Molecular mimicry of host structures by bacterial lipopolysaccharides and its contribution to disease
Moran, Anthony P. Prendergast, Martina M. Appelmelk, Ben J.
Moran, Anthony P.
Prendergast, Martina M.
Appelmelk, Ben J.
Publication Date
1996-12-01
Keywords
neisseria spp, haemophilus influenzae, campylobacter jejuni, helicobacter pylori, lipopolysaccharide, molecular mimicry, guillain-barre syndrome, guillain-barre-syndrome, neisseria-gonorrhoeae lipooligosaccharides, campylobacter-jejuni lipopolysaccharides, n-acetylneuraminic acid, helicobacter-pylori, haemophilus-ducreyi, igg antibodies, lewis-x, human glycosphingolipids, core oligosaccharides
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Article
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Citation
Moran, Anthony P. Prendergast, Martina M.; Appelmelk, Ben J. (1996). Molecular mimicry of host structures by bacterial lipopolysaccharides and its contribution to disease. FEMS Immunology & Medical Microbiology 16 (2), 105-115
Abstract
The core oligosaccharides of low-molecular-weight lipopolysaccharide (LPS), also termed lipooligosaccharide (LOS), of pathogenic Neisseria spp. mimic the carbohydrate moieties of glycosphingolipids present on human cells. Such mimicry may serve to camouflage the bacterial surface from the host. The LOS component is antigenically and/or chemically identical to lactoneoseries glycosphingolipids and can become sialylated in Neisseria gonorrhoeae when the bacterium is grown in the presence of cytidine 5'-monophospho-N-acetylneuraminic acid, the nucleotide sugar of sialic acid. Strains of Neisseria meningitidis and Haemophilus influenzae also express similarly sialylated LPS. Sialylation of the LOS influences susceptibility to bactericidal antibody, may decrease or prevent phagocytosis, cause down-regulation of complement activation, and decrease adherence to neutrophils and the subsequent oxidative burst response. The core oligosaccharides of LPS of Campylobacter jejuni serotypes which are associated with the development of the neurological disorder, Guillain-Barre syndrome (GBS), exhibit mimicry of gangliosides. Cross-reactive antibodies between C. jejuni LPS and gangliosides are considered to play an important role in GBS pathogenesis. In contrast, the O-chain of a number of Helicobacter pylori strains exhibit mimicry of Lewis(x) and Lewis(y) blood group antigens. The role of this mimicry remains to be investigated, but may play a role in bacterial camouflage, the induction of autoimmunity and immune suppression in H. pylori-associated disease.
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Publisher
Oxford University Press (OUP)
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Attribution-NonCommercial-NoDerivs 3.0 Ireland