides

  NCBI PubMed ID: 11208793
  Journal NLM ID: 2985120R
  Publisher: American Society for Microbiology
  Correspondence: DS64@UMAIL.UMD.EDTJ
  Institutions: Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, Maryland 20742
  Methods: ESI-MS, CID-MS/MS, FACE
  
   
  
  Neisseria meningitidis F62 lgtA lgtE
  CSDB ID 5392 (all data & tools)
• Article ID: 3964
  Wenzel CQ, St-Michael F, Stupak J, Li J, Cox AD, Richards JC "Functional characterization of Lpt3 and Lpt6, the inner-core lipooligosaccharide phosphoethanolamine transferases from Neisseria meningitidis" - Journal of Bacteriology 192(1) (2010) 208-216
  

  The lipooligosaccharide (LOS) of Neisseria meningitidis contains heptose (Hep) residues that are modified with phosphoethanolamine (PEtn) at the 3 (3-PEtn) and/or 6 (6-PEtn) position. The lpt3 (NMB2010) and lpt6 (NMA0408) genes of N. meningitidis, which are proposed to encode the required HepII 3- and 6-PEtn transferases, respectively, were cloned and overexpressed as C-terminally polyhistidine-tagged fusion proteins in Escherichia coli and found to localize to the inner membrane, based on sucrose density gradient centrifugation. Lpt3-His(6) and Lpt6-His(6) were purified from Triton X-100-solubilized membranes by nickel chelation chromatography, and dot blot analysis of enzymatic reactions with 3-PEtn- and 6-PEtn-specific monoclonal antibodies demonstrated conclusively that Lpt3 and Lpt6 are phosphatidylethanolamine-dependent LOS Hep.

  lipopolysaccharides, Neisseria meningitidis, gene, Escherichia coli, antibodies, inner core, Ethanolaminephosphotransferase

  NCBI PubMed ID: 19854897
  Journal NLM ID: 2985120R
  Publisher: American Society for Microbiology
  Correspondence: Cory.Wenzel@nrc-cnrc.gc.ca
  Institutions: Institute for Biological Sciences, 100 Sussex Drive, National Research Council, Ottawa, ON, Canada K1A 0R6
  Methods: DNA techniques, genetic methods, CE-MS
  
   
  
  Neisseria meningitidis MC58 (galE)
  CSDB ID 25884 (all data & tools)