A potent Henipavirus cross-neutralizing antibody reveals a dynamic fusion-triggering pattern of the G-tetramer

Pengfei Fan (), Mengmeng Sun, Xinghai Zhang, Huajun Zhang, Yujiao Liu, Yanfeng Yao, Ming Li, Ting Fang, Bingjie Sun, Zhengshan Chen, Xiangyang Chi, Li Chen, Cheng Peng, Zhen Chen, Guanying Zhang, Yi Ren, Zixuan Liu, Yaohui Li, Jianmin Li, Entao Li, Wuxiang Guan, Shanshan Li, Rui Gong (), Kaiming Zhang (), Changming Yu () and Sandra Chiu ()
Additional contact information
Pengfei Fan: Institute of Biotechnology
Mengmeng Sun: University of Science and Technology of China
Xinghai Zhang: Chinese Academy of Sciences
Huajun Zhang: Chinese Academy of Sciences
Yujiao Liu: Institute of Biotechnology
Yanfeng Yao: Chinese Academy of Sciences
Ming Li: University of Science and Technology of China
Ting Fang: Institute of Biotechnology
Bingjie Sun: Institute of Biotechnology
Zhengshan Chen: Institute of Biotechnology
Xiangyang Chi: Institute of Biotechnology
Li Chen: Chinese Academy of Sciences
Cheng Peng: Chinese Academy of Sciences
Zhen Chen: Chinese Academy of Sciences
Guanying Zhang: Institute of Biotechnology
Yi Ren: Institute of Biotechnology
Zixuan Liu: Institute of Biotechnology
Yaohui Li: Institute of Biotechnology
Jianmin Li: Institute of Biotechnology
Entao Li: University of Science and Technology of China
Wuxiang Guan: Chinese Academy of Sciences
Shanshan Li: University of Science and Technology of China
Rui Gong: Chinese Academy of Sciences
Kaiming Zhang: University of Science and Technology of China
Changming Yu: Institute of Biotechnology
Sandra Chiu: University of Science and Technology of China

Nature Communications, 2024, vol. 15, issue 1, 1-17

Abstract: Abstract The Hendra and Nipah viruses (HNVs) are highly pathogenic pathogens without approved interventions for human use. In addition, the interaction pattern between the attachment (G) and fusion (F) glycoproteins required for virus entry remains unclear. Here, we isolate a panel of Macaca-derived G-specific antibodies that cross-neutralize HNVs via multiple mechanisms. The most potent antibody, 1E5, confers adequate protection against the Nipah virus challenge in female hamsters. Crystallography demonstrates that 1E5 has a highly similar binding pattern to the receptor. In cryo-electron microscopy studies, the tendency of 1E5 to bind to the upper or lower heads results in two distinct quaternary structures of G. Furthermore, we identify the extended outer loop β1S2-β1S3 of G and two pockets on the apical region of fusion (F) glycoprotein as the essential sites for G-F interactions. This work highlights promising drug candidates against HNVs and contributes deeper insights into the viruses.

Date: 2024
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DOI: 10.1038/s41467-024-48601-w

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