Toxins 2010, 2(6), 1179-1206; doi:10.3390/toxins2061179
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Serine Protease Autotransporters of Enterobacteriaceae (SPATEs): Biogenesis and Function

Department of Biology, The Catholic University of America, 620 Michigan Avenue N.E., Washington, DC, 20064, USA
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)
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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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