Structural basis for germ-line gene usage of a potent class of antibodies targeting the CD4-binding site of HIV-1 gp120

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

Volumn 109, Issue 30, 2012, Pages

  West, Anthony P ^a   Diskin, Ron ^a   Nussenzweig, Michel C ^b   Bjorkman, Pamela J ^a  

^a CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

^b ROCKEFELLER UNIVERSITY   (United States)

Author keywords

Analysis; Selection

Indexed keywords

CD4 ANTIGEN; GLYCOPROTEIN GP 120; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY;

ANTIBODY COMBINING SITE; ANTIBODY DETECTION; ANTIBODY STRUCTURE; ARTICLE; BINDING ASSAY; CRYSTAL STRUCTURE; DRUG POTENCY; GERM LINE; HUMAN IMMUNODEFICIENCY VIRUS 1; IN VITRO STUDY; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; SEQUENCE ALIGNMENT; VIRUS ENVELOPE; VIRUS NEUTRALIZATION;

HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 84864363185     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1208984109     Document Type: Article

References (42)

1. Wei X, et al. (2003) Antibody neutralization and escape by HIV-1. Nature 422: 307-312. (Pubitemid 36378357)
2. Kwong PD, et al. (2002) HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites. Nature 420:678-682. (Pubitemid 36764500)
3. Labrijn AF, et al. (2003) Access of antibody molecules to the conserved coreceptor binding site on glycoprotein gp120 is sterically restricted on primary human immunodeficiency virus type 1. J Virol 77:10557-10565. (Pubitemid 37129699)
4. Kwong PD, et al. (1998) Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393:648-659. (Pubitemid 28289647)
5. Wyatt R, et al. (1997) Analysis of the interaction of the human immunodeficiency virus type 1 gp120 envelope glycoprotein with the gp41 transmembrane glycoprotein. J Virol 71:9722-9731. (Pubitemid 27492421)
6. Moore JP, Sodroski J (1996) Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein. J Virol 70:1863-1872. (Pubitemid 26062950)
7. Starcich BR, et al. (1986) Identification and characterization of conserved and variable regions in the envelope gene of HTLV-III/LAV, the retrovirus of AIDS. Cell 45:637-648. (Pubitemid 16063128)
8. Klein JS, Bjorkman PJ (2010) Few and far between: How HIV may be evading antibody avidity. PLoS Pathog 6:e1000908.
9. Mouquet H, et al. (2010) Polyreactivity increases the apparent affinity of anti-HIV antibodies by heteroligation. Nature 467:591-595.
10. Gray ES, et al.; and the CAPRISA002 Study Team (2011) The neutralization breadth of HIV-1 develops incrementally over four years and is associated with CD4+ T cell decline and high viral load during acute infection. J Virol 85:4828-4840.
11. Mikell I, et al. (2011) Characteristics of the earliest cross-neutralizing antibody response to HIV-1. PLoS Pathog 7:e1001251.
12. Muster T, et al. (1993) A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1. J Virol 67:6642-6647. (Pubitemid 23309131)
13. Buchacher A, et al. (1994) Generation of human monoclonal antibodies against HIV-1 proteins; electrofusion and Epstein-Barr virus transformation for peripheral blood lymphocyte immortalization. AIDS Res Hum Retroviruses 10:359-369. (Pubitemid 24141210)
14. Trkola A, et al. (1996) Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1. J Virol 70:1100-1108. (Pubitemid 26029030)
15. Burton DR, et al. (1994) Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody. Science 266:1024-1027. (Pubitemid 24373715)
16. Scheid JF, et al. (2009) Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals. Nature 458:636-640.
17. Scheid JF, et al. (2009) A method for identification of HIV gp140 binding memory B cells in human blood. J Immunol Methods 343:65-67.
18. Walker LM, et al.; Protocol G Principal Investigators (2009) Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 326:285-289.
