Structural transition of GP64 triggered by a pH-sensitive multi-histidine switch

doi:10.1038/s41467-024-51799-4

	Structural transition of GP64 triggered by a pH-sensitive multi-histidine switch
	Guo JL(郭金两)1 ; Li SR(李尚蓉)1 ; Bai LS(白丽莎)2; Zhao HM(赵慧敏)1 ; Shang WY(尚文煜)1 ; Zhong ZJ(钟昭君)1 ; 吐尔逊江·买买提1 ; Gao XY(高雪岩)1 ; Ning Ji 2; Chao YJ(晁彦杰)3; Du DJ(杜迪军)1 ; Li CF(李朝飞)2
	2024-09
发表期刊	NATURE COMMUNICATIONS (IF:14.7[JCR-2023],16.1[5-Year])
ISSN	2041-1723
EISSN	2041-1723
卷号	15 期号:1
发表状态	已发表
DOI	10.1038/s41467-024-51799-4
摘要	The fusion of viruses with cellular membranes is a critical step in the life cycle of enveloped viruses. This process is facilitated by viral fusion proteins, many of which are conformationally pH-sensitive. The specifics of how changes in pH initiate this fusion have remained largely elusive. This study presents the cryo-electron microscopy (cryo-EM) structures of a prototype class III fusion protein, GP64, in its prefusion and early intermediate states, revealing the structural intermediates accompanying the membrane fusion process. The structures identify the involvement of a pH-sensitive switch, comprising H23, H245, and H304, in sensing the low pH that triggers the initial step of membrane fusion. The pH sensing role of this switch is corroborated by assays of cell-cell syncytium formation and dual dye-labeling. The findings demonstrate that coordination between multiple histidine residues acts as a pH sensor and activator. The involvement of a multi-histidine switch in viral fusion is applicable to fusogens of human-infecting thogotoviruses and other viruses, which could lead to strategies for developing anti-viral therapies and vaccines.
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收录类别	SCI
语种	英语
资助项目	National Natural Science Foundation of China["31971133","32172485"] ; Science and Technology Commission of Shanghai Municipality["19PJ1407900","19JC1414000","22WZ2504100"]
WOS研究方向	Science & Technology - Other Topics
WOS类目	Multidisciplinary Sciences
WOS记录号	WOS:001389506900013
出版者	NATURE PORTFOLIO
引用统计	被引频次：3[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/421766
专题	生命科学与技术学院_PI研究组_杜迪军组生命科学与技术学院_博士生
共同第一作者	Li SR(李尚蓉); Bai LS(白丽莎); Zhao HM(赵慧敏)
通讯作者	Du DJ(杜迪军); Li CF(李朝飞)
作者单位	1.School of Life Science and Technology, ShanghaiTech University, Shanghai, China 2.State Key Laboratory of Crop Stress Biology for Arid Areas, Key Laboratory of Plant Protection Resources and Pest Management of Ministry of Education, Key Laboratory of Integrated Pest Management on the Loess Plateau of Ministry of Agriculture and Rural Affairs, College of Plant Protection, Northwest A&F University, Yangling, 712100, Shaanxi, China 3.CAS Key Laboratory of Molecular Virology and Immunology, Shanghai Institute of Immunity and Infection, Chinese Academy of Sciences, Shanghai, China
第一作者单位	生命科学与技术学院
通讯作者单位	生命科学与技术学院
第一作者的第一单位	生命科学与技术学院
推荐引用方式 GB/T 7714	Guo JL,Li SR,Bai LS,et al. Structural transition of GP64 triggered by a pH-sensitive multi-histidine switch[J]. NATURE COMMUNICATIONS,2024,15(1).
APA	Guo JL.,Li SR.,Bai LS.,Zhao HM.,Shang WY.,...&Li CF.(2024).Structural transition of GP64 triggered by a pH-sensitive multi-histidine switch.NATURE COMMUNICATIONS,15(1).
MLA	Guo JL,et al."Structural transition of GP64 triggered by a pH-sensitive multi-histidine switch".NATURE COMMUNICATIONS 15.1(2024).