메뉴 건너뛰기




Volumn 30, Issue 5, 2012, Pages 922-930

An engineered mutant of HIV-1 gp120 formulated with adjuvant Quil A promotes elicitation of antibody responses overlapping the CD4-binding site

Author keywords

B12; Hyperglycosylation; Immunofocusing; Protein engineering

Indexed keywords

CD4 ANTIGEN; EPITOPE; GLYCOPROTEIN GP 120; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY B12; MONOCLONAL ANTIBODY B13; MONOCLONAL ANTIBODY VRCO3; NEUTRALIZING ANTIBODY; PHOSPHORYL LIPID A; QUIL A; UNCLASSIFIED DRUG;

EID: 84855433610     PISSN: 0264410X     EISSN: 18732518     Source Type: Journal    
DOI: 10.1016/j.vaccine.2011.11.089     Document Type: Article
Times cited : (25)

References (82)
  • 1
    • 77952311370 scopus 로고    scopus 로고
    • The role of antibodies in HIV vaccines
    • Mascola J.R., Montefiori D.C. The role of antibodies in HIV vaccines. Annu Rev Immunol 2010, 28:413-444.
    • (2010) Annu Rev Immunol , vol.28 , pp. 413-444
    • Mascola, J.R.1    Montefiori, D.C.2
  • 2
    • 77958490167 scopus 로고    scopus 로고
    • Induction of immunity to human immunodeficiency virus Type-1 by vaccination
    • McElrath M.J., Haynes B.F. Induction of immunity to human immunodeficiency virus Type-1 by vaccination. Immunity 2010, 33:542-554.
    • (2010) Immunity , vol.33 , pp. 542-554
    • McElrath, M.J.1    Haynes, B.F.2
  • 3
    • 69149083668 scopus 로고    scopus 로고
    • Neutralizing antibodies generated during natural HIV-1 infection: good news for an HIV-1 vaccine
    • Stamatatos L., Morris L., Burton D.R., Mascola J.R. Neutralizing antibodies generated during natural HIV-1 infection: good news for an HIV-1 vaccine. Nat Med 2009, 15:866-870.
    • (2009) Nat Med , vol.15 , pp. 866-870
    • Stamatatos, L.1    Morris, L.2    Burton, D.R.3    Mascola, J.R.4
  • 4
    • 79957726572 scopus 로고    scopus 로고
    • Role of immune mechanisms in induction of HIV-1 broadly neutralizing antibodies
    • Verkoczy L., Kelsoe G., Moody M.A., Haynes B.F. Role of immune mechanisms in induction of HIV-1 broadly neutralizing antibodies. Curr Opin Immunol 2011, 23:383-390.
    • (2011) Curr Opin Immunol , vol.23 , pp. 383-390
    • Verkoczy, L.1    Kelsoe, G.2    Moody, M.A.3    Haynes, B.F.4
  • 5
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens
    • Wyatt R., Sodroski J. The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens. Science 1998, 280:1884-1888.
    • (1998) Science , vol.280 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2
  • 6
    • 56449131391 scopus 로고    scopus 로고
    • Profiling the specificity of neutralizing antibodies in a large panel of plasmas from patients chronically infected with human immunodeficiency virus type 1 subtypes B and C
    • Binley J.M., Lybarger E.A., Crooks E.T., Seaman M.S., Gray E., Davis K.L., et al. Profiling the specificity of neutralizing antibodies in a large panel of plasmas from patients chronically infected with human immunodeficiency virus type 1 subtypes B and C. J Virol 2008, 82:11651-11668.
    • (2008) J Virol , vol.82 , pp. 11651-11668
    • Binley, J.M.1    Lybarger, E.A.2    Crooks, E.T.3    Seaman, M.S.4    Gray, E.5    Davis, K.L.6
  • 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., Langedijk J.P.M., Hinz A., Seaman M.S., Vanzetta F., Fernandez-Rodriguez B.M., et al. Analysis of memory B cell responses and isolation of novel monoclonal antibodies with neutralizing breadth from HIV-1-infected individuals. PLoS One 2010, 5:e8805.
    • (2010) PLoS One , vol.5
    • Corti, D.1    Langedijk, J.P.M.2    Hinz, A.3    Seaman, M.S.4    Vanzetta, F.5    Fernandez-Rodriguez, B.M.6
  • 8
    • 34948854718 scopus 로고    scopus 로고
    • Broad HIV-1 neutralization mediated by CD4-binding site antibodies
    • Li Y., Migueles S.A., Welcher B., Svehla K., Phogat A., Louder M.K., et al. Broad HIV-1 neutralization mediated by CD4-binding site antibodies. Nat Med 2007, 13:1032-1034.
    • (2007) Nat Med , vol.13 , pp. 1032-1034
    • Li, Y.1    Migueles, S.A.2    Welcher, B.3    Svehla, K.4    Phogat, A.5    Louder, M.K.6
  • 9
    • 58149517700 scopus 로고    scopus 로고
    • Analysis of neutralization specificities in polyclonal sera derived from human immunodeficiency virus type 1-infected individuals
    • Li Y., Svehla K., Louder M.K., Wycuff D., Phogat S., Tang M., et al. Analysis of neutralization specificities in polyclonal sera derived from human immunodeficiency virus type 1-infected individuals. J Virol 2009, 83:1045-1059.
