ArticleThe Journal of biological chemistry2012
The PmrAB system-inducing conditions control both lipid A remodeling and O-antigen length distribution, influencing the Salmonella Typhimurium-host interactions.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 41 citations in OpenAlex.
- Structure and function of Salmonella inner membrane.Archives of microbiology · 2026Review
- Evasion of serum antibodies and complement by Salmonella Typhi and Paratyphi A.PLoS pathogens · 2025Article
- A Sensitive GC-MS Method for Quantitation of Lipid A Backbone Components and Terminal Phosphate Modifications.Journal of the American Society for Mass Spectrometry · 2022Article
- The role of bacterial transport systems in the removal of host antimicrobial peptides in Gram-negative bacteria.FEMS microbiology reviews · 2022Review
- LpxT-Dependent Phosphorylation of Lipid A inFrontiers in microbiology · 2021Article
- Lipopolysaccharide O-antigens-bacterial glycans made to measure.The Journal of biological chemistry · 2020Review
- Exposure to Sub-inhibitory Concentrations of the Chemosensitizer 1-(1-Naphthylmethyl)-Piperazine Creates Membrane Destabilization in Multi-Drug ResistantFrontiers in microbiology · 2019Article
- Novel Role of VisP and the Wzz System during O-Antigen Assembly in Salmonella enterica Serovar Typhimurium Pathogenesis.Infection and immunity · 2018Article
- Essential Two-Component Systems Regulating Cell Envelope Functions: Opportunities for Novel Antibiotic Therapies.The Journal of membrane biology · 2018Review
- S. Typhimurium strategies to resist killing by cationic antimicrobial peptides.Biochimica et biophysica acta · 2015Review
- Kdo2 -lipid A: structural diversity and impact on immunopharmacology.Biological reviews of the Cambridge Philosophical Society · 2015Review
- Article
- Evolving Bacterial Envelopes and Plasticity of TLR2-Dependent Responses: Basic Research and Translational Opportunities.Frontiers in immunology · 2013Review
- Conflicting roles for a cell surface modification in Salmonella.Molecular microbiology · 2013Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
The Salmonella enterica serovar Typhimurium lipopolysaccharide consisting of covalently linked lipid A, non-repeating core oligosaccharide, and the O-antigen polysaccharide is the most exposed component of the cell envelope. Previous studies demonstrated that all of these regions act against the host immunity barrier. The aim of this study was to define the role and interaction of PmrAB-dependent gene products required for the lipopolysaccharide component synthesis or modification mainly during the Salmonella infection. The PmrAB two-component system activation promotes a remodeling of lipid A and the core region by addition of 4-aminoarabinose and/or phosphoethanolamine. These PmrA-dependent activities are produced by activation of ugd, pbgPE, pmrC, cpta, and pmrG transcription. In addition, under PmrA regulator activation, the expression of wzz(fepE) and wzz(st) genes is induced, and their products are required to determine the O-antigen chain length. Here we report for the first time that Wzz(st) protein is necessary to maintain the balance of 4-aminoarabinose and phosphoethanolamine lipid A modifications. Moreover, we demonstrate that the interaction of the PmrA-dependent pbgE(2) and pbgE(3) gene products is important for the formation of the short O-antigen region. Our results establish that PmrAB is the global regulatory system that controls lipopolysaccharide modification, leading to a coordinate regulation of 4-aminoarabinose incorporation and O-antigen chain length to respond against the host defense mechanisms.
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