메뉴 건너뛰기




Volumn 111, Issue 7, 2014, Pages

Vaccine-elicited primate antibodies use a distinct approach to the HIV-1 primary receptor binding site informing vaccine redesign

Author keywords

Mode of recognition; Neutralizing antibodies; NHP

Indexed keywords

ALANINE; CD4 ANTIGEN; CHEMOKINE RECEPTOR CCR5; EPITOPE; GLYCOPROTEIN GP 120; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; IMMUNOGLOBULIN F(AB) FRAGMENT; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; VIRUS ENVELOPE PROTEIN; VIRUS RECEPTOR; FLUCICLOVINE F 18;

EID: 84894355475     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1319512111     Document Type: Article
Times cited : (62)

References (50)
  • 1
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: Fusogens, antigens, and immunogens
    • Wyatt R, Sodroski J (1998) The HIV-1 envelope glycoproteins: Fusogens, antigens, and immunogens. Science 280(5371):1884-1888.
    • (1998) Science , vol.280 , Issue.5371 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2
  • 2
    • 33847101745 scopus 로고    scopus 로고
    • Structural definition of a conserved neutralization epitope on HIV-1 gp120
    • Zhou T, et al. (2007) Structural definition of a conserved neutralization epitope on HIV-1 gp120. Nature 445(7129):732-737.
    • (2007) Nature , vol.445 , Issue.7129 , pp. 732-737
    • Zhou, T.1
  • 3
    • 77954920017 scopus 로고    scopus 로고
    • Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1
    • Wu X, et al. (2010) Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1. Science 329(5993):856-861.
    • (2010) Science , vol.329 , Issue.5993 , pp. 856-861
    • Wu, X.1
  • 4
    • 77954943648 scopus 로고    scopus 로고
    • Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01
    • Zhou T, et al. (2010) Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01. Science 329(5993):811-817.
    • (2010) Science , vol.329 , Issue.5993 , pp. 811-817
    • Zhou, T.1
  • 5
    • 80052925616 scopus 로고    scopus 로고
    • Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding
    • Scheid JF, et al. (2011) Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding. Science 333(6049):1633-1637.
    • (2011) Science , vol.333 , Issue.6049 , pp. 1633-1637
    • Scheid, J.F.1
  • 6
    • 84876797103 scopus 로고    scopus 로고
    • NISC Comparative Sequencing Program (2013) Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus
    • Liao HX, et al.; NISC Comparative Sequencing Program (2013) Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus. Nature 496(7446):469-476.
    • Nature , vol.496 , Issue.7446 , pp. 469-476
    • Liao, H.X.1
  • 7
    • 77649318846 scopus 로고    scopus 로고
    • Analysis of memory B cell responses and isolation of novel monoclonal antibodies with neutralizing breadth from HIV-1-infected individuals
    • 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(1):e8805.
    • (2010) PLoS ONE , vol.5 , Issue.1
    • Corti, D.1
  • 8
    • 82755184131 scopus 로고    scopus 로고
    • Increasing the potency and breadth of an HIV antibody by using structure-based rational design
    • Diskin R, et al. (2011) Increasing the potency and breadth of an HIV antibody by using structure-based rational design. Science 334(6060):1289-1293.
    • (2011) Science , vol.334 , Issue.6060 , pp. 1289-1293
    • Diskin, R.1
  • 9
    • 33846172297 scopus 로고    scopus 로고
    • Rational modifications of HIV-1 envelope glycoproteins for immunogen design
    • Phogat S, Wyatt R (2007) Rational modifications of HIV-1 envelope glycoproteins for immunogen design. Curr Pharm Des 13(2):213-227.
