Cryo-EM structure of severe fever with thrombocytopenia syndrome virus

Shouwen Du, Ruchao Peng, Wang Xu, Xiaoyun Qu, Yuhang Wang, Jiamin Wang, Letian Li, Mingyao Tian, Yudong Guan, Jigang Wang, Guoqing Wang, Hao Li, Lingcong Deng, Xiaoshuang Shi, Yidan Ma, Fengting Liu, Minhua Sun, Zhengkai Wei, Ningyi Jin, Wei Liu (), Jianxun Qi (), Quan Liu (), Ming Liao () and Chang Li ()
Additional contact information
Shouwen Du: Scientific Observation and Experiment Station of Veterinary Drugs and Diagnostic Techniques of Guangdong Province, Ministry of Agriculture and Rural Affairs, Institute of Animal Health, Guangdong Academy of Agricultural Sciences
Ruchao Peng: University of Pennsylvania
Wang Xu: Chinese Academy of Medical Sciences, Changchun Veterinary Research Institute, Chinese Academy of Agricultural Sciences
Xiaoyun Qu: Scientific Observation and Experiment Station of Veterinary Drugs and Diagnostic Techniques of Guangdong Province, Ministry of Agriculture and Rural Affairs, Institute of Animal Health, Guangdong Academy of Agricultural Sciences
Yuhang Wang: Southern University of Science and Technology
Jiamin Wang: Chinese Academy of Medical Sciences, Changchun Veterinary Research Institute, Chinese Academy of Agricultural Sciences
Letian Li: Chinese Academy of Medical Sciences, Changchun Veterinary Research Institute, Chinese Academy of Agricultural Sciences
Mingyao Tian: Chinese Academy of Medical Sciences, Changchun Veterinary Research Institute, Chinese Academy of Agricultural Sciences
Yudong Guan: Southern University of Science and Technology
Jigang Wang: Southern University of Science and Technology
Guoqing Wang: The First Hospital of Jilin University
Hao Li: Beijing Institute of Microbiology and Epidemiology
Lingcong Deng: Chinese Academy of Medical Sciences, Changchun Veterinary Research Institute, Chinese Academy of Agricultural Sciences
Xiaoshuang Shi: Chinese Academy of Medical Sciences, Changchun Veterinary Research Institute, Chinese Academy of Agricultural Sciences
Yidan Ma: Chinese Academy of Medical Sciences, Changchun Veterinary Research Institute, Chinese Academy of Agricultural Sciences
Fengting Liu: Southern University of Science and Technology
Minhua Sun: Scientific Observation and Experiment Station of Veterinary Drugs and Diagnostic Techniques of Guangdong Province, Ministry of Agriculture and Rural Affairs, Institute of Animal Health, Guangdong Academy of Agricultural Sciences
Zhengkai Wei: Scientific Observation and Experiment Station of Veterinary Drugs and Diagnostic Techniques of Guangdong Province, Ministry of Agriculture and Rural Affairs, Institute of Animal Health, Guangdong Academy of Agricultural Sciences
Ningyi Jin: Chinese Academy of Medical Sciences, Changchun Veterinary Research Institute, Chinese Academy of Agricultural Sciences
Wei Liu: Beijing Institute of Microbiology and Epidemiology
Jianxun Qi: Institute of Microbiology, Chinese Academy of Sciences
Quan Liu: Scientific Observation and Experiment Station of Veterinary Drugs and Diagnostic Techniques of Guangdong Province, Ministry of Agriculture and Rural Affairs, Institute of Animal Health, Guangdong Academy of Agricultural Sciences
Ming Liao: Scientific Observation and Experiment Station of Veterinary Drugs and Diagnostic Techniques of Guangdong Province, Ministry of Agriculture and Rural Affairs, Institute of Animal Health, Guangdong Academy of Agricultural Sciences
Chang Li: The First Hospital of Jilin University

Nature Communications, 2023, vol. 14, issue 1, 1-14

Abstract: Abstract The severe fever with thrombocytopenia syndrome virus (SFTSV) is a tick-borne human-infecting bunyavirus, which utilizes two envelope glycoproteins, Gn and Gc, to enter host cells. However, the structure and organization of these glycoproteins on virion surface are not yet known. Here we describe the structure of SFTSV determined by single particle reconstruction, which allows mechanistic insights into bunyavirus assembly at near-atomic resolution. The SFTSV Gn and Gc proteins exist as heterodimers and further assemble into pentameric and hexameric peplomers, shielding the Gc fusion loops by both intra- and inter-heterodimer interactions. Individual peplomers are associated mainly through the ectodomains, in which the highly conserved glycans on N914 of Gc play a crucial role. This elaborate assembly stabilizes Gc in the metastable prefusion conformation and creates some cryptic epitopes that are only accessible in the intermediate states during virus entry. These findings provide an important basis for developing vaccines and therapeutic drugs.

Date: 2023
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DOI: 10.1038/s41467-023-41804-7

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