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在金色葡萄球菌的宽谱β-乳糖耐药性的结构基础

J Andrew N Alexander^1,2, Liam J Worrall^1,2,3, Jinhong Hu^1,2

¹Department of Biochemistry and Molecular Biology, The University of British Columbia, Vancouver, British Columbia, Canada.

|January 4, 2023

概括

黄金葡萄球菌的抗生素耐药性是一个全球性的威胁. 研究人员发现BlaR1受体直接切割BlaI抑制器,这是激活抵抗机制的关键步骤.

科学领域:

微生物学
分子生物学
结构生物学

背景情况:

金色葡萄球菌的宽谱β-乳酸抗生素耐药性构成了全球重大健康挑战.
BlaR1受体是这种抗性的核心,感知β-乳酸盐并激活下游信号.
已知BlaR1的金属蛋白酶域会去压BlaI,从而导致像blaZ和mecA这样的抗性基因的表达.

研究的目的:

阐明 BlaR1 禁用 BlaI 抑制器的直接机制.
确定BlaR1的功能和信号的结构基础.
研究BlaR1的自分裂机制及其在BlaI分裂中的作用.

主要方法:

使用冷电子显微镜 (cryo-EM) 确定野生型和突变 BlaR1 的结构.
在存在或缺少β-乳糖时对BlaR1进行结构分析.
对BlaR1的自分裂和BlaI分裂活动的生物化学特征.

主要成果:

在不需要其他组件的情况下, BlaR1 直接切割 BlaI 压缩器.
低温电磁结构显示了一个对信号循环稳定至关重要的域交换二元体.
BlaR1经历自发裂变,它的结构阐明了自我和BlaI裂变的机制.
乙酸乳结合会诱导形状变化,转移传感器域并激活金属蛋白酶域以实现有效的BlaI裂变.

结论:

这项研究提供了对二元信号受体BlaR1的首次结构见解.
这些发现表明,BlaR1通过直接切割BlaI抑制剂来调解抗生素耐药性.
了解这种机制为对抗金黄色葡萄球菌抗生素耐药性提供了潜在的目标.

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