    • (2007) Curr Pharm Des , vol.13 , Issue.2 , pp. 213-227
    • Phogat, S.1    Wyatt, R.2
  • 10
    • 84876051105 scopus 로고    scopus 로고
    • Structural basis for HIV-1 gp120 recognition by a germ-line version of a broadly neutralizing antibody
    • Scharf L, et al. (2013) Structural basis for HIV-1 gp120 recognition by a germ-line version of a broadly neutralizing antibody. Proc Natl Acad Sci USA 110(15):6049-6054.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.15 , pp. 6049-6054
    • Scharf, L.1
  • 11
    • 84863915210 scopus 로고    scopus 로고
    • High-resolution definition of vaccine-elicited B cell responses against the HIV primary receptor binding site
    • Sundling C, et al. (2012) High-resolution definition of vaccine-elicited B cell responses against the HIV primary receptor binding site. Sci Transl Med 4(142):42ra96.
    • (2012) Sci Transl Med , vol.4 , Issue.142
    • Sundling, C.1
  • 12
    • 75449099267 scopus 로고    scopus 로고
    • Influence of novel CD4 binding-defective HIV-1 envelope glycoprotein immunogens on neutralizing antibody and T-cell responses in nonhuman primates
    • Douagi I, et al. (2010) Influence of novel CD4 binding-defective HIV-1 envelope glycoprotein immunogens on neutralizing antibody and T-cell responses in nonhuman primates. J Virol 84(4):1683-1695.
    • (2010) J Virol , vol.84 , Issue.4 , pp. 1683-1695
    • Douagi, I.1
  • 13
    • 84857306337 scopus 로고    scopus 로고
    • Biochemically defined HIV-1 envelope glycoprotein variant immunogens display differential binding and neutralizing specificities to the CD4-binding site
    • 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(8):5673-5686.
    • (2012) J Biol Chem , vol.287 , Issue.8 , pp. 5673-5686
    • Feng, Y.1
  • 14
    • 77956261658 scopus 로고    scopus 로고
    • Soluble HIV-1 Env trimers in adjuvant elicit potent and diverse functional B cell responses in primates
    • Sundling C, et al. (2010) Soluble HIV-1 Env trimers in adjuvant elicit potent and diverse functional B cell responses in primates. J Exp Med 207(9):2003-2017.
    • (2010) J Exp Med , vol.207 , Issue.9 , pp. 2017
    • Sundling, C.1
  • 15
    • 0027458347 scopus 로고
    • Neutralization of HIV-1 by F105, a human monoclonal antibody to the CD4 binding site of gp120
    • Posner MR, Cavacini LA, Emes CL, Power J, Byrn R (1993) Neutralization of HIV-1 by F105, a human monoclonal antibody to the CD4 binding site of gp120. J Acquir Immune Defic Syndr 6(1):7-14.
    • (1993) J Acquir Immune Defic Syndr , vol.6 , Issue.1 , pp. 7-14
    • Posner, M.R.1    Cavacini, L.A.2    Emes, C.L.3    Power, J.4    Byrn, R.5
  • 16
    • 0345832301 scopus 로고    scopus 로고
    • ClusPro: An automated docking and discrimination method for the prediction of protein complexes
    • Comeau SR, Gatchell DW, Vajda S, Camacho CJ (2004) ClusPro: An automated docking and discrimination method for the prediction of protein complexes. Bioinformatics 20(1):45-50.
    • (2004) Bioinformatics , vol.20 , Issue.1 , pp. 45-50
    • Comeau, S.R.1    Gatchell, D.W.2    Vajda, S.3    Camacho, C.J.4
  • 18
    • 84864603281 scopus 로고    scopus 로고
    • Structural mechanism of trimeric HIV-1 envelope glycoprotein activation
    • Tran EE, et al. (2012) Structural mechanism of trimeric HIV-1 envelope glycoprotein activation. PLoS Pathog 8(7):e1002797.
    • (2012) PLoS Pathog , vol.8 , Issue.7
    • Tran, E.E.1
  • 19
    • 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. (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(16):10108-10125.
    • (2005) J Virol , vol.79 , Issue.16 , pp. 10108-10125
    • Li, M.1
  • 20
    • 84863932778 scopus 로고    scopus 로고
    • Magnitude and breadth of the neutralizing antibody response in the RV144 and Vax003 HIV-1 vaccine efficacy trials
    • Montefiori DC, et al. (2012) Magnitude and breadth of the neutralizing antibody response in the RV144 and Vax003 HIV-1 vaccine efficacy trials. J Infect Dis 206(3): 431-441.
