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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 |
Sumario: | 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. |
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