Scholarlink

<p>This study elucidates a novel mechanism by which the natural product berberine (BBR) reverses methicillin-resistant <i>Staphylococcus aureus</i> (MRSA) resistance to β-lactam antibiotics. It was established that BBR interferes with the BlaR1/BlaI regulatory pathway by means of downregulating the signal sensor gene <i>blaR1</i> and the repressor gene <i>blaI</i>, thereby significantly suppressing the expression of the β-lactamase-encoding gene <i>blaZ</i> at the transcriptional level. The combination susceptibility testing demonstrated that BBR and Oxacillin exhibited synergistic or additive effects in 76.92% of the bacterial strains that were tested. This enhanced efficacy was closely associated with the presence of the <i>blaZ</i> gene. Molecular docking and dynamics simulations further confirmed that BBR stably binds to the active site of the BlaZ protein. These findings systematically clarify the multi-target mechanism of BBR as an antibiotic synergist and provide an important theoretical basis for developing combination therapeutic strategies against MRSA.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Study on the Mechanism of Berberine Reversing MRSA Resistance to β-Lactam Antibiotics by Inhibiting blaZ Expression

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年5月22日

查看全文
  • Fangfang Zhou,
  • Xuemei Gu,
  • Ming Lin,
  • Yue Dai,
  • Yanan Li,
  • Mingming Jiang,
  • Bianba Yangzong,
  • Ying Wang,
  • Xiaochun Sun,
  • Lei Wang

摘要

This study elucidates a novel mechanism by which the natural product berberine (BBR) reverses methicillin-resistant Staphylococcus aureus (MRSA) resistance to β-lactam antibiotics. It was established that BBR interferes with the BlaR1/BlaI regulatory pathway by means of downregulating the signal sensor gene blaR1 and the repressor gene blaI, thereby significantly suppressing the expression of the β-lactamase-encoding gene blaZ at the transcriptional level. The combination susceptibility testing demonstrated that BBR and Oxacillin exhibited synergistic or additive effects in 76.92% of the bacterial strains that were tested. This enhanced efficacy was closely associated with the presence of the blaZ gene. Molecular docking and dynamics simulations further confirmed that BBR stably binds to the active site of the BlaZ protein. These findings systematically clarify the multi-target mechanism of BBR as an antibiotic synergist and provide an important theoretical basis for developing combination therapeutic strategies against MRSA.