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

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

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

Publication types

  • Review

MeSH terms

  • Animals
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Bacterial Toxins / chemistry
  • Bacterial Toxins / genetics
  • Bacterial Toxins / metabolism*
  • Escherichia coli*
  • Humans
  • Protein Structure, Tertiary
  • Protein Transport
  • Serine Proteases / chemistry
  • Serine Proteases / genetics
  • Serine Proteases / metabolism*
  • Shigella flexneri*

Substances

  • Bacterial Proteins
  • Bacterial Toxins
  • Serine Proteases