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Bacterial matrix metalloproteases and serine proteases contribute to the extra-host inactivation of enteroviruses in lake water

Enteroviruses are ubiquitous contaminants of surface waters, yet their fate in presence of microbial congeners is poorly understood. In this work, we investigated the inactivation of Echovirus-11 (E11) and Coxsackievirus-A9 (CVA9) by bacteria isolated from Lake Geneva. Incubation of E11 or CVA9 in b...

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Autores principales: Corre, Marie-Hélène, Bachmann, Virginie, Kohn, Tamar
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9296489/
https://www.ncbi.nlm.nih.gov/pubmed/35545659
http://dx.doi.org/10.1038/s41396-022-01246-3
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author Corre, Marie-Hélène
Bachmann, Virginie
Kohn, Tamar
author_facet Corre, Marie-Hélène
Bachmann, Virginie
Kohn, Tamar
author_sort Corre, Marie-Hélène
collection PubMed
description Enteroviruses are ubiquitous contaminants of surface waters, yet their fate in presence of microbial congeners is poorly understood. In this work, we investigated the inactivation of Echovirus-11 (E11) and Coxsackievirus-A9 (CVA9) by bacteria isolated from Lake Geneva. Incubation of E11 or CVA9 in biologically active lake water caused inactivation of 2- and 4-log(10), respectively, within 48 h. To evaluate the antiviral action of individual bacterial species, we isolated 136 bacterial strains belonging to 31 genera from Lake Geneva. The majority of isolates (92) induced decay of at least 1.5-log(10) of CVA9, whereas only 13 isolates induced a comparable inactivation on E11. The most extensive viral decay was induced by bacterial isolates producing matrix metalloproteases (MMPs). Correspondingly, the addition of a specific MMP inhibitor to lake water reduced the extent of inactivation for both viruses. A lesser, though significant protective effect was also observed with inhibitors of chymotrypsin-like or trypsin-like proteases, suggesting involvement of serine proteases in enterovirus inactivation in natural systems. Overall, we demonstrate the direct effect of bacterial proteases on the inactivation of enteroviruses and identify MMPs as effective controls on enteroviruses’ environmental persistence.
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spelling pubmed-92964892022-07-21 Bacterial matrix metalloproteases and serine proteases contribute to the extra-host inactivation of enteroviruses in lake water Corre, Marie-Hélène Bachmann, Virginie Kohn, Tamar ISME J Article Enteroviruses are ubiquitous contaminants of surface waters, yet their fate in presence of microbial congeners is poorly understood. In this work, we investigated the inactivation of Echovirus-11 (E11) and Coxsackievirus-A9 (CVA9) by bacteria isolated from Lake Geneva. Incubation of E11 or CVA9 in biologically active lake water caused inactivation of 2- and 4-log(10), respectively, within 48 h. To evaluate the antiviral action of individual bacterial species, we isolated 136 bacterial strains belonging to 31 genera from Lake Geneva. The majority of isolates (92) induced decay of at least 1.5-log(10) of CVA9, whereas only 13 isolates induced a comparable inactivation on E11. The most extensive viral decay was induced by bacterial isolates producing matrix metalloproteases (MMPs). Correspondingly, the addition of a specific MMP inhibitor to lake water reduced the extent of inactivation for both viruses. A lesser, though significant protective effect was also observed with inhibitors of chymotrypsin-like or trypsin-like proteases, suggesting involvement of serine proteases in enterovirus inactivation in natural systems. Overall, we demonstrate the direct effect of bacterial proteases on the inactivation of enteroviruses and identify MMPs as effective controls on enteroviruses’ environmental persistence. Nature Publishing Group UK 2022-05-11 2022-08 /pmc/articles/PMC9296489/ /pubmed/35545659 http://dx.doi.org/10.1038/s41396-022-01246-3 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Corre, Marie-Hélène
Bachmann, Virginie
Kohn, Tamar
Bacterial matrix metalloproteases and serine proteases contribute to the extra-host inactivation of enteroviruses in lake water
title Bacterial matrix metalloproteases and serine proteases contribute to the extra-host inactivation of enteroviruses in lake water
title_full Bacterial matrix metalloproteases and serine proteases contribute to the extra-host inactivation of enteroviruses in lake water
title_fullStr Bacterial matrix metalloproteases and serine proteases contribute to the extra-host inactivation of enteroviruses in lake water
title_full_unstemmed Bacterial matrix metalloproteases and serine proteases contribute to the extra-host inactivation of enteroviruses in lake water
title_short Bacterial matrix metalloproteases and serine proteases contribute to the extra-host inactivation of enteroviruses in lake water
title_sort bacterial matrix metalloproteases and serine proteases contribute to the extra-host inactivation of enteroviruses in lake water
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9296489/
https://www.ncbi.nlm.nih.gov/pubmed/35545659
http://dx.doi.org/10.1038/s41396-022-01246-3
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