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

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

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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 GPCN79Q 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.

Lassa virus(LASV)Glycoprotein complex(GPC)Glycosylation siteMembrane fusion

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

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State Key Laboratory of Virology,Wuhan Institute of Virology,Center for Biosafety Mega-Science,Chinese Academy of Sciences,Wuhan,430207,China

University of the Chinese Academy of Sciences,Beijing,100049,China

College of Pharmacy and State Key Laboratory of Medicinal Chemical Biology,Nankai University,Tianjin,300071,China

National Key Research and Development ProgramNational Key Research and Development ProgramStrategic Priority Research Program of the Chinese Academy of SciencesNational Natural Science Foundation of ChinaNational Natural Science Foundation of China

2022YFC23033002018YFA0507204XDB04900008217227331670165

2023

中国病毒学
中国科学院武汉病毒研究所,中国微生物学会

中国病毒学

CSTPCDCSCD
影响因子:0.393
ISSN:1674-0769
年,卷(期):2023.38(3)
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