Escherichia coli Serogroup O107/O117 Lipopolysaccharide Binds and Neutralizes Shiga Toxin 2
| Autor: | Colleen M. McGannon, Alison A. Weiss, Shantini D. Gamage |
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| Jazyk: | angličtina |
| Rok vydání: | 2004 |
| Předmět: |
Molecular Sequence Data
Receptors Cell Surface Biology medicine.disease_cause Shiga Toxin 1 Microbiology Shiga Toxin 2 Virulence factor chemistry.chemical_compound Shiga-like toxin fluids and secretions Chlorocebus aethiops medicine Escherichia coli Animals Molecular Biology Vero Cells Molecular Biology of Pathogens Toxin Trihexosylceramides O Antigens Shiga toxin AB5 toxin biology.organism_classification Enterobacteriaceae chemistry biology.protein Vero cell Protein Binding |
| Popis: | The AB 5 toxin Shiga toxin 2 (Stx2) has been implicated as a major virulence factor of Escherichia coli O157:H7 and other Shiga toxin-producing E. coli strains in the progression of intestinal disease to more severe systemic complications. Here, we demonstrate that supernatant from a normal E. coli isolate, FI-29, neutralizes the effect of Stx2, but not the related Stx1, on Vero cells. Biochemical characterization of the neutralizing activity identified the lipopolysaccharide (LPS) of FI-29, a serogroup O107/O117 strain, as the toxin-neutralizing component. LPSs from FI-29 as well as from type strains E. coli O107 and E. coli O117 were able bind Stx2 but not Stx1, indicating that the mechanism of toxin neutralization may involve inhibition of the interaction between Stx2 and the Gb 3 receptor on Vero cells. |
| Databáze: | OpenAIRE |
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