病毒受体结合蛋白通过突变产生新的功能,导致三元体不稳定性和功能异质性
Hannah M Strobel1, Sweetzel D Labador1, Dwaipayan Basu2,3
1School of Biological Sciences, University of California San Diego, La Jolla, CA, USA.
Molecular biology and evolution
|April 8, 2024
概括
蛋白质进化可以导致不稳定,这可能会意外地驱动新的功能. 这项研究表明,不稳定的菌体蛋白通过改变受体结合,进化出新的宿主范围.
科学领域:
- 进化生物学是进化的生物学.
- 分子生物学分子生物学
- 生物化学 生物化学
背景情况:
- 赋予新活动的蛋白质突变往往会降低稳定性.
- 传统上,不稳定性被视为蛋白质进化的不利成本.
- 最近的证据表明,不稳定的构造可能有助于进化过渡.
研究的目的:
- 为了研究蛋白质不稳定性是否可以增强新蛋白质活动的进化.
- 检查细菌受体结合蛋白在宿主范围进化中的不稳定性作用.
主要方法:
- 在宿主范围进化之前和之后,对菌体兰巴达受体结合蛋白进行比较分析.
- 结构建模用于预测形状变化.
- 在体外寡合体状态分析以评估蛋白质稳定性和相互作用.
主要成果:
- 进化的受体结合蛋白比祖先形式不那么稳定.
- 不稳定性与破坏蛋白质三元体形成的突变有关.
- 进化的蛋白质可能采用多种形状,具有不同的受体偏好.
结论:
- 蛋白质不稳定性,特别是受体结合蛋白,可能在病毒宿主范围扩张中发挥关键作用.
- 这挑战了传统的不稳定性观点,认为它在蛋白质进化中仅仅是有害的.
- 不稳定的蛋白质构造可能是病毒适应性进化的关键媒介.
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