Enterotoxigenic escherichia coli secretes a highly conserved mucin-degrading metalloprotease to effectively engage intestinal epithelial cells

Qingwei Luo, Pardeep Kumar, Tim J. Vickers, Alaullah Sheikh, Warren G. Lewis, David A. Rasko, Jeticia Sistrunk, James M. Fleckenstein

Research output: Contribution to journalArticlepeer-review

105 Scopus citations

Abstract

Enterotoxigenic Escherichia coli (ETEC) is a leading cause of death due to diarrheal illness among young children in developing countries, and there is currently no effective vaccine. Many elements of ETEC pathogenesis are still poorly defined. Here we demonstrate that YghJ, a secreted ETEC antigen identified in immunoproteomic studies using convalescent patient sera, is required for efficient access to small intestinal enterocytes and for the optimal delivery of heat-labile toxin (LT). Furthermore, YghJ is a highly conserved metalloprotease that influences intestinal colonization of ETEC by degrading the major mucins in the small intestine, MUC2 and MUC3. Genes encoding YghJ and its cognate type II secretion system (T2SS), which also secretes LT, are highly conserved in ETEC and exist in other enteric pathogens, including other diarrheagenic E. coli and Vibrio cholerae bacteria, suggesting that this mucin-degrading enzyme may represent a shared virulence feature of these important pathogens.

Original languageEnglish
Pages (from-to)509-521
Number of pages13
JournalInfection and immunity
Volume82
Issue number2
DOIs
StatePublished - Feb 2014

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