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- W1522589910 abstract "In Bacillus subtilis, the extracytoplasmic function (ECF) σ factors σ(M) , σ(W) and σ(X) all contribute to resistance against lantibiotics. Nisin, a model lantibiotic, has a dual mode of action: it inhibits cell wall synthesis by binding lipid II, and this complex also forms pores in the cytoplasmic membrane. These activities can be separated in a nisin hinge-region variant (N20P M21P) that binds lipid II, but no longer permeabilizes membranes. The major contribution of σ(M) to nisin resistance is expression of ltaSa, encoding a stress-activated lipoteichoic acid synthase, and σ(X) functions primarily by activation of the dlt operon controlling d-alanylation of teichoic acids. Together, σ(M) and σ(X) regulate cell envelope structure to decrease access of nisin to its lipid II target. In contrast, σ(W) is principally involved in protection against membrane permeabilization as it provides little protection against the nisin hinge region variant. σ(W) contributes to nisin resistance by regulation of a signal peptide peptidase (SppA), phage shock proteins (PspA and YvlC, a PspC homologue) and tellurite resistance related proteins (YceGHI). These defensive mechanisms are also effective against other lantibiotics such as mersacidin, gallidermin and subtilin and comprise an important subset of the intrinsic antibiotic resistome of B. subtilis." @default.
- W1522589910 created "2016-06-24" @default.
- W1522589910 creator A5029976904 @default.
- W1522589910 creator A5063735514 @default.
- W1522589910 creator A5068744241 @default.
- W1522589910 date "2013-09-16" @default.
- W1522589910 modified "2023-10-03" @default.
- W1522589910 title "Contributions of the σ<sup>W</sup>, σ<sup>M</sup>and σ<sup>X</sup>regulons to the lantibiotic resistome of<i>Bacillus subtilis</i>" @default.
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- W1522589910 doi "https://doi.org/10.1111/mmi.12380" @default.
- W1522589910 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4067139" @default.
- W1522589910 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23980836" @default.