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A novel aquaporin Aagp contributes to Streptococcus suis H(2)O(2) efflux and virulence
Streptococcus suis is a bacterium that can cause infections in pigs and humans. Although oxidative stress is common occurrence during bacterial growth and infection, the regulation networks of S. suis under oxidative stress remain poorly understood. To address this, we utilized RNA-Seq to reveal the...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10461500/ https://www.ncbi.nlm.nih.gov/pubmed/37621097 http://dx.doi.org/10.1080/21505594.2023.2249789 |
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author | Zhu, Xinchi Wang, Shuoyue Du, Yu Liang, Zijing Yao, Huochun Chen, Xiang Wu, Zongfu |
author_facet | Zhu, Xinchi Wang, Shuoyue Du, Yu Liang, Zijing Yao, Huochun Chen, Xiang Wu, Zongfu |
author_sort | Zhu, Xinchi |
collection | PubMed |
description | Streptococcus suis is a bacterium that can cause infections in pigs and humans. Although oxidative stress is common occurrence during bacterial growth and infection, the regulation networks of S. suis under oxidative stress remain poorly understood. To address this, we utilized RNA-Seq to reveal the transcriptional landscape of S. suis in response to H(2)O(2) stress. We identified novel genes responsible for S. suis resistance to oxidative stress, including those involved in DNA repair or protection, and essential for the biosynthesis of amino acids and nucleic acids. In addition, we found that a novel aquaporin, Aagp, belonging to atypical aquaglyceroporins and widely distributed in diverse S. suis serotypes, plays a crucial role during H(2)O(2) stress. By performing oxidative stress assays and measuring the intracellular H(2)O(2) concentrations of the wild-type strain and Aagp mutants during H(2)O(2) stress, we found that Aagp facilitated H(2)O(2) efflux. Additionally, we found that Aagp might be involved in glycerol transport, as shown by the growth inhibition and H(2)O(2) production in the presence of glycerol. Mice infection experiments indicated that Aagp contributed to S. suis virulence. This study contributes to understanding the mechanism of S. suis oxidative stress response, S. suis pathogenesis, and the function of aquaporins in prokaryotes. |
format | Online Article Text |
id | pubmed-10461500 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Taylor & Francis |
record_format | MEDLINE/PubMed |
spelling | pubmed-104615002023-08-29 A novel aquaporin Aagp contributes to Streptococcus suis H(2)O(2) efflux and virulence Zhu, Xinchi Wang, Shuoyue Du, Yu Liang, Zijing Yao, Huochun Chen, Xiang Wu, Zongfu Virulence Research Paper Streptococcus suis is a bacterium that can cause infections in pigs and humans. Although oxidative stress is common occurrence during bacterial growth and infection, the regulation networks of S. suis under oxidative stress remain poorly understood. To address this, we utilized RNA-Seq to reveal the transcriptional landscape of S. suis in response to H(2)O(2) stress. We identified novel genes responsible for S. suis resistance to oxidative stress, including those involved in DNA repair or protection, and essential for the biosynthesis of amino acids and nucleic acids. In addition, we found that a novel aquaporin, Aagp, belonging to atypical aquaglyceroporins and widely distributed in diverse S. suis serotypes, plays a crucial role during H(2)O(2) stress. By performing oxidative stress assays and measuring the intracellular H(2)O(2) concentrations of the wild-type strain and Aagp mutants during H(2)O(2) stress, we found that Aagp facilitated H(2)O(2) efflux. Additionally, we found that Aagp might be involved in glycerol transport, as shown by the growth inhibition and H(2)O(2) production in the presence of glycerol. Mice infection experiments indicated that Aagp contributed to S. suis virulence. This study contributes to understanding the mechanism of S. suis oxidative stress response, S. suis pathogenesis, and the function of aquaporins in prokaryotes. Taylor & Francis 2023-08-24 /pmc/articles/PMC10461500/ /pubmed/37621097 http://dx.doi.org/10.1080/21505594.2023.2249789 Text en © 2023 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The terms on which this article has been published allow the posting of the Accepted Manuscript in a repository by the author(s) or with their consent. |
spellingShingle | Research Paper Zhu, Xinchi Wang, Shuoyue Du, Yu Liang, Zijing Yao, Huochun Chen, Xiang Wu, Zongfu A novel aquaporin Aagp contributes to Streptococcus suis H(2)O(2) efflux and virulence |
title | A novel aquaporin Aagp contributes to Streptococcus suis H(2)O(2) efflux and virulence |
title_full | A novel aquaporin Aagp contributes to Streptococcus suis H(2)O(2) efflux and virulence |
title_fullStr | A novel aquaporin Aagp contributes to Streptococcus suis H(2)O(2) efflux and virulence |
title_full_unstemmed | A novel aquaporin Aagp contributes to Streptococcus suis H(2)O(2) efflux and virulence |
title_short | A novel aquaporin Aagp contributes to Streptococcus suis H(2)O(2) efflux and virulence |
title_sort | novel aquaporin aagp contributes to streptococcus suis h(2)o(2) efflux and virulence |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10461500/ https://www.ncbi.nlm.nih.gov/pubmed/37621097 http://dx.doi.org/10.1080/21505594.2023.2249789 |
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