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Serine Protease Autotransporters of Enterobacteriaceae (SPATEs): Biogenesis and Function

Author(s): Nathalie Dautin

Journal: Toxins
ISSN 2072-6651

Volume: 2;
Issue: 6;
Start page: 1179;
Date: 2010;
Original page

Keywords: SPATE | autotransporters | pathogenic E. coli | Shigella;EspP | Pet | EspC | Sat | Vat | Hbp | EpeA | Pic | SepA | SigA | Tsh

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.