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

      review-article
      Toxins
      MDPI
      SPATE, autotransporters, pathogenic E. coli, Shigella, EspP, Pet, EspC, Sat, Vat, Hbp, EpeA, Pic, SepA, SigA, Tsh

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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.

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          Most cited references88

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          Role of a highly conserved bacterial protein in outer membrane protein assembly.

          After transport across the cytoplasmic membrane, bacterial outer membrane proteins are assembled into the outer membrane. Meningococcal Omp85 is a highly conserved protein in Gram-negative bacteria, and its homolog Toc75 is a component of the chloroplast protein-import machinery. Omp85 appeared to be essential for viability, and unassembled forms of various outer membrane proteins accumulated upon Omp85 depletion. Immunofluorescence microscopy revealed decreased surface exposure of outer membrane proteins, which was particularly apparent at the cell-division planes. Thus, Omp85 is likely to play a role in outer membrane protein assembly.
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            Enteropathogenic Escherichia coli contains a putative type III secretion system necessary for the export of proteins involved in attaching and effacing lesion formation.

            Enteropathogenic Escherichia coli (EPEC) causes a characteristic histopathology in intestinal epithelial cells called the attaching and effacing lesion. Although the histopathological lesion is well described the bacterial factors responsible for it are poorly characterized. We have identified four EPEC chromosomal genes whose predicted protein sequences are similar to components of a recently described secretory pathway (type III) responsible for exporting proteins lacking a typical signal sequence. We have designated the genes sepA, sepB, sepC, and sepD (sep, for secretion of E. coli proteins). The predicted Sep polypeptides are similar to the Lcr (low calcium response) and Ysc (yersinia secretion) proteins of Yersinia species and the Mxi (membrane expression of invasion plasmid antigens) and Spa (surface presentation of antigens) regions of Shigella flexneri. Culture supernatants of EPEC strain E2348/69 contain several polypeptides ranging in size from 110 kDa to 19 kDa. Proteins of comparable size were recognized by human convalescent serum from a volunteer experimentally infected with strain E2348/69. A sepB mutant of EPEC secreted only the 110-kDa polypeptide and was defective in the formation of attaching and effacing lesions and protein-tyrosine phosphorylation in tissue culture cells. These phenotypes were restored upon complementation with a plasmid carrying an intact sepB gene. These data suggest that the EPEC Sep proteins are components of a type III secretory apparatus necessary for the export of virulence determinants.
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              The great escape: structure and function of the autotransporter proteins.

              The autotransporters, a family of secreted proteins from Gram-negative bacteria, possess an overall unifying structure comprising three functional domains: the amino-terminal leader sequence, the secreted mature protein (passenger domain) and a carboxy-terminal (beta-) domain that forms a beta-barrel pore to allow secretion of the passenger protein. Members of this family have been implicated as important or putative virulence factors in many Gram-negative pathogens.
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                Author and article information

                Journal
                Toxins (Basel)
                toxins
                Toxins
                MDPI
                2072-6651
                28 May 2010
                June 2010
                : 2
                : 6
                : 1179-1206
                Affiliations
                Department of Biology, The Catholic University of America, 620 Michigan Avenue N.E., Washington, DC, 20064, USA; Email: dautin@ 123456cua.edu ; Tel.: +1-202-319-5278; Fax: +1-202-319-5721
                Article
                toxins-02-01179
                10.3390/toxins2061179
                3153244
                22069633
                ef07ca8e-0a2d-4424-b731-597fbcd282cd
                © 2010 by the authors; licensee MDPI, Basel, Switzerland

                This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/3.0/).

                History
                : 02 April 2010
                : 17 May 2010
                : 27 May 2010
                Categories
                Review

                Molecular medicine
                spate,autotransporters,pathogenic e. coli,shigella,espp,pet,espc,sat,vat,hbp,epea,pic,sepa,siga,tsh
                Molecular medicine
                spate, autotransporters, pathogenic e. coli, shigella, espp, pet, espc, sat, vat, hbp, epea, pic, sepa, siga, tsh

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