    • (2012) J Infect Dis , vol.206 , Issue.3 , pp. 431-441
    • Montefiori, D.C.1
  • 21
    • 77958041963 scopus 로고    scopus 로고
    • The JCSG high-throughput structural biology pipeline
    • Elsliger MA, et al. (2010) The JCSG high-throughput structural biology pipeline. Acta Crystallogr Sect F Struct Biol Cryst Commun 66(Pt 10):1137-1142.
    • (2010) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.66 , Issue.PART 10 , pp. 1137-1142
    • Elsliger, M.A.1
  • 22
    • 70450182950 scopus 로고    scopus 로고
    • Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120
    • Chen L, et al. (2009) Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120. Science 326(5956):1123-1127.
    • (2009) Science , vol.326 , Issue.5956 , pp. 1123-1127
    • Chen, L.1
  • 23
    • 80052942203 scopus 로고    scopus 로고
    • Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing
    • NISC Comparative Sequencing Program
    • Wu X, et al.; NISC Comparative Sequencing Program (2011) Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing. Science 333(6049):1593-1602.
    • (2011) Science , vol.333 , Issue.6049 , pp. 1593-1602
    • Wu, X.1
  • 24
    • 67249085575 scopus 로고    scopus 로고
    • Structure-based stabilization of HIV-1 gp120 enhances humoral immune responses to the induced co-receptor binding site
    • Dey B, et al. (2009) Structure-based stabilization of HIV-1 gp120 enhances humoral immune responses to the induced co-receptor binding site. PLoS Pathog 5(5): E1000445.
    • (2009) PLoS Pathog , vol.5 , Issue.5
    • Dey, B.1
  • 25
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • 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(6686): 648-659.
    • (1998) Nature , vol.393 , Issue.6686 , pp. 648-659
    • Kwong, P.D.1
  • 26
    • 26444450696 scopus 로고    scopus 로고
    • Dissection of the carbohydrate specificity of the broadly neutralizing anti-HIV-1 antibody 2G12
    • Calarese DA, et al. (2005) Dissection of the carbohydrate specificity of the broadly neutralizing anti-HIV-1 antibody 2G12. Proc Natl Acad Sci USA 102(38):13372-13377.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.38 , pp. 13372-13377
    • Calarese, D.A.1
  • 27
    • 12444291017 scopus 로고    scopus 로고
    • Antibody domain exchange is an immunological solution to carbohydrate cluster recognition
    • Calarese DA, et al. (2003) Antibody domain exchange is an immunological solution to carbohydrate cluster recognition. Science 300(5628):2065-2071.
    • (2003) Science , vol.300 , Issue.5628 , pp. 2065-2071
    • Calarese, D.A.1
  • 28
    • 80053132436 scopus 로고    scopus 로고
    • Broad neutralization coverage of HIV by multiple highly potent antibodies
    • Protocol G Principal Investigators
    • Walker LM, et al.; Protocol G Principal Investigators (2011) Broad neutralization coverage of HIV by multiple highly potent antibodies. Nature 477(7365):466-470.
    • (2011) Nature , vol.477 , Issue.7365 , pp. 466-470
    • Walker, L.M.1
  • 29
    • 84878519611 scopus 로고    scopus 로고
    • Broadly neutralizing antibody PGT121 allosterically modulates CD4 binding via recognition of the HIV-1 gp120 V3 base and multiple surrounding glycans
    • Julien JP, et al. (2013) Broadly neutralizing antibody PGT121 allosterically modulates CD4 binding via recognition of the HIV-1 gp120 V3 base and multiple surrounding glycans. PLoS Pathog 9(5):e1003342.
    • (2013) PLoS Pathog , vol.9 , Issue.5
    • Julien, J.P.1
  • 30
    • 84883275866 scopus 로고    scopus 로고
    • Structural characterization of cleaved, soluble HIV-1 envelope glycoprotein trimers
    • Khayat R, et al. (2013) Structural characterization of cleaved, soluble HIV-1 envelope glycoprotein trimers. J Virol 87(17):9865-9872.
