Adhesin degradation accelerates delivery of heat-labile toxin by enterotoxigenic Escherichia coli

Koushik Roy, Rita Kansal, Scott R. Bartels, David J. Hamilton, Salwa Shaaban, James M. Fleckenstein

Research output: Contribution to journalArticlepeer-review

35 Scopus citations

Abstract

Many enteric pathogens, including enterotoxigenic Escherichia coli (ETEC), produce one or more serine proteases that are secreted via the autotransporter (or type V) bacterial secretion pathway. These molecules have collectively been referred to as SPATE proteins (serine protease autotransporter of the Enterobacteriaceae). EatA, an autotransporter previously identifiedinETEC, possessesafunctionalserineproteasemotifwithinits secreted amino-terminal passenger domain. Although this protein is expressed by many ETEC strains and is highly immunogenic, its precise function is unknown. Here, we demonstrate that EatA degrades a recently characterized adhesin, EtpA, resulting in modulation of bacterial adhesion and accelerated delivery of the heatlabile toxin, a principal ETEC virulence determinant. Antibodies raised against the passenger domain of EatA impair ETEC delivery of labile toxin to epithelial cells suggesting that EatA may be an effective target for vaccine development.

Original languageEnglish
Pages (from-to)29771-29779
Number of pages9
JournalJournal of Biological Chemistry
Volume286
Issue number34
DOIs
StatePublished - Aug 26 2011

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