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

Lin Q, Li T, Chen Y, Lau SY, Wei M, Zhang Y, Zhang Z, Yao Q, Li J, Li Z, Wang D, Zheng Q, Yu H, Gu Y, Zhang J, Chen H, Li S, Xia N
J Virol 92 (2018)
Cited: 8 times
EuropePMC logo PMID: 29925655

Abstract

Human infection with highly pathogenic avian influenza A viruses causes severe disease and fatalities. We previously identified a potent and broadly neutralizing antibody (bnAb), 13D4, against the H5N1 virus. Here, we report the co-crystal structure of 13D4 in complex with the hemagglutinin (HA) of A/Vietnam/1194/2004 (H5N1). We show that heavy-chain complementarity-determining region 3 (HCDR3) of 13D4 confers broad yet specific neutralization against H5N1, undergoing conformational rearrangement to bind to the receptor binding site (RBS). Further, we show that mutating four critical residues within the RBS-Trp153, Lys156, Lys193, and Leu194-disrupts the binding between 13D4 and HA. Viruses bearing Asn193 instead of Lys/Arg can evade 13D4 neutralization, indicating that Lys193 polymorphism might be, at least in part, involved in the antigenicity of recent H5 genotypes (such as H5N6 and H5N8) as distinguished from H5N1. BnAb 13D4 may offers a template for therapeutic RBS inhibitor design and serve as an indicator of antigenic change for current H5 viruses.

Reviews - 6a0z mentioned but not cited (1)

  1. Analysis of the conserved protective epitopes of hemagglutinin on influenza A viruses. Jiao C, Wang B, Chen P, Jiang Y, Liu J. Front Immunol 14 1086297 (2023)

Articles - 6a0z mentioned but not cited (2)

  1. An expanded benchmark for antibody-antigen docking and affinity prediction reveals insights into antibody recognition determinants. Guest JD, Vreven T, Zhou J, Moal I, Jeliazkov JR, Gray JJ, Weng Z, Pierce BG. Structure 29 606-621.e5 (2021)
  2. Structural Basis for the Broad, Antibody-Mediated Neutralization of H5N1 Influenza Virus. Lin Q, Li T, Chen Y, Lau SY, Wei M, Zhang Y, Zhang Z, Yao Q, Li J, Li Z, Wang D, Zheng Q, Yu H, Gu Y, Zhang J, Chen H, Li S, Xia N. J Virol 92 e00547-18 (2018)


Reviews citing this publication (1)

  1. Inducing broad-based immunity against viruses with pandemic potential. Sette A, Saphire EO. Immunity 55 738-748 (2022)

Articles citing this publication (4)

  1. An IgM antibody targeting the receptor binding site of influenza B blocks viral infection with great breadth and potency. Shen C, Zhang M, Chen Y, Zhang L, Wang G, Chen J, Chen S, Li Z, Wei F, Chen J, Yang K, Guo S, Wang Y, Zheng Q, Yu H, Luo W, Zhang J, Chen H, Chen Y, Xia N. Theranostics 9 210-231 (2019)
  2. Identification of a cross-neutralizing antibody that targets the receptor binding site of H1N1 and H5N1 influenza viruses. Li T, Chen J, Zheng Q, Xue W, Zhang L, Rong R, Zhang S, Wang Q, Hong M, Zhang Y, Cui L, He M, Lu Z, Zhang Z, Chi X, Li J, Huang Y, Wang H, Tang J, Ying D, Zhou L, Wang Y, Yu H, Zhang J, Gu Y, Chen Y, Li S, Xia N. Nat Commun 13 5182 (2022)
  3. Identification of Hemagglutinin Mutations Caused by Neuraminidase Antibody Pressure. Wang F, Wan Z, Wang Y, Wu J, Fu H, Gao W, Shao H, Qian K, Ye J, Qin A. Microbiol Spectr 9 e0143921 (2021)
  4. A stepwise docking molecular dynamics approach for simulating antibody recognition with substantial conformational changes. Huang Y, Li Z, Hong Q, Zhou L, Ma Y, Hu Y, Xin J, Li T, Kong Z, Zheng Q, Chen Y, Zhao Q, Gu Y, Zhang J, Wang Y, Yu H, Li S, Xia N. Comput Struct Biotechnol J 20 710-720 (2022)


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