ArticleFrontiers in cellular and infection microbiology2025
Discovery of amino acid substitutions in penicillin-binding proteins associated with adaptation to D-Ala-D-Lac in vancomycin-resistant
Article in Frontiers in cellular and infection microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Indigenous Fruit-Derived Lactic Acid Bacteria with Probiotic Potential and Angiotensin-Converting Enzyme I Inhibitory Activity.Probiotics and antimicrobial proteins · 2026Article
- Biological activities of metal oxide nanoparticles modified with hexadeca-substituted cobalt(ii) phthalocyanine bearing fluorinated substituents.RSC advances · 2026Article
- Proteomic Insights into Antimicrobial Resistance Mechanisms in Human-Associated Bacterial Pathogens.Microbial ecology · 2026Review
- Vancomycin resistance in gram-positive infections: evolutionary strategies of survival.Archives of microbiology · 2026Review
- Bovine Mastitis Therapy at a Crossroads: Pharmacokinetic Barriers, Biofilms, Antimicrobial Resistance, and Emerging Solutions.Pharmaceuticals (Basel, Switzerland) · 2026Review
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Authors and funding
4 authors.
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Abstract
The bacterial cell wall, essential for structural integrity, is synthesized with penicillin-binding proteins (PBPs). Vancomycin-resistant enterococci (VRE) evades vancomycin by replacing D-Ala-D-Ala in their cell wall precursors with D-Ala-D-Lac, reducing the drug's effectiveness. However, how PBPs-which typically use D-Ala-D-Ala as a substrate-adapt to recognize D-Ala-D-Lac remains unclear. Here, we performed Sanger sequencing and alignment of PBP genes from both vancomycin-susceptible and -resistant
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