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. 1982 May;36(2):615–620. doi: 10.1128/iai.36.2.615-620.1982

Degradation of intestinal glycoproteins by pathogenic Shigella flexneri.

R Prizont
PMCID: PMC351273  PMID: 6282754

Abstract

Intestinal mucin glycoproteins were examined for their ability to sustain growth of pathogenic shigella. Inoculation of germfree cecal mucin glycoproteins with Shigella flexneri 4b resulted at 48 h in a 940-fold increase in the enteropathogen concentration. Investigation in vitro of enzymatic degradation by the pathogen led to the identification of a blood group B-degrading glycosidase produced by the bacteria. In in vivo experiments, fecal supernatants of mice monocontaminated with S. flexneri 4b contained an alpha-galactosidase active against the p-nitrophenyl-glycoside. This fecal alpha-galactosidase peaked 5 days after shigella contamination, showing 2.8 +/- 1.4 mU of enzyme activity per mg of protein. Contaminated fecal supernatants similarly destroyed the blood group B reactivity of cecal mucin glycoproteins. These data suggested that S. flexneri 4b could proliferate within ileocolonic environment by enzymatically degrading mucin glycoprotein sugars.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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