ArticleAntimicrobial agents and chemotherapy2015
PmrD is required for modifications to escherichia coli endotoxin that promote antimicrobial resistance.
Article in Antimicrobial agents and chemotherapy, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 110 citations in OpenAlex.
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- Analysis of stress-induced small proteins inbioRxiv : the preprint server for biology · 2025Article
- PhoPQ-mediated lipopolysaccharide modification governs intrinsic resistance to tetracycline and glycylcycline antibiotics inmSystems · 2024Article
- Molecular Mechanisms of Bacterial Resistance to Antimicrobial Peptides in the Modern Era: An Updated Review.Microorganisms · 2024Review
- A Review on Colistin Resistance: An Antibiotic of Last Resort.Microorganisms · 2024Review
- Influence of PhoPQ and PmrAB two component system alternations on colistin resistance from non-mcr colistin resistant clinical E. Coli strains.BMC microbiology · 2024Article
- Polyphosphate kinase regulates LPS structure and polymyxin resistance during starvation in E. coli.PLoS biology · 2024Article
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- Genomic Insights into Bacterial Resistance to Proline-Rich Antimicrobial Peptide Bac7.Membranes · 2023Article
- The QseB response regulator imparts tolerance to positively charged antibiotics by controlling metabolism and minor changes to LPS.bioRxiv : the preprint server for biology · 2023Article
- Diacylglycerol Kinase A Is Essential for Polymyxin Resistance Provided by EptA, MCR-1, and Other Lipid A Phosphoethanolamine Transferases.Journal of bacteriology · 2022Article
- Global colistin use: a review of the emergence of resistant Enterobacterales and the impact on their genetic basis.FEMS microbiology reviews · 2022Review
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4 authors at 1 institution in 1 country.
Funding
Abstract
In Salmonella enterica, PmrD is a connector protein that links the two-component systems PhoP-PhoQ and PmrA-PmrB. While Escherichia coli encodes a PmrD homolog, it is thought to be incapable of connecting PhoPQ and PmrAB in this organism due to functional divergence from the S. enterica protein. However, our laboratory previously observed that low concentrations of Mg(2+), a PhoPQ-activating signal, leads to the induction of PmrAB-dependent lipid A modifications in wild-type E. coli (C. M. Herrera, J. V. Hankins, and M. S. Trent, Mol Microbiol 76:1444-1460, 2010, http://dx.doi.org/10.1111/j.1365-2958.2010.07150.x). These modifications include phosphoethanolamine (pEtN) and 4-amino-4-deoxy-l-arabinose (l-Ara4N), which promote bacterial resistance to cationic antimicrobial peptides (CAMPs) when affixed to lipid A. Here, we demonstrate that pmrD is required for modification of the lipid A domain of E. coli lipopolysaccharide (LPS) under low-Mg(2+) growth conditions. Further, RNA sequencing shows that E. coli pmrD influences the expression of pmrA and its downstream targets, including genes coding for the modification enzymes that transfer pEtN and l-Ara4N to the lipid A molecule. In line with these findings, a pmrD mutant is dramatically impaired in survival compared with the wild-type strain when exposed to the CAMP polymyxin B. Notably, we also reveal the presence of an unknown factor or system capable of activating pmrD to promote lipid A modification in the absence of the PhoPQ system. These results illuminate a more complex network of protein interactions surrounding activation of PhoPQ and PmrAB in E. coli than previously understood.
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