在Bombyx mori核多重体病毒GP64中存在的必不可少的histidine残留物中介于pH依赖的膜融合
Haijue Tian1, Kai Chen1, Xinyu Li1
1Jiangsu Key Laboratory of Sericultural and Animal Biotechnology, School of Biotechnology, Jiangsu University of Science and Technology, Zhenjiang, China.
在Bombyx mori核多重体病毒 (BmNPV) GP64中,特定的歇斯蒂丁残留物充当pH传感器,控制病毒融合. 这项研究确定了对pH诱导的形状变化和丝虫病毒感染性至关重要的关键类素.
科学领域:
- 病毒学 病毒学
- 分子生物学分子生物学
- 生物化学 生物化学
背景情况:
- 包裹病毒利用病毒融合蛋白进入宿主细胞.
- 在I组α巴库洛病毒中,GP64调解了低pH诱导的膜融合.
- 与AcMNPV相比,Bombyx mori核聚合体病毒 (BmNPV) GP64具有独特的胺残留物,影响其融合pH值.
研究的目的:
- 为了研究BmNPV GP64中特定的胺残留物作为pH传感器的作用.
- 阐明这些histidines如何导致pH依赖的构造变化和膜融合.
- 了解相关的alphabaculoviruses之间的融合激活机制的差异.
主要方法:
- 产生了BmNPV GP64.4的14个单基斯蒂丁-阿兰因突变.
- 评估了BmN细胞中的突变表达,细胞表面定位和融合性.
- 利用gp64-null的巴克米德来评估病毒感染性和pH诱导的形状转变.
主要成果:
- 所有突变物都形成了三元体,并定位在细胞表面.
- 几种歇斯蒂丁突变消除或减少了低pH诱导的突触形成.
- 在H168,H172,H342和H351的突变对pH诱导的形状变化和病毒感染性至关重要.
结论:
- 在BmNPV GP64中确定了特定的histidine残留物 (H168,H172,H342,H351) 作为必要的pH传感器.
- 证明了这些histidines在调解pH依赖的形状转换和病毒融合中的作用.
- 提供了控制丝虫BmNPV感染的基础知识,并了解病毒进入.
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