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Volumn 125, Issue 6, 2015, Pages 2523-2531

Redesigned HIV antibodies exhibit enhanced neutralizing potency and breadth

Author keywords

[No Author keywords available]

Indexed keywords

HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; NEUTRALIZING ANTIBODY; PG9 ANTIBODY; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN; COMPLEMENTARITY DETERMINING REGION; GLYCOPROTEIN GP 160; GP160 PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 84930389498     PISSN: 00219738     EISSN: 15588238     Source Type: Journal    
DOI: 10.1172/JCI80693     Document Type: Article
Times cited : (26)

References (47)
  • 1
    • 84875551472 scopus 로고    scopus 로고
    • Broadly neutralizing antiviral antibodies
    • Corti D, Lanzavecchia A. Broadly neutralizing antiviral antibodies. Annu Rev Immunol. 2013;31: 705-742.
    • (2013) Annu Rev Immunol , vol.31 , pp. 705-742
    • Corti, D.1    Lanzavecchia, A.2
  • 2
    • 83455254775 scopus 로고    scopus 로고
    • Structure of HIV-1 gp120 V1/ V2 domain with broadly neutralizing antibody PG9
    • McLellan JS, et al. Structure of HIV-1 gp120 V1/ V2 domain with broadly neutralizing antibody PG9. Nature. 2011;480(7377): 336-343.
    • (2011) Nature , vol.480 , Issue.7377 , pp. 336-343
    • McLellan, J.S.1
  • 3
    • 80053132436 scopus 로고    scopus 로고
    • Broad neutralization coverage of HIV by multiple highly potent antibodies
    • Walker LM, et al. Broad neutralization coverage of HIV by multiple highly potent antibodies. Nature. 2011;477(7365): 466-470.
    • (2011) Nature , vol.477 , Issue.7365 , pp. 466-470
    • Walker, L.M.1
  • 4
    • 77954912140 scopus 로고    scopus 로고
    • Structure and function of broadly reactive antibody PG16 reveal an H3 subdomain that mediates potent neutralization of HIV-1
    • Pejchal R, et al. Structure and function of broadly reactive antibody PG16 reveal an H3 subdomain that mediates potent neutralization of HIV-1. Proc Natl Acad Sci USA. 2010;107(25): 11483-11488.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.25 , pp. 11483-11488
    • Pejchal, R.1
  • 5
    • 77954982131 scopus 로고    scopus 로고
    • Crystal structure of PG16 and chimeric dissection with somatically related PG9: Structure-function analysis of two quaternary- specific antibodies that effectively neutralize HIV-1
    • Pancera M, et al. Crystal structure of PG16 and chimeric dissection with somatically related PG9: Structure-function analysis of two quaternary- specific antibodies that effectively neutralize HIV-1. J Virol. 2010;84(16): 8098-8110.
    • (2010) J Virol , vol.84 , Issue.16 , pp. 8098-8110
    • Pancera, M.1
  • 6
    • 84880149399 scopus 로고    scopus 로고
    • Structural basis for diverse N-glycan recognition by HIV-1-neutralizing V1-V2-directed antibody PG16
    • Pancera M, et al. Structural basis for diverse N-glycan recognition by HIV-1-neutralizing V1-V2-directed antibody PG16. Nat Struct Mol Biol. 2013;20(7): 804-813.
    • (2013) Nat Struct Mol Biol , vol.20 , Issue.7 , pp. 804-813
    • Pancera, M.1
  • 7
    • 79956017135 scopus 로고    scopus 로고
    • Computational design of proteins targeting the conserved stem region of influenza hemagglutinin
    • Fleishman SJ, et al. Computational design of proteins targeting the conserved stem region of influenza hemagglutinin. Science. 2011;332(6031): 816-821.
    • (2011) Science , vol.332 , Issue.6031 , pp. 816-821
    • Fleishman, S.J.1
  • 8
    • 79959615159 scopus 로고    scopus 로고
    • RosettaScripts: A scripting language interface to the Rosetta macromolecular modeling suite
    • Fleishman SJ, et al. RosettaScripts: A scripting language interface to the Rosetta macromolecular modeling suite. PLoS One. 2011;6(6): E20161.
    • (2011) PLoS One , vol.6 , Issue.6 , pp. e20161
    • Fleishman, S.J.1
  • 9
    • 0034641749 scopus 로고    scopus 로고
    • Native protein sequences are close to optimal for their structures
    • Kuhlman B, Baker D. Native protein sequences are close to optimal for their structures. Proc Natl Acad Sci USA. 2000;97(19): 10383-10388.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.19 , pp. 10383-10388
    • Kuhlman, B.1    Baker, D.2
  • 10
    • 77950673061 scopus 로고    scopus 로고
    • Practically useful: What the Rosetta protein modeling suite can do for you
