Broadly neutralizing human antibody that recognizes the receptor-binding pocket of influenza virus hemagglutinin

Proceedings of the National Academy of Sciences of the United States of America

Volumn 108, Issue 34, 2011, Pages 14216-14221

  Whittle, James R R ^a   Zhang, Ruijun ^b   Khurana, Surender ^c   King, Lisa R ^c   Manischewitz, Jody ^c   Golding, Hana ^c   Dormitzer, Philip R ^d   Haynes, Barton F ^b   Walter, Emmanuel B ^b   Moody, M Anthony ^b   Kepler, Thomas B ^b   Liao, Hua Xin ^b   Harrison, Stephen C ^a  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^b DUKE UNIVERSITY MEDICAL CENTER   (United States)

^c CENTER FOR BIOLOGICS EVALUATION AND RESEARCH   (United States)

^d NOVARTIS VACCINES AND DIAGNOSTICS   (United States)

Author keywords

Affinity maturation; B cell lineage; X ray crystallography

Indexed keywords

INFLUENZA VACCINE; INFLUENZA VIRUS HEMAGGLUTININ; NEUTRALIZING ANTIBODY; SIALIC ACID;

ARTICLE; CELL SELECTION; COMPLEMENTARITY DETERMINING REGION; CONTROLLED STUDY; CRYSTAL STRUCTURE; GENE ISOLATION; HUMAN; HUMAN CELL; INFLUENZA VIRUS A H1N1; PLASMA CELL; PRIORITY JOURNAL; PROTEIN INTERACTION; RECEPTOR BINDING; VIRUS INFECTIVITY; VIRUS STRAIN;

AMINO ACID SEQUENCE; ANTIBODIES, MONOCLONAL; ANTIBODIES, NEUTRALIZING; ANTIBODIES, VIRAL; ANTIBODY AFFINITY; ANTIBODY SPECIFICITY; BINDING SITES; COMPLEMENTARITY DETERMINING REGIONS; GLYCOSYLATION; HEMAGGLUTININ GLYCOPROTEINS, INFLUENZA VIRUS; HUMANS; INFLUENZA A VIRUS, H1N1 SUBTYPE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHYLOGENY; PROTEIN BINDING; RECEPTORS, VIRUS;

ORTHOMYXOVIRIDAE;

EID: 80052184942     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1111497108     Document Type: Article

References (28)

1. Skehel JJ, Wiley DC (2000) Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin. Annu Rev Biochem 69:531-569.
2. Knossow M, Skehel JJ (2006) Variation and infectivity neutralization in influenza. Immunology 119:1-7. (Pubitemid 44201150)
3. Wiley DC, Skehel JJ (1987) The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu Rev Biochem 56:365-394.
4. Fleury D, Wharton SA, Skehel JJ, Knossow M, Bizebard T (1998) Antigen distortion allows influenza virus to escape neutralization. Nat Struct Biol 5:119-123.
5. Barbey-Martin C, et al. (2002) An antibody that prevents the hemagglutinin low pH fusogenic transition. Virology 294:70-74. (Pubitemid 34921290)
6. Liao HX, et al. (2009) High-throughput isolation of immunoglobulin genes from single human B cells and expression as monoclonal antibodies. J Virol Methods 158:171-179.
7. Gamblin SJ, et al. (2004) The structure and receptor binding properties of the 1918 influenza hemagglutinin. Science 303:1838-1842. (Pubitemid 38374870)
8. Xu R, et al. (2010) Structural basis of preexisting immunity to the 2009 H1N1 pandemic influenza virus. Science 328:357-360.
9. Zhang W, et al. (2010) Crystal structure of the swine-origin A (H1N1)-2009 influenza A virus hemagglutinin (HA) reveals similar antigenicity to that of the 1918 pandemic virus. Protein Cell 1:459-467.
10. Caton AJ, Brownlee GG, Yewdell JW, GerhardW (1982) The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (H1 subtype). Cell 31:417-427. (Pubitemid 13178866)
11. Wei CJ, et al. (2010) Cross-neutralization of 1918 and 2009 influenza viruses: Role of glycans in viral evolution and vaccine design. Sci Transl Med 2(24): 24ra21.
12. Wrammert J, et al. (2008) Rapid cloning of high-affinity human monoclonal antibodies against influenza virus. Nature 453:667-671. (Pubitemid 351769295)
13. Volpe JM, Kepler TB (2008) Large-scale analysis of human heavy chain V(D)J recombination patterns. Immunome Res 4:3.
14. Wiley DC, Wilson IA, Skehel JJ (1981) Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation. Nature 289:373-378.
15. Wilson IA, Skehel JJ, Wiley DC (1981) Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature 289:366-373.
16. Zhou T, et al. (2010) Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01. Science 329:811-817.
17. Ma B-J, et al. (2011) Envelope deglycosylation enhances antigenicity of HIV-1 gp41 neutralizing eptiopes for broad neutralizing antibodies and their putative germlines. PLoS Pathog, in press.
18. Dharan NJ, et al.; Oseltamivir-Resistance Working Group (2009) Infections with oseltamivir-resistant influenza A(H1N1) virus in the United States. JAMA 301: 1034-1041.
19. Simmons CP, et al. (2007) Prophylactic and therapeutic efficacy of human monoclonal antibodies against H5N1 influenza. PLoS Med 4:e178.
20. Ewing B, Hillier L, Wendl MC, Green P (1998) Base-calling of automated sequencer traces using phred. I. Accuracy assessment. Genome Res 8:175-185. (Pubitemid 28177229)
21. Kepler TB, et al. (2010) Chiropteran types I and II interferon genes inferred from genome sequencing traces by a statistical gene-family assembler. BMC Genomics 11:444.
22. Felsenstein J (1981) Evolutionary trees from DNA sequences: A maximum likelihood approach. J Mol Evol 17:368-376.
23. Nicely NI, et al. (2010) Crystal structure of a non-neutralizing antibody to the HIV-1 gp41 membrane-proximal external region. Nat Struct Mol Biol 17:1492-1494.
24. Hancock K, et al. (2009) Cross-reactive antibody responses to the 2009 pandemic H1N1 influenza virus. N Engl J Med 361:1945-1952.
25. McCoy AJ, et al. (2007) Phaser crystallographic software. J Appl Cryst 40:658-674. (Pubitemid 47080256)
26. Brunger AT (2007) Version 1.2 of the Crystallography and NMR system. Nat Protoc 2: 2728-2733.
27. Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60(Pt 12 Pt 1):2126-2132. (Pubitemid 41742764)
28. Adams PD, et al. (2002) PHENIX: Building new software for automated crystallographic structure determination. Acta Crystallogr D Biol Crystallogr 58:1948-1954. (Pubitemid 35337293)