Toxins 2010, 2(6), 1179-1206; doi:10.3390/toxins2061179
Review

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

Received: 2 April 2010; in revised form: 17 May 2010 / Accepted: 27 May 2010 / Published: 28 May 2010
(This article belongs to the Special Issue Protein Toxins as Proteases)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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.
Keywords: SPATE; autotransporters; pathogenic E. coli; Shigella;EspP; Pet; EspC; Sat; Vat; Hbp; EpeA; Pic; SepA; SigA; Tsh
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MDPI and ACS Style

Dautin, N. Serine Protease Autotransporters of Enterobacteriaceae (SPATEs): Biogenesis and Function. Toxins 2010, 2, 1179-1206.

AMA Style

Dautin N. Serine Protease Autotransporters of Enterobacteriaceae (SPATEs): Biogenesis and Function. Toxins. 2010; 2(6):1179-1206.

Chicago/Turabian Style

Dautin, Nathalie. 2010. "Serine Protease Autotransporters of Enterobacteriaceae (SPATEs): Biogenesis and Function." Toxins 2, no. 6: 1179-1206.

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