    • (2013) J Virol , vol.87 , Issue.17 , pp. 9865-9872
    • Khayat, R.1
  • 31
    • 84875034460 scopus 로고    scopus 로고
    • Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9
    • Julien JP, et al. (2013) Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9. Proc Natl Acad Sci USA 110(11):4351-4356.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.11 , pp. 4351-4356
    • Julien, J.P.1
  • 32
    • 84864363185 scopus 로고    scopus 로고
    • Structural basis for germline gene usage of a potent class of antibodies targeting the CD4-binding site of HIV-1 gp120
    • West AP, Jr., Diskin R, Nussenzweig MC, Bjorkman PJ (2012) Structural basis for germline gene usage of a potent class of antibodies targeting the CD4-binding site of HIV-1 gp120. Proc Natl Acad Sci USA 109(30):E2083-E2090.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.30
    • West Jr., A.P.1    Diskin, R.2    Nussenzweig, M.C.3    Bjorkman, P.J.4
  • 33
    • 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. (2013) Somatic mutations of the immunoglobulin framework are generally required for broad and potent HIV-1 neutralization. Cell 153(1):126-138.
    • (2013) Cell , vol.153 , Issue.1 , pp. 126-138
    • Klein, F.1
  • 34
    • 0031969423 scopus 로고    scopus 로고
    • Neutralization of human immunodeficiency virus type 1 by antibody to gp120 is determined primarily by occupancy of sites on the virion irrespective of epitope specificity
    • Parren PW, et al. (1998) Neutralization of human immunodeficiency virus type 1 by antibody to gp120 is determined primarily by occupancy of sites on the virion irrespective of epitope specificity. J Virol 72(5):3512-3519.
    • (1998) J Virol , vol.72 , Issue.5 , pp. 3512-3519
    • Parren, P.W.1
  • 35
    • 0037069682 scopus 로고    scopus 로고
    • HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites
    • Kwong PD, et al. (2002) HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites. Nature 420(6916):678-682.
    • (2002) Nature , vol.420 , Issue.6916 , pp. 678-682
    • Kwong, P.D.1
  • 36
    • 70350320690 scopus 로고    scopus 로고
    • Mechanism of human immunodeficiency virus type 1 resistance to monoclonal antibody B12 that effectively targets the site of CD4 attachment
    • Wu X, et al. (2009) Mechanism of human immunodeficiency virus type 1 resistance to monoclonal antibody B12 that effectively targets the site of CD4 attachment. J Virol 83(21):10892-10907.
    • (2009) J Virol , vol.83 , Issue.21 , pp. 10892-10907
    • Wu, X.1
  • 37
    • 84867630116 scopus 로고    scopus 로고
    • A blueprint for HIV vaccine discovery
    • Burton DR, et al. (2012) A Blueprint for HIV Vaccine Discovery. Cell Host Microbe 12(4):396-407.
    • (2012) Cell Host Microbe , vol.12 , Issue.4 , pp. 396-407
    • Burton, D.R.1
  • 38
    • 84879302728 scopus 로고    scopus 로고
    • HIV-1 neutralizing antibodies: Understanding nature's pathways
    • Mascola JR, Haynes BF (2013) HIV-1 neutralizing antibodies: Understanding nature's pathways. Immunol Rev 254(1):225-244.
    • (2013) Immunol Rev , vol.254 , Issue.1 , pp. 225-244
    • Mascola, J.R.1    Haynes, B.F.2
  • 39
    • 38349081511 scopus 로고    scopus 로고
    • The challenges of eliciting neutralizing antibodies to HIV-1 and to influenza virus
    • Karlsson Hedestam GB, et al. (2008) The challenges of eliciting neutralizing antibodies to HIV-1 and to influenza virus. Nat Rev Microbiol 6(2):143-155.
