Cryo-EM structure of glycoprotein C from Crimean-Congo hemorrhagic fever virus

作     者：Na Li Guibo Rao Zhiqiang Li Jiayi Yin Tingting Chong Kexing Tian Yan Fu Sheng Cao Na Li;Guibo Rao;Zhiqiang Li;Jiayi Yin;Tingting Chong;Kexing Tian;Yan Fu;Sheng Cao

作者机构：CAS Key Laboratory of Special PathogensCenter for Biosafety Mega-ScienceWuhan Institute of VirologyChinese Academy of SciencesWuhan430071China University of Chinese Academy of SciencesBeijing100049China 

出 版 物：《Virologica Sinica》 (中国病毒学（英文版）)

年 卷 期：2022年第37卷第1期

页      面：127-137页

核心收录：

学科分类：0710[理学-生物学] 1007[医学-药学(可授医学、理学学位)] 100705[医学-微生物与生化药学] 1001[医学-基础医学(可授医学、理学学位)] 100103[医学-病原生物学] 10[医学] 

基　　金：supported by the National Natural Science Foundation of China(31570161) 

主　　题：Crimean-Congo hemorrhagic Fever virus(CCHFV) Glycoprotein C Fusion protein Bunyavirus 

摘      要：Crimean-Congo hemorrhagic fever virus(CCHFV)is a causative agent of serious hemorrhagic diseases in humans with high mortality *** glycoprotein Gc plays critical roles in mediating virus-host membrane fusion and has been studied extensively as an ***,the molecular mechanisms involved in membrane fusion and Gc-specific antibody-antigen interactions remain unresolved largely because structural information of this glycoprotein is *** designed a trimeric protein including most of the ectodomain region of Gc from the prototype CCHFV strain,Ib Ar10200,which enabled the cryo-electron microscopy structure to be solved at a resolution of 2.8Å.The structure confirms that CCHFV Gc is a class Ⅱ fusion ***,structural comparisons with other solved Gc trimers in the postfusion conformation revealed that CCHFV Gc adopted hybrid architectural features of the fusion loops from hantaviruses and domain Ⅲ from phenuiviruses,suggesting a complex evolutionary pathway among these *** sites on CCHFV Gc that protective neutralizing antibodies target were mapped onto the CCHFV Gc structure,providing valuable information that improved our understanding of potential neutralization mechanisms of various antibodies.