Atomic structures of Coxsackievirus A6 and its complex with a neutralizing antibody

Longfa Xu, Qingbing Zheng, Shaowei Li, Maozhou He, Yangtao Wu, Yongchao Li, Rui Zhu, Hai Yu, Qiyang Hong, Jie Jiang, Zizhen Li, Shuxuan Li, Huan Zhao, Lisheng Yang, Wangheng Hou, Wei Wang, Xiangzhong Ye, Jun Zhang, Timothy S. Baker, Tong Cheng (), Z. Hong Zhou, Xiaodong Yan () and Ningshao Xia ()
Additional contact information
Longfa Xu: Xiamen University
Qingbing Zheng: Xiamen University
Shaowei Li: Xiamen University
Maozhou He: Xiamen University
Yangtao Wu: Xiamen University
Yongchao Li: Xiamen University
Rui Zhu: Xiamen University
Hai Yu: Xiamen University
Qiyang Hong: Xiamen University
Jie Jiang: Xiamen University
Zizhen Li: Xiamen University
Shuxuan Li: Xiamen University
Huan Zhao: Xiamen University
Lisheng Yang: Department of Research & Development Beijing Wantai Biological Pharmacy Enterprise Co., Ltd.
Wangheng Hou: Xiamen University
Wei Wang: Xiamen University
Xiangzhong Ye: Department of Research & Development Beijing Wantai Biological Pharmacy Enterprise Co., Ltd.
Jun Zhang: Xiamen University
Timothy S. Baker: University of California-San Diego
Tong Cheng: Xiamen University
Z. Hong Zhou: The California NanoSystems Institute (CNSI), UCLA
Xiaodong Yan: Xiamen University
Ningshao Xia: Xiamen University

Nature Communications, 2017, vol. 8, issue 1, 1-12

Abstract: Abstract Coxsackievirus A6 (CVA6) has recently emerged as a major cause of hand, foot and mouth disease in children worldwide but no vaccine is available against CVA6 infections. Here, we demonstrate the isolation of two forms of stable CVA6 particles-procapsid and A-particle-with excellent biochemical stability and natural antigenicity to serve as vaccine candidates. Despite the presence (in A-particle) or absence (in procapsid) of capsid-RNA interactions, the two CVA6 particles have essentially identical atomic capsid structures resembling the uncoating intermediates of other enteroviruses. Our near-atomic resolution structure of CVA6 A-particle complexed with a neutralizing antibody maps an immune-dominant neutralizing epitope to the surface loops of VP1. The structure-guided cell-based inhibition studies further demonstrate that these loops could serve as excellent targets for designing anti-CVA6 vaccines.

Date: 2017
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DOI: 10.1038/s41467-017-00477-9

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