    • (2008) Nat Rev Microbiol , vol.6 , Issue.2 , pp. 143-155
    • Karlsson Hedestam, G.B.1
  • 40
    • 23844492576 scopus 로고    scopus 로고
    • Auto-rickshaw: An automated crystal structure determination platform as an efficient tool for the validation of an X-ray diffraction experiment
    • Panjikar S, Parthasarathy V, Lamzin VS, Weiss MS, Tucker PA (2005) Auto-rickshaw: An automated crystal structure determination platform as an efficient tool for the validation of an X-ray diffraction experiment. Acta Crystallogr D Biol Crystallogr 61(Pt 4): 449-457.
    • (2005) Acta Crystallogr D Biol Crystallogr , vol.61 , Issue.PART 4 , pp. 449-457
    • Panjikar, S.1    Parthasarathy, V.2    Lamzin, V.S.3    Weiss, M.S.4    Tucker, P.A.5
  • 41
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: Building new software for automated crystallographic structure determination
    • Adams PD, et al. (2002) PHENIX: Building new software for automated crystallographic structure determination. Acta Crystallogr D Biol Crystallogr 58(Pt 11): 1948-1954.
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , Issue.PART 11 , pp. 1948-1954
    • Adams, P.D.1
  • 42
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60(Pt 12 Pt 1):2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PART 12 PART 1 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 43
    • 20544468931 scopus 로고    scopus 로고
    • Automated molecular microscopy: The new Leginon system
    • Suloway C, et al. (2005) Automated molecular microscopy: The new Leginon system. J Struct Biol 151(1):41-60.
    • (2005) J Struct Biol , vol.151 , Issue.1 , pp. 41-60
    • Suloway, C.1
  • 44
    • 63649113687 scopus 로고    scopus 로고
    • DoG Picker and TiltPicker: Software tools to facilitate particle selection in single particle electron microscopy
    • Voss NR, Yoshioka CK, Radermacher M, Potter CS, Carragher B (2009) DoG Picker and TiltPicker: Software tools to facilitate particle selection in single particle electron microscopy. J Struct Biol 166(2):205-213.
    • (2009) J Struct Biol , vol.166 , Issue.2 , pp. 205-213
    • Voss, N.R.1    Yoshioka, C.K.2    Radermacher, M.3    Potter, C.S.4    Carragher, B.5
  • 45
    • 60649103238 scopus 로고    scopus 로고
    • Appion: An integrated, database-driven pipeline to facilitate EM image processing
    • Lander GC, et al. (2009) Appion: An integrated, database-driven pipeline to facilitate EM image processing. J Struct Biol 166(1):95-102.
    • (2009) J Struct Biol , vol.166 , Issue.1 , pp. 95-102
    • Lander, G.C.1
  • 46
    • 77953710827 scopus 로고    scopus 로고
    • A clustering approach to multireference alignment of singleparticle projections in electron microscopy
    • Sorzano CO, et al. (2010) A clustering approach to multireference alignment of singleparticle projections in electron microscopy. J Struct Biol 171(2):197-206.
    • (2010) J Struct Biol , vol.171 , Issue.2 , pp. 197-206
    • Sorzano, C.O.1
  • 47
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • Tang G, et al. (2007) EMAN2: An extensible image processing suite for electron microscopy. J Struct Biol 157(1):38-46.
    • (2007) J Struct Biol , vol.157 , Issue.1 , pp. 38-46
    • Tang, G.1
  • 48
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke SJ, Baldwin PR, Chiu W (1999) EMAN: Semiautomated software for high-resolution single-particle reconstructions. J Struct Biol 128(1):82-97.
    • (1999) J Struct Biol , vol.128 , Issue.1 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 49
    • 0036280741 scopus 로고    scopus 로고
    • Molecular dynamics applied to X-ray structure refinement
    • Brunger AT, Adams PD (2002) Molecular dynamics applied to X-ray structure refinement. Accounts of Chemical Research 35(6):404-412.
    • (2002) Accounts of Chemical Research , vol.35 , Issue.6 , pp. 404-412
    • Brunger, A.T.1    Adams, P.D.2
  • 50
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen VB, et al. (2010) MolProbity: All-atom structure validation for macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 66(Pt 1):12-21.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.PART 1 , pp. 12-21
    • Chen, V.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.