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Ecotin: A versatile protease inhibitor of bacteria and eukaryotes

Serine protease inhibitors are a large family of proteins involved in important pathways and processes, such as inflammatory responses and blood clotting. Most are characterized by a precise mode of action, thereby targeting a narrow range of protease substrates. However, the serine-protease inhibit...

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Detalles Bibliográficos
Autores principales: De Meyer, Frédéric, Carlier, Aurélien
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9904509/
https://www.ncbi.nlm.nih.gov/pubmed/36760512
http://dx.doi.org/10.3389/fmicb.2023.1114690
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author De Meyer, Frédéric
Carlier, Aurélien
author_facet De Meyer, Frédéric
Carlier, Aurélien
author_sort De Meyer, Frédéric
collection PubMed
description Serine protease inhibitors are a large family of proteins involved in important pathways and processes, such as inflammatory responses and blood clotting. Most are characterized by a precise mode of action, thereby targeting a narrow range of protease substrates. However, the serine-protease inhibitor ecotin is able to inhibit a broad range of serine proteases that display a wide range of specificities. This specificity is driven by special structural features which allow unique flexibility upon binding to targets. Although frequently observed in many human/animal-associated bacteria, ecotin homologs may also be found in plant-associated taxa and environmental species. The purpose of this review is to provide an update on the biological importance, role in host–microbe interactions, and evolutionary relationship between ecotin orthologs isolated from Eukaryotic and Prokaryotic species across the Tree of Life.
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spelling pubmed-99045092023-02-08 Ecotin: A versatile protease inhibitor of bacteria and eukaryotes De Meyer, Frédéric Carlier, Aurélien Front Microbiol Microbiology Serine protease inhibitors are a large family of proteins involved in important pathways and processes, such as inflammatory responses and blood clotting. Most are characterized by a precise mode of action, thereby targeting a narrow range of protease substrates. However, the serine-protease inhibitor ecotin is able to inhibit a broad range of serine proteases that display a wide range of specificities. This specificity is driven by special structural features which allow unique flexibility upon binding to targets. Although frequently observed in many human/animal-associated bacteria, ecotin homologs may also be found in plant-associated taxa and environmental species. The purpose of this review is to provide an update on the biological importance, role in host–microbe interactions, and evolutionary relationship between ecotin orthologs isolated from Eukaryotic and Prokaryotic species across the Tree of Life. Frontiers Media S.A. 2023-01-24 /pmc/articles/PMC9904509/ /pubmed/36760512 http://dx.doi.org/10.3389/fmicb.2023.1114690 Text en Copyright © 2023 De Meyer and Carlier. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Microbiology
De Meyer, Frédéric
Carlier, Aurélien
Ecotin: A versatile protease inhibitor of bacteria and eukaryotes
title Ecotin: A versatile protease inhibitor of bacteria and eukaryotes
title_full Ecotin: A versatile protease inhibitor of bacteria and eukaryotes
title_fullStr Ecotin: A versatile protease inhibitor of bacteria and eukaryotes
title_full_unstemmed Ecotin: A versatile protease inhibitor of bacteria and eukaryotes
title_short Ecotin: A versatile protease inhibitor of bacteria and eukaryotes
title_sort ecotin: a versatile protease inhibitor of bacteria and eukaryotes
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9904509/
https://www.ncbi.nlm.nih.gov/pubmed/36760512
http://dx.doi.org/10.3389/fmicb.2023.1114690
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