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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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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2010
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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. |
format | Online Article Text |
id | pubmed-3153244 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT dautinnathalie serineproteaseautotransportersofenterobacteriaceaespatesbiogenesisandfunction |