ArticleMicrobiologyOpen2019
Single mutations in BraRS confer high resistance against nisin A in Staphylococcus aureus.
Article in MicrobiologyOpen, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 30 citations in OpenAlex.
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- Bacterial Biofilm Formation on Biomaterials and Approaches to Its Treatment and Prevention.International journal of molecular sciences · 2023Review
- Nisin Mutant Prevention Concentration and the Role of Subinhibitory Concentrations on Resistance Development by Diabetic FootAntibiotics (Basel, Switzerland) · 2022Article
- Recombinant production of the lantibiotic nisin using Corynebacterium glutamicum in a two-step process.Microbial cell factories · 2022Article
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- Staphylococcus aureus Virulence Affected by an Alternative Nisin A Resistance Mechanism.Applied and environmental microbiology · 2020Article
- The Synergistic Effect of Mud Crab Antimicrobial Peptides Sphistin and SphFrontiers in cellular and infection microbiology · 2020Article
- Mutations Selected After Exposure to Bacteriocin Lcn972 Activate a Bce-Like Bacitracin Resistance Module inFrontiers in microbiology · 2020Article
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- Antimicrobial resistance: A multifaceted problem with multipronged solutions.MicrobiologyOpen · 2019Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nisin A is a lantibiotic produced by Lactococcus lactis that is widely used as a food preservative. In Staphylococcus aureus, the BraRS two-component system (TCS) senses nisin A and regulates the expression of the ABC transporter VraDE, which is responsible for nisin A resistance. In this study, we exposed S. aureus to a sub-minimum inhibition concentration of nisin A and obtained three spontaneous mutants that were highly resistant to this lantibiotic, designated as SAN (S. aureus nisin resistant) 1, SAN8, and SAN87. In the wild-type S. aureus strain, VraDE expression was induced by nisin A. In contrast, SAN8 and SAN87 showed constitutively high VraDE expression, even in the absence of nisin A, while SAN1 showed higher BraRS expression, which resulted in high VraDE expression in the presence of nisin A. We identified a single mutation in the promoter region of braXRS in SAN1, whereas SAN8 and SAN87 had single mutations in braR and braS, respectively. Interestingly, even the unphosphorylated form of the mutant BraR protein induced VraDE expression. These results indicate that conformational changes in BraS or BraR resulting from the point mutations may result in the constitutive expression of VraDE, allowing S. aureus to adapt to high concentrations of nisin A.
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