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Serine protease autotransporters of enterobacteriaceae (SPATEs): biogenesis and function.

ABSTRACT: Serine Protease Autotransporters of Enterobacteriaceae (SPATEs) constitute a large family of proteases secreted by Escherichia coli and Shigella. SPATEs exhibit two distinct proteolytic activities. First, a C-terminal catalytic site triggers an intra-molecular cleavage that releases the N-terminal portion of these proteins in the extracellular medium. Second, the secreted N-terminal domains of SPATEs are themselves proteases; each contains a canonical serine-protease catalytic site. Some of these secreted proteases are toxins, eliciting various effects on mammalian cells. Here, we discuss the biogenesis of SPATEs and their function as toxins.

SUBMITTER: Dautin N

PROVIDER: S-EPMC3153244 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature

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Serine protease autotransporters of enterobacteriaceae (SPATEs): biogenesis and function.

Dautin Nathalie N

Toxins 20100528 6

Serine Protease Autotransporters of Enterobacteriaceae (SPATEs) constitute a large family of proteases secreted by Escherichia coli and Shigella. SPATEs exhibit two distinct proteolytic activities. First, a C-terminal catalytic site triggers an intra-molecular cleavage that releases the N-terminal portion of these proteins in the extracellular medium. Second, the secreted N-terminal domains of SPATEs are themselves proteases; each contains a canonical serine-protease catalytic site. Some of thes ...[more]

PMID: 22069633

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