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

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 p...

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Autor principal: Dautin, Nathalie
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3153244/
https://www.ncbi.nlm.nih.gov/pubmed/22069633
http://dx.doi.org/10.3390/toxins2061179
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author Dautin, Nathalie
author_facet Dautin, Nathalie
author_sort Dautin, Nathalie
collection PubMed
description 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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spelling pubmed-31532442011-11-08 Serine Protease Autotransporters of Enterobacteriaceae (SPATEs): Biogenesis and Function Dautin, Nathalie Toxins (Basel) Review 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. MDPI 2010-05-28 /pmc/articles/PMC3153244/ /pubmed/22069633 http://dx.doi.org/10.3390/toxins2061179 Text en © 2010 by the authors; licensee MDPI, Basel, Switzerland http://creativecommons.org/licenses/by/3.0/ 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/).
spellingShingle Review
Dautin, Nathalie
Serine Protease Autotransporters of Enterobacteriaceae (SPATEs): Biogenesis and Function
title Serine Protease Autotransporters of Enterobacteriaceae (SPATEs): Biogenesis and Function
title_full Serine Protease Autotransporters of Enterobacteriaceae (SPATEs): Biogenesis and Function
title_fullStr Serine Protease Autotransporters of Enterobacteriaceae (SPATEs): Biogenesis and Function
title_full_unstemmed Serine Protease Autotransporters of Enterobacteriaceae (SPATEs): Biogenesis and Function
title_short Serine Protease Autotransporters of Enterobacteriaceae (SPATEs): Biogenesis and Function
title_sort serine protease autotransporters of enterobacteriaceae (spates): biogenesis and function
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3153244/
https://www.ncbi.nlm.nih.gov/pubmed/22069633
http://dx.doi.org/10.3390/toxins2061179
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