    • Kaufmann KW, Lemmon GH, Deluca SL, Sheehan JH, Meiler J. Practically useful: What the Rosetta protein modeling suite can do for you. Biochemistry. 2010;49(14): 2987-2998.
    • (2010) Biochemistry , vol.49 , Issue.14 , pp. 2987-2998
    • Kaufmann, K.W.1    Lemmon, G.H.2    Deluca, S.L.3    Sheehan, J.H.4    Meiler, J.5
  • 11
    • 0004032583 scopus 로고
    • Bethesda, Maryland, USA: US Department of Health and Human Services, Public Health Service, National Institutes of Health
    • Kabat EA. Sequences of Proteins of Immunological Interest. Bethesda, Maryland, USA: US Department of Health and Human Services, Public Health Service, National Institutes of Health; 1991.
    • (1991) Sequences of Proteins of Immunological Interest
    • Kabat, E.A.1
  • 12
    • 70349887757 scopus 로고    scopus 로고
    • Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target
    • Walker LM, et al. Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science. 2009;326(5950): 285-289.
    • (2009) Science , vol.326 , Issue.5950 , pp. 285-289
    • Walker, L.M.1
  • 13
    • 23244434512 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 env clones from acute and early subtype B infections for standardized assessments of vaccine-elicited neutralizing antibodies
    • Li M, et al. Human immunodeficiency virus type 1 env clones from acute and early subtype B infections for standardized assessments of vaccine-elicited neutralizing antibodies. J Virol. 2005;79(16): 10108-10125.
    • (2005) J Virol , vol.79 , Issue.16 , pp. 10108-10125
    • Li, M.1
  • 14
    • 33751224478 scopus 로고    scopus 로고
    • Genetic and neutralization properties of subtype C human immunodeficiency virus type 1 molecular env clones from acute and early heterosexually acquired infections in Southern Africa
    • Li M, et al. Genetic and neutralization properties of subtype C human immunodeficiency virus type 1 molecular env clones from acute and early heterosexually acquired infections in Southern Africa. J Virol. 2006;80(23): 11776-11790.
    • (2006) J Virol , vol.80 , Issue.23 , pp. 11776-11790
    • Li, M.1
  • 15
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K. Coot: Model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr. 2004;60(pt 12 pt 1): 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 16
    • 84875034460 scopus 로고    scopus 로고
    • Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9
    • Julien JP, et al. Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9. Proc Natl Acad Sci USA. 2013;110(11): 4351-4356.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.11 , pp. 4351-4356
    • Julien, J.P.1
  • 17
    • 0036333661 scopus 로고    scopus 로고
    • Stabilization of the soluble, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1
    • Sanders RW, et al. Stabilization of the soluble, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1. J Virol. 2002;76(17): 8875-8889.
    • (2002) J Virol , vol.76 , Issue.17 , pp. 8875-8889
    • Sanders, R.W.1
  • 18
    • 84884678235 scopus 로고    scopus 로고
    • A next-generation cleaved, soluble HIV-1 Env Trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodies
    • Sanders RW, et al. A next-generation cleaved, soluble HIV-1 Env Trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodies. PLoS Pathog. 2013;9(9): E1003618.
    • (2013) PLoS Pathog , vol.9 , Issue.9 , pp. e1003618
    • Sanders, R.W.1
  • 19
    • 60349089294 scopus 로고    scopus 로고
    • Measuring HIV neutralization in a luciferase reporter gene assay
    • Montefiori DC. Measuring HIV neutralization in a luciferase reporter gene assay. Methods Mol Biol. 2009;485: 395-405.
    • (2009) Methods Mol Biol , vol.485 , pp. 395-405
    • Montefiori, D.C.1
  • 20
    • 77957198704 scopus 로고    scopus 로고
    • Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16
    • Doores KJ, Doores KJ, Burton DR, Burton DR. Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16. J Virol. 2010;84(20): 10510-10521.
    • (2010) J Virol , vol.84 , Issue.20 , pp. 10510-10521
    • Doores, K.J.1    Doores, K.J.2    Burton, D.R.3    Burton, D.R.4
  • 21
    • 33847416982 scopus 로고    scopus 로고
    • A broad range of Fab stabilities within a host of therapeutic IgGs
    • Garber E, Demarest SJ. A broad range of Fab stabilities within a host of therapeutic IgGs. Biochem Biophys Res Commun. 2007;355(3): 751-757.
