多个州的Banna病毒的冷EM结构揭示了病毒尖峰的逐步分离
Zhiqiang Li1,2, Han Xia1, Guibo Rao1
1CAS Key Laboratory of Special Pathogens, Wuhan Institute of Virology, Center for Biosafety Mega-Science, Chinese Academy of Sciences, Wuhan, 430071, PR China.
Nature communications
|March 14, 2024
概括
班纳病毒 (BAV) 结构研究显示,独特的VP10蛋白对组装至关重要. 高和低pH处理提供了简单的方法,分别生成BAV核心和修改病毒尖峰.
科学领域:
- 结构生物学是结构生物学.
- 病毒学 病毒学
- 低温电子显微镜的使用方法
背景情况:
- 班纳病毒 (BAV) 是一种Seadornavirus,之前的结构研究有限.
- 相关病毒家族的reoviruses经历了更广泛的结构分析.
研究的目的:
- 为了确定不同状态的BAV病毒的原子冷电子显微镜 (cryo-EM) 结构.
- 阐明VP10蛋白在BAV组装和结构中的作用.
- 研究pH对BAV病毒结构和蛋白质组件的影响.
主要方法:
- 原子冷EM可视化BAV病毒在完整,部分和核心状态.
- 生物化学处理 (高和低pH) 诱导结构变化.
- 在病毒囊中分析蛋白质-蛋白质相互作用.
主要成果:
- 确定了BAV全维龙 (120个尖头),部分维龙 (60个尖头) 和核心的原子结构.
- BAV核心具有双层结构,附有额外的外蛋白,VP10.
- VP10 作为凝固蛋白,与 VP2,VP8 和 VP4 相互作用,促进病毒组合.
- 高pH处理破坏了VP10-VP4相互作用,使核心生产成为可能.
- 低pH处理会去除VP9并改变VP4的形状,影响膜透.
结论:
- 与其他reoviruses相比,BAV病毒表现出明显的表面蛋白组织.
- 独特的结构表明BAV通过内膜进入宿主细胞的新机制.
- VP10是BAV病毒组合和稳定的关键组成部分.
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