Structural Basis for the Broad, Antibody-Mediated Neutralization of H5N1 Influenza Virus

Author:

Lin Qingshan1,Li Tingting1,Chen Yixin12,Lau Siu-Ying3,Wei Minxi1,Zhang Yuyun2,Zhang Zhenyong1,Yao Qiaobin1,Li Jinjin2,Li Zhihai1,Wang Daning2,Zheng Qingbing2,Yu Hai2,Gu Ying12,Zhang Jun2,Chen Honglin23ORCID,Li Shaowei12,Xia Ningshao12

Affiliation:

1. State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, Xiamen University, Xiamen, China

2. National Institute of Diagnostics and Vaccine Development in Infectious Disease, School of Public Health, Xiamen University, Xiamen, China

3. State Key Laboratory for Emerging Infectious Diseases, Department of Microbiology, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Hong Kong SAR, China

Abstract

Infection by highly pathogenic avian influenza A virus remains a threat to public health. Our broadly neutralizing antibody, 13D4, is capable of neutralizing all representative H5N1 viruses and protecting mice against lethal challenge. Structural analysis revealed that 13D4 uses heavy-chain complementarity-determining region 3 (HCDR3) to fit the receptor binding site (RBS) via conformational rearrangement. Four conserved residues within the RBS are critical for the broad potency of 13D4. Importantly, polymorphism of Lys193 on the RBS may be associated with the antigenicity shift from H5N1 to other newly emerging viruses, such as H5N6 and H5N8. Our findings may pave the way for highly pathogenic avian influenza virus vaccine development and therapeutic RBS inhibitor design.

Funder

Scientific Research Foundation of State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics

Research Grants Council of the Hong Kong SAR

National Natural Science Foundation of China

Fujian Provincial Department of Science and Technology

Xiamen Municipal Bureau of Science and Technology

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

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