Schwerer B, Neisser A, Polt RJ, Bernheimer H, Moran AP Antibody cross-reactivities between gangliosides and lipopolysaccharide of Campylobacter jejuni serotypes associated with Guillain-Barre syndrome Journal of Endotoxin Research2 (1995)
395-403
Publication DOI:10.1177/096805199600200602 Journal NLM ID:9433350 Publisher: Maney Publishing Institutions: Klinisches Institut fur Neurologie, University of Vienna, Vienna, Austria, Department of Microbiology, University College, Galwas, Ireland
Ganglioside-antibodies produced subsequent to Campylobacter jejuni infection may play a role in the pathogenesis of the neurological sidorder Guillain-Barre syndrome (GBS). Since lipopolysaccharides (LPS) of certain C. jejuni serotypes associated with GBS (O:2, O:4, O:19) exhibit structural mimicry of gangliosides in their core oligosaccharides, we investigated antibody and ligand cross-reactivities between gangliosides and LPS of thewe C. jejuni serotypes. GM1-antibody reacted with O:19 LPS reflecting GM1 mimicry by the O:19 core oligosaccharide. On the other hand, asialoGM1-antibody bound to O:2 and L:19 LPS indicating a shared epitope not dependent on ganglioside mimicry. Serum IgA from GBS patients after C. jejuni infection reacted with gangliosides, predominantly GM1, and LPS of all three serotypes. Cholera toxin (GM1 ligand) recognized O:4 and O:19 LPS, whereas peanut agglutinin (Galb(1-3)GalNAc Ligand) recognized LPS of all three serotypes, thereby confirming strucutral mimicry. These results suggest that LPS from certain C. jejuni strains may function as cross-reactive antigens for anti-ganglioside B cells.
Methods: TLC, serological methods Biological activity: serological data
Related record ID(s): 589, 8110, 8111, 9048, 124135 NCBI Taxonomy refs (TaxIDs):197 Reference(s) to other database(s): GTC:G33839QQ Show glycosyltransferases
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