Serine Protease Autotransporters of Enterobacteriaceae (SPATEs) Biogenesis and Function 英文参考文献.docVIP

Toxins 2010, 2, 1179-1206; doi:10.3390/toxins2061179 OPEN ACCESS toxins ISSN 2072-6651 /journal/toxins Review Serine Protease Autotransporters of Enterobacteriaceae (SPATEs): Biogenesis and Function Nathalie Dautin Department of Biology, The Catholic University of America, 620 Michigan Avenue N.E., Washington, DC, 20064, USA; E-Mail: dautin@; Tel.: +1-202-319-5278; Fax: +1-202-319-5721 Received: 2 April 2010; in revised form: 17 May 2010 / Accepted: 27 May 2010 / Published: 28 May 2010 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 1. Introduction 1.1. The Autotransporter Pathway SPATE (Serine Protease Autotransporters of Enterobactericeae) is a family of extracellular proteases produced by the Enterobacteriaceae. As their name indicates, they are “autotransporters” (ATs), meaning they are secreted by the Type Va secretion system from gram-negative bacteria. ATs are very diverse in their function (adhesin, protease, esterase, lipase, etc.) [1], but it is assumed that they share the same export mechanism. They are recognized based on their common organization: they are comprised of an N-terminal, sec-dependent, signal-peptide required for targeting to- and expo