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• W3132975648 abstract "Abstract Porins are highly conserved bacterial outer membrane proteins involved in the selective transport of charged molecules across the membrane. Despite their important contributions to the pathogenesis of Gram-negative bacteria, their precise role in salmonellosis remains elusive. In this study, we investigated the role of porins (OmpA, OmpC, OmpD, and OmpF) in Salmonella Typhimurium (STM) pathogenesis. OmpA played a multifaceted role in STM pathogenesis, and a strain deleted for ompA (STM ΔompA ) showed enhanced proneness to phagocytosis and compromised proliferation in macrophages. However, in epithelial cells, despite being invasion deficient, it was hyper-proliferative. The poor colocalization of STM ΔompA with LAMP-1 confirmed impaired stability of SCV membrane around the intracellular bacteria, resulting in its (STM ΔompA ) release into the cytosol of macrophages where it is assaulted with reactive nitrogen intermediates (RNI). The cytosolic localization of STM ΔompA was responsible for the downregulation of SPI-2 encoded virulence factor SpiC, which is required to suppress the activity of iNOS. The reduced recruitment of nitrotyrosine on STM in the macrophage cytosol upon ectopically expressing Listeriolysin O (LLO) explicitly supported the pro-bacterial role of OmpA against the host nitrosative stress. Further, we show that time-dependent generation of redox burst could be responsible for the enhanced sensitivity of STM ΔompA towards nitrosative stress. The absence of OmpA in STM ΔompA resulted in the loss of integrity and enhanced porosity of the outer membrane, which was attributed to the upregulated expression of ompC , ompD, and ompF . We show the involvement of OmpC and OmpF in the entry of excess nitrite in STM ΔompA . In conclusion, we illustrated a mechanism of strategic utilization of OmpA compared to other porins by wildtype Salmonella for combating the nitrosative stress in macrophages." @default.
• W3132975648 created "2021-03-01" @default.
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• W3132975648 date "2021-02-12" @default.
• W3132975648 modified "2023-09-23" @default.
• W3132975648 title "Salmonella Typhimurium outer membrane protein A (OmpA) renders protection against nitrosative stress by promoting SCV stability in murine macrophages" @default.
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• W3132975648 doi "https://doi.org/10.1101/2021.02.12.430987" @default.
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