    • (2007) Biochem Biophys Res Commun , vol.355 , Issue.3 , pp. 751-757
    • Garber, E.1    Demarest, S.J.2
  • 22
    • 43249105327 scopus 로고    scopus 로고
    • Contribution of variable domains to the stability of humanized IgG1 monoclonal antibodies
    • Ionescu RM, Vlasak J, Price C, Kirchmeier M. Contribution of variable domains to the stability of humanized IgG1 monoclonal antibodies. J Pharm Sci. 2008;97(4): 1414-1426.
    • (2008) J Pharm Sci , vol.97 , Issue.4 , pp. 1414-1426
    • Ionescu, R.M.1    Vlasak, J.2    Price, C.3    Kirchmeier, M.4
  • 24
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study
    • Privalov PL, Khechinashvili NN. A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study. J Mol Biol. 1974;86(3): 665-684.
    • (1974) J Mol Biol , vol.86 , Issue.3 , pp. 665-684
    • Privalov, P.L.1    Khechinashvili, N.N.2
  • 25
    • 15444365480 scopus 로고    scopus 로고
    • Defective B cell tolerance checkpoints in systemic lupus erythematosus
    • Yurasov S. Defective B cell tolerance checkpoints in systemic lupus erythematosus. J Exp Med. 2005;201(5): 703-711.
    • (2005) J Exp Med , vol.201 , Issue.5 , pp. 703-711
    • Yurasov, S.1
  • 26
    • 84860706280 scopus 로고    scopus 로고
    • Human peripheral blood antibodies with long HCDR3s are established primarily at original recombination using a limited subset of germline genes
    • Briney BS, Willis JR, Crowe JE. Human peripheral blood antibodies with long HCDR3s are established primarily at original recombination using a limited subset of germline genes. PLoS One. 2012;7(5): E36750.
    • (2012) PLoS One , vol.7 , Issue.5 , pp. e36750
    • Briney, B.S.1    Willis, J.R.2    Crowe, J.E.3
  • 27
    • 21344434534 scopus 로고    scopus 로고
    • Cardiolipin polyspecific autoreactivity in two broadly neutralizing HIV-1 antibodies
    • Haynes BF, et al. Cardiolipin polyspecific autoreactivity in two broadly neutralizing HIV-1 antibodies. Science. 2005;308(5730): 1906-1908.
    • (2005) Science , vol.308 , Issue.5730 , pp. 1906-1908
    • Haynes, B.F.1
  • 28
    • 84902544617 scopus 로고    scopus 로고
    • Motavizumab treatment of infants hospitalized with respiratory syncytial virus infection does not decrease viral load or severity of illness
    • Ramilo O, et al. Motavizumab treatment of infants hospitalized with respiratory syncytial virus infection does not decrease viral load or severity of illness. Pediatr Infect Dis J. 2014;33(7): 703-709.
    • (2014) Pediatr Infect Dis J , vol.33 , Issue.7 , pp. 703-709
    • Ramilo, O.1
  • 29
    • 84875759341 scopus 로고    scopus 로고
    • Somatic mutations of the immunoglobulin framework are generally required for broad and potent HIV-1 neutralization
    • Klein F, et al. Somatic mutations of the immunoglobulin framework are generally required for broad and potent HIV-1 neutralization. Cell. 2013;153(1): 126-138.
    • (2013) Cell , vol.153 , Issue.1 , pp. 126-138
    • Klein, F.1
  • 31
    • 84871994029 scopus 로고    scopus 로고
    • Preconfiguration of the antigen- binding site during affinity maturation of a broadly neutralizing influenza virus antibody
    • Schmidt AG, et al. Preconfiguration of the antigen- binding site during affinity maturation of a broadly neutralizing influenza virus antibody. Proc Natl Acad Sci USA. 2013;110(1): 264-269.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.1 , pp. 264-269
    • Schmidt, A.G.1
  • 32
    • 79551493763 scopus 로고    scopus 로고
    • Effects of somatic mutations on CDR loop flexibility during affinity maturation
    • Wong SE, Sellers BD, Jacobson MP. Effects of somatic mutations on CDR loop flexibility during affinity maturation. Proteins. 2011;79(3): 821-829.
    • (2011) Proteins , vol.79 , Issue.3 , pp. 821-829
    • Wong, S.E.1    Sellers, B.D.2    Jacobson, M.P.3
  • 34
    • 0030821164 scopus 로고    scopus 로고
    • Structural insights into the evolution of an antibody combining site
    • Wedemayer GJ, Patten PA, Wang LH, Schultz PG, Stevens RC. Structural insights into the evolution of an antibody combining site. Science. 1997;276(5319): 1665-1669.
    • (1997) Science , vol.276 , Issue.5319 , pp. 1665-1669
    • Wedemayer, G.J.1    Patten, P.A.2    Wang, L.H.3    Schultz, P.G.4    Stevens, R.C.5
  • 35
    • 84917705974 scopus 로고    scopus 로고
