Deletion of the first glycosylation site promotes Lassa virus glycoprotein-mediated membrane fusion  

作　　者：Siqi Dong Wenting Mao Yang Liu Xiaoying Jia Yueli Zhang Minmin Zhou Yuxia Hou Gengfu Xiao Wei Wang 

机构地区：[1]State Key Laboratory of Virology,Wuhan Institute of Virology,Center for Biosafety Mega-Science,Chinese Academy of Sciences,Wuhan,430207,China [2]University of the Chinese Academy of Sciences,Beijing,100049,China [3]College of Pharmacy and State Key Laboratory of Medicinal Chemical Biology,Nankai University,Tianjin,300071,China

出　　处：《Virologica Sinica》2023年第3期380-386,共7页中国病毒学（英文版）

基　　金：the National Key Research and Development Program(2022YFC2303300,2018YFA0507204);the Strategic Priority Research Program of the Chinese Academy of Sciences(XDB0490000);the Na-tional Natural Science Foundation of China(82172273,31670165).

摘　　要：The Lassa virus(LASV)is endemic in West Africa and causes severe hemorrhagic Lassa fever in humans.The glycoprotein complex(GPC)of LASV is highly glycosylation-modified,with 11 N-glycosylation sites.All 11 N-linked glycan chains play critical roles in GPC cleavage,folding,receptor binding,membrane fusion,and immune evasion.In this study,we focused on the first glycosylation site because its deletion mutant(N79Q)results in an unexpected enhanced membrane fusion,whereas it exerts little effect on GPC expression,cleavage,and receptor binding.Meanwhile,the pseudotype virus bearing GPC_(N79Q)was more sensitive to the neutralizing antibody 37.7H and was attenuated in virulence.Exploring the biological functions of the key glycosylation site on LASV GPC will help elucidate the mechanism of LASV infection and provide strategies for the development of attenuated vaccines against LASV infection.

关 键 词：Lassa virus(LASV) Glycoprotein complex(GPC) Glycosylation site Membrane fusion 

分 类 号：R373[医药卫生—病原生物学]