Human Monoclonal Immunoglobulin M Antibodies to Ganglioside GM1 Show Diverse Cross-Reactivities with Lipopolysaccharides of Campylobacter jejuni Strains Associated with Guillain-Barré Syndrome
AUTOR(ES)
Prendergast, Martina M.
FONTE
American Society for Microbiology
RESUMO
We examined the reactivity of a panel of anti-GM1 immunoglobulin M monoclonal antibodies (MAbs) cloned from multifocal motor neuropathy patients with lipopolysaccharides (LPSs) of Campylobacter jejuni strains, including serotype O:41 strains associated with Guillain-Barré syndrome. The MAbs reacted with ganglioside GM1 to different degrees, and these differences in fine specificities for GM1 were reflected in the different degrees of reactivity with each of the C. jejuni LPSs tested. Antibodies could also be discriminated by the varying patterns of inhibition by cholera toxin (a GM1 ligand) in LPS binding studies. These results indicate that there is a substantial heterogeneity among C. jejuni O:41 strains in their expression of GM1-like epitopes and among the fine specificities of different neuropathy-associated anti-GM1 antibodies.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=116569Documentos Relacionados
- Lipopolysaccharides from Campylobacter jejuni O:41 Strains Associated with Guillain-Barré Syndrome Exhibit Mimicry of GM1 Ganglioside
- Carbohydrate mimicry between human ganglioside GM1 and Campylobacter jejuni lipooligosaccharide causes Guillain–Barré syndrome
- Lipopolysaccharides from Campylobacter jejuni associated with Guillain-Barré syndrome patients mimic human gangliosides in structure.
- Monoclonal antibodies raised against Guillain-Barré syndrome–associated Campylobacter jejuni lipopolysaccharides react with neuronal gangliosides and paralyze muscle-nerve preparations
- Monoclonal antibodies raised against Guillain-Barré syndrome–associated Campylobacter jejuni lipopolysaccharides react with neuronal gangliosides and paralyze muscle-nerve preparations