ArticleFrontiers in microbiology2025
Proteomics and acetyl-proteomics reveal the antibacterial mechanism of berberine sulfate against methicillin-resistant
Article in Frontiers in microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- Synthesis of the Natural Product Berberine.ACS omega · 2026Article
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10 authors.
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Abstract
Introduction: The rising prevalence of methicillin-resistant Methods: To elucidate its mechanism, this study employed quantitative proteomics to analyze protein expression changes in MRSA before and after drug treatment. Acetylomics was further applied to investigate the impact on post-translational modifications. Key findings were functionally validated using site-directed mutagenesis and electrophoretic mobility shift assays (EMSA). Results: Quantitative proteomics identified 255 differentially expressed proteins. Acetylomic analysis further revealed 38 differentially acetylated sites, among which berberine sulfate specifically induced acetylation at the K82 site of the global regulator SarA. Functional experiments demonstrated that the K82-mutated SarA protein showed significantly reduced binding affinity to the promoter of the virulence gene cluster Discussion: These results indicate that berberine sulfate mediates a comprehensive stress response in MRSA through extensive alterations in protein expression and post-translational modifications. Specifically, the acetylation of SarA at K82 and the consequent impairment of its DNA-binding capacity represent a potential core mechanism by which berberine sulfate suppresses MRSA virulence and adaptability.
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