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Characterization of terminal NeuNAcalpha2-3Galbeta1-4GlcNAc sequence in lipooligosaccharides of Neisseria meningitidis.

Abstract
Group B and C Neisseria meningitidis are the major cause of meningococcal disease in the United States and in Europe. N . meningitidis lipooligosaccharide (LOS), a major surface antigen, can be divided into 12 immunotypes of which L1 through L8 were found among Group B and C organisms. Groups B and C but not Group A may sialylate their LOSs with N-acetylneuraminic acid (NeuNAc) at the nonreducing end because they synthesize CMP-NeuNAc. Using sialic acid-galactose binding lectins as probes in an ELISA format, six of the eight LOS immunotypes (L2, L3, L4, L5, L7, and L8) in Groups B and C bound specifically to Maackia amurensis leukoagglutinin (MAL), which recognizes NeuNAcalpha2-3Galbeta1-4GlcNAc/Glc sequence, but not to Sambucus nigra agglutinin, which binds NeuNAcalpha2-6Gal sequence. The combination of SDS-PAGE and MAL-blot analyses revealed that these six LOSs contained only the NeuNAcalpha2-3Galbeta1-4GlcNAc trisaccharide sequence in their 4.1 kDa LOS components, which have a common terminal lacto-N-neotetraose (LNnT, Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc) structure when nonsialylated as shown by previous studies. The LOS-lectin binding was abolished when the LOSs were treated with Newcastle disease viral neuraminidase which cleaves alpha2-->3 linked sialic acid. Methylation analysis of a representative LOS (L2) confirmed that NeuNAc is 2-->3 linked to Gal. Thus, these LOSs structurally mimic certain glycolipids, i.e., paragloboside (LNnT-ceramide) and sialylparagloboside and some glycoproteins in having LNnT and N-acetyllactosamine sequences, respectively, with or without alpha2-->3 linked NeuNAc. The molecular mimicry of the LOSs may play a role in the pathogenesis of N.meningitidis by assisting the organism to evade host immune defenses in man.
AuthorsC M Tsai, W H Chen, P A Balakonis
JournalGlycobiology (Glycobiology) Vol. 8 Issue 4 Pg. 359-65 (Apr 1998) ISSN: 0959-6658 [Print] England
PMID9499383 (Publication Type: Journal Article)
Chemical References
  • Antigens, Bacterial
  • Antigens, Surface
  • Lectins
  • Lipopolysaccharides
  • lipid-linked oligosaccharides
Topics
  • Antigens, Bacterial (chemistry)
  • Antigens, Surface (chemistry)
  • Binding Sites
  • Carbohydrate Conformation
  • Carbohydrate Sequence
  • Humans
  • Immunophenotyping
  • In Vitro Techniques
  • Lectins (metabolism)
  • Lipopolysaccharides (chemistry, immunology, metabolism)
  • Methylation
  • Molecular Mimicry
  • Molecular Sequence Data
  • Neisseria meningitidis (chemistry, immunology, pathogenicity)
  • Virulence (immunology)

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