ArticlePLoS pathogens2022
Salmonella Typhimurium outer membrane protein A (OmpA) renders protection from nitrosative stress of macrophages by maintaining the stability of bacterial outer membrane.
Article in PLoS pathogens, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 54 citations in OpenAlex.
- Divergent roles of OmpA family proteins in physiology, stress tolerance, and virulence ofVirulence · 2026Article
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- Assessment of the Immune Potential of Calcium Phosphate-Outer Membrane Protein-Nanoparticles (CaP-Omp-Nps) Adjuvanted Nano-Vaccine AgainstPharmaceutics · 2026Article
- The structures and functions of Salmonella outer membrane.Archives of microbiology · 2026Review
- Molecular strategies ofFrontiers in cellular and infection microbiology · 2026Review
- Genetic diversity ofGut microbes · 2025Article
- Intracellular formate modulates a motility-invasion switch in Salmonella Typhimurium.PLoS pathogens · 2025Article
- Reverse vaccinology-based identification and in silico characterization of immunogenic membrane proteins of Salmonella Typhimurium as novel vaccine targets against multidrug-resistant infections.BMC microbiology · 2025Article
- Ecotin protects Salmonella Typhimurium against the microbicidal activity of host proteases.PLoS pathogens · 2025Article
- Antibacterial properties ofFrontiers in nutrition · 2025Article
- First whole genome report ofCurrent research in microbial sciences · 2025Article
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- Recent advances in bacterial outer membrane vesicles: Effects on the immune system, mechanisms and their usage for tumor treatment.Journal of pharmaceutical analysis · 2024Review
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- Genomic insights of Salmonella isolated from dry fermented sausage production chains in Spain and France.Scientific reports · 2024Article
- TLR-mediated aggresome-like induced structures comprise antimicrobial peptides and attenuate intracellular bacterial survival.Molecular biology of the cell · 2024Article
- Stress response ofCurrent research in food science · 2024Article
- Outer membrane protein OMP76 ofVirulence · 2023Article
- FromACS omega · 2023Review
- A CcdB toxin-derived peptide acts as a broad-spectrum antibacterial therapeutic in infected mice.EMBO reports · 2023Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial porins are highly conserved outer membrane proteins used in the selective transport of charged molecules across the membrane. In addition to their significant contributions to the pathogenesis of Gram-negative bacteria, their role(s) in salmonellosis remains elusive. In this study, we investigated the role of outer membrane protein A (OmpA), one of the major outer membrane porins of Salmonella, in the pathogenesis of Salmonella Typhimurium (STM). Our study revealed that OmpA plays an important role in the intracellular virulence of Salmonella. An ompA deficient strain of Salmonella (STM ΔompA) showed compromised proliferation in macrophages. We found that the SPI-2 encoded virulence factors such as sifA and ssaV are downregulated in STM ΔompA. The poor colocalization of STM ΔompA with LAMP-1 showed that disruption of SCV facilitated its release into the cytosol of macrophages, where it was assaulted by reactive nitrogen intermediates (RNI). The enhanced recruitment of nitrotyrosine on the cytosolic population of STM ΔompAΔsifA and ΔompAΔssaV compared to STM ΔsifA and ΔssaV showed an additional role of OmpA in protecting the bacteria from host nitrosative stress. Further, we showed that the generation of greater redox burst could be responsible for enhanced sensitivity of STM ΔompA to the nitrosative stress. The expression of several other outer membrane porins such as ompC, ompD, and ompF was upregulated in STM ΔompA. We found that in the absence of ompA, the enhanced expression of ompF increased the outer membrane porosity of Salmonella and made it susceptible to in vitro and in vivo nitrosative stress. Our study illustrates a novel mechanism for the strategic utilization of OmpA by Salmonella to protect itself from the nitrosative stress of macrophages.
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