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Toxins (Basel). 2010 Jun;2(6):1179-206. doi: 10.3390/toxins2061179. Epub 2010 May 28.

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

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  • 1Department of Biology, The Catholic University of America, 620 Michigan Avenue N.E., Washington, DC, 20064, USA.


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.


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

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