    • Recombinant HIV envelope trimer selects for quaternary-dependent antibodies targeting the trimer apex
    • Sok D, et al. Recombinant HIV envelope trimer selects for quaternary-dependent antibodies targeting the trimer apex. Proc Natl Acad Sci USA. 2014;111(49): 17624-17629.
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.49 , pp. 17624-17629
    • Sok, D.1
  • 36
    • 84896315237 scopus 로고    scopus 로고
    • Proof of principle for epitope-focused vaccine design
    • Correia BE, et al. Proof of principle for epitope-focused vaccine design. Nature. 2014;507(7491): 201-206.
    • (2014) Nature , vol.507 , Issue.7491 , pp. 201-206
    • Correia, B.E.1
  • 37
    • 84877609579 scopus 로고    scopus 로고
    • Rational HIV immunogen design to target specific germline B cell receptors
    • Jardine J, et al. Rational HIV immunogen design to target specific germline B cell receptors. Science. 2013;340(6133): 711-716.
    • (2013) Science , vol.340 , Issue.6133 , pp. 711-716
    • Jardine, J.1
  • 38
    • 84887277978 scopus 로고    scopus 로고
    • Structure-based design of a fusion glycoprotein vaccine for respiratory syncytial virus
    • McLellan JS, et al. Structure-based design of a fusion glycoprotein vaccine for respiratory syncytial virus. Science. 2013;342(6158): 592-598.
    • (2013) Science , vol.342 , Issue.6158 , pp. 592-598
    • McLellan, J.S.1
  • 39
    • 84860432843 scopus 로고    scopus 로고
    • Prediction of HIV-1 protease/inhibitor affinity using RosettaLigand
    • Lemmon G, Kaufmann K, Meiler J. Prediction of HIV-1 protease/inhibitor affinity using RosettaLigand. Chem Biol Drug Des. 2012;79(6): 888-896.
    • (2012) Chem Biol Drug Des , vol.79 , Issue.6 , pp. 888-896
    • Lemmon, G.1    Kaufmann, K.2    Meiler, J.3
  • 40
    • 77951165843 scopus 로고    scopus 로고
    • Structural basis of preexisting immunity to the 2009 H1N1 pandemic influenza virus
    • Xu R, Ekiert DC, Krause JC, Hai R, Crowe JE Jr, Wilson IA. Structural basis of preexisting immunity to the 2009 H1N1 pandemic influenza virus. Science. 2010;328(5976): 357-360.
    • (2010) Science , vol.328 , pp. 357-360
    • Xu, R.1    Ekiert, D.C.2    Krause, J.C.3    Hai, R.4    Crowe, J.E.5    Wilson, I.A.6
  • 41
    • 45849125030 scopus 로고    scopus 로고
    • Evaluating neutralizing antibodies against HIV, SIV, and SHIV in luciferase reporter gene assays
    • Chapter 12: Unit 12.11
    • Montefiori DC. Evaluating neutralizing antibodies against HIV, SIV, and SHIV in luciferase reporter gene assays. Curr Protoc Immunol. 2005;Chapter 12: Unit 12.11.
    • (2005) Curr Protoc Immunol
    • Montefiori, D.C.1
  • 42
    • 84906084946 scopus 로고    scopus 로고
    • Optimization and validation of the TZM-bl assay for standardized assessments of neutralizing antibodies against HIV-1
    • Sarzotti-Kelsoe M, et al. Optimization and validation of the TZM-bl assay for standardized assessments of neutralizing antibodies against HIV-1. J Immunol Methods. 2014;409: 131-146.
    • (2014) J Immunol Methods , vol.409 , pp. 131-146
    • Sarzotti-Kelsoe, M.1
  • 43
    • 76449106188 scopus 로고    scopus 로고
    • Integration, scaling, space-group assignment and post-refinement
    • Kabsch W. Integration, scaling, space-group assignment and post-refinement. Acta Crystallogr D Biol Crystallogr. 2010;66(pt 2): 125-132.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 125-132
    • Kabsch, W.1
  • 45
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr. 2010;66(pt 2): 213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 46
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera - A visualization system for exploratory research and analysis
    • Pettersen EF, et al. UCSF Chimera - A visualization system for exploratory research and analysis. J Comput Chem. 2004;25(13): 1605-1612.
    • (2004) J Comput Chem , vol.25 , Issue.13 , pp. 1605-1612
    • Pettersen, E.F.1
  • 47
    • 0345276458 scopus 로고    scopus 로고
    • IMGT-ONTOLOGY and IMGT databases, tools and Web resources for immunogenetics and immunoinformatics
    • Lefranc MP. IMGT-ONTOLOGY and IMGT databases, tools and Web resources for immunogenetics and immunoinformatics. Mol Immunol. 2004;40(10): 647-660.
    • (2004) Mol Immunol , vol.40 , Issue.10 , pp. 647-660
    • Lefranc, M.P.1


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