19. Walker LM, et al.; Protocol G Principal Investigators (2011) Broad neutralization coverage of HIV by multiple highly potent antibodies. Nature 477:466-470.
20. Wu X, et al. (2010) Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1. Science 329:856-861.
21. Wu X, et al.; NISC Comparative Sequencing Program (2011) Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing. Science 333:1593-1602.
22. Corti D, et al. (2010) Analysis of memory B cell responses and isolation of novel monoclonal antibodies with neutralizing breadth from HIV-1-infected individuals. PLoS ONE 5:e8805.
23. Scheid JF, et al. (2011) Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding. Science 333:1633-1637.
24. Diskin R, et al. (2011) Increasing the potency and breadth of an HIV antibody by using structure-based rational design. Science 334:1289-1293.
25. Zhou T, et al. (2010) Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01. Science 329:811-817.
26. Lefranc MP, Lefranc G (2001) The Immunoglobulin FactsBook (Academic, London).
27. Wu X, et al. (2012) Selection pressure on HIV-1 envelope by broadly neutralizing antibodies to the conserved CD4-binding site. J Virol 86:5844-5856.
28. Xiao X, et al. (2009) Germline-like predecessors of broadly neutralizing antibodies lack measurable binding to HIV-1 envelope glycoproteins: Implications for evasion of immune responses and design of vaccine immunogens. Biochem Biophys Res Commun 390:404-409.
29. Lefranc MP, et al. (2009) IMGT, the international ImMunoGeneTics information system. Nucleic Acids Res 37(Database issue):D1006-D1012.
30. Arnaout R, et al. (2011) High-resolution description of antibody heavy-chain repertoires in humans. PLoS ONE 6:e22365.
31. Thullier P, Chahboun S, Pelat T (2010) A comparison of human and macaque (Macaca mulatta) immunoglobulin germline V regions and its implications for antibody engineering. MAbs 2:528-538.
32. Brochet X, Lefranc MP, Giudicelli V (2008) IMGT/V-QUEST: The highly customized and integrated system for IG and TR standardized V-J and V-D-J sequence analysis. Nucleic Acids Res 36(Web Server issue):W503-W508.
33. Mascola JR, Montefiori DC (2010) The role of antibodies in HIV vaccines. Annu Rev Immunol 28:413-444.
34. Dunlop DC, et al. (2010) Polysaccharide mimicry of the epitope of the broadly neutralizing anti-HIV antibody, 2G12, induces enhanced antibody responses to self oligomannose glycans. Glycobiology 20:812-823.
35. Correia BE, et al. (2010) Computational design of epitope-scaffolds allows induction of antibodies specific for a poorly immunogenic HIV vaccine epitope. Structure 18:1116-1126.
36. Guenaga J, et al. (2011) Heterologous epitope-scaffold prime:boosting immunofocuses B cell responses to the HIV-1 gp41 2F5 neutralization determinant. PLoS ONE 6:e16074.
37. Feng Y, et al. (2012) Biochemically defined HIV-1 envelope glycoprotein variant immunogens display differential binding and neutralizing specificities to the CD4-binding site. J Biol Chem 287:5673-5686.
38. Nabel G, Kwong P, Mascola J (2011) Progress in the rational design of an AIDS vaccine. Philos Trans R Soc Biol Sci 366(1579):2759-2765.
39. Lonberg N (2005) Human antibodies from transgenic animals. Nat Biotechnol 23:1117-1125.
40. Durocher Y, Perret S, Kamen A (2002) High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells. Nucleic Acids Res 30:E9.
41. Li M, et al. (2005) Human immunodeficiency virus type 1 env clones from acute and early subtype B infections for standardized assessments of vaccine-elicited neutralizing antibodies. J Virol 79:10108-10125. (Pubitemid 41098552)
42. Montefiori DC (2005) Evaluating neutralizing antibodies against HIV, SIV, and SHIV in luciferase reporter gene assays. Current Protocols in Immunology, eds Coligan JE, et al. (John Wiley & Sons, New York), Chap 12, Unit 12.11.