    • (2009) J Virol , vol.83 , pp. 1045-1059
    • Li, Y.1    Svehla, K.2    Louder, M.K.3    Wycuff, D.4    Phogat, S.5    Tang, M.6
  • 10
    • 58149487645 scopus 로고    scopus 로고
    • Factors associated with the development of cross-reactive neutralizing antibodies during human immunodeficiency virus type 1 infection
    • Sather D.N., Armann J., Ching L.K., Mavrantoni A., Sellhorn G., Caldwell Z., et al. Factors associated with the development of cross-reactive neutralizing antibodies during human immunodeficiency virus type 1 infection. J Virol 2009, 83:757-769.
    • (2009) J Virol , vol.83 , pp. 757-769
    • Sather, D.N.1    Armann, J.2    Ching, L.K.3    Mavrantoni, A.4    Sellhorn, G.5    Caldwell, Z.6
  • 11
    • 77952516203 scopus 로고    scopus 로고
    • Epitope specificities of broadly neutralizing plasmas from HIV-1 infected subjects
    • Sather D.N., Stamatatos L. Epitope specificities of broadly neutralizing plasmas from HIV-1 infected subjects. Vaccine 2010, 28:B8-B12.
    • (2010) Vaccine , vol.28
    • Sather, D.N.1    Stamatatos, L.2
  • 12
    • 77958115264 scopus 로고    scopus 로고
    • A limited number of antibody specificities mediate broad and potent serum neutralization in selected HIV-1 infected individuals
    • Walker L.M., Simek M.D., Priddy F., Gach J.S., Wagner D., Zwick M.B., et al. A limited number of antibody specificities mediate broad and potent serum neutralization in selected HIV-1 infected individuals. PLoS Pathog 2010, 6:e1001028.
    • (2010) PLoS Pathog , vol.6
    • Walker, L.M.1    Simek, M.D.2    Priddy, F.3    Gach, J.S.4    Wagner, D.5    Zwick, M.B.6
  • 13
    • 34249950588 scopus 로고    scopus 로고
    • Dissecting the neutralizing antibody specificities of broadly neutralizing sera from human immunodeficiency virus type 1-infected donors
    • Dhillon A.K., Donners H., Pantophlet R., Johnson W.E., Decker J.M., Shaw G.M., et al. Dissecting the neutralizing antibody specificities of broadly neutralizing sera from human immunodeficiency virus type 1-infected donors. J Virol 2007, 81:6548-6562.
    • (2007) J Virol , vol.81 , pp. 6548-6562
    • Dhillon, A.K.1    Donners, H.2    Pantophlet, R.3    Johnson, W.E.4    Decker, J.M.5    Shaw, G.M.6
  • 14
    • 80055104586 scopus 로고    scopus 로고
    • Polyclonal B cell responses to conserved neutralization epitopes in a subset of HIV-1- infected individuals
    • Tomaras G.D., Binley J.M., Gray E.S., Crooks E.T., Osawa K., Moore P.L., et al. Polyclonal B cell responses to conserved neutralization epitopes in a subset of HIV-1- infected individuals. J Virol 2011, 85:11502-11519.
    • (2011) J Virol , vol.85 , pp. 11502-11519
    • Tomaras, G.D.1    Binley, J.M.2    Gray, E.S.3    Crooks, E.T.4    Osawa, K.5    Moore, P.L.6
  • 15
    • 80052925616 scopus 로고    scopus 로고
    • Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding
    • Scheid J.F., Mouquet H., Ueberheide B., Diskin R., Klein F., Olivera T.Y., et al. Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding. Science 2011, 16:1633-1637.
    • (2011) Science , vol.16 , pp. 1633-1637
    • Scheid, J.F.1    Mouquet, H.2    Ueberheide, B.3    Diskin, R.4    Klein, F.5    Olivera, T.Y.6
  • 16
    • 80053132436 scopus 로고    scopus 로고
    • Broad neutralization coverage of HIV by multiple highly potent antibodies
    • Walker L.M., Huber M., Doores K.J., Falkowska E., Pejchal R., Julien J.-P., et al. Broad neutralization coverage of HIV by multiple highly potent antibodies. Nature 2011, 477:466-470.
    • (2011) Nature , vol.477 , pp. 466-470
    • Walker, L.M.1    Huber, M.2    Doores, K.J.3    Falkowska, E.4    Pejchal, R.5    Julien, J.-P.6
  • 17
    • 80052942203 scopus 로고    scopus 로고
    • Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing
    • Wu X., Zhou T., Zhu J., Zhang B., Georgiev I., Wang C., et al. Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing. Science 2011, 333:1593-1602.
    • (2011) Science , vol.333 , pp. 1593-1602
    • Wu, X.1    Zhou, T.2    Zhu, J.3    Zhang, B.4    Georgiev, I.5    Wang, C.6
  • 18
    • 69249208675 scopus 로고    scopus 로고
    • Antibody specificities associated with neutralization breadth in plasma from human immunodeficiency virus type 1 subtype C-infected blood donors
    • Gray E.S., Taylor N., Wycuff D., Moore P.L., Tomaras G.D., Wibmer C.K., et al. Antibody specificities associated with neutralization breadth in plasma from human immunodeficiency virus type 1 subtype C-infected blood donors. J Virol 2009, 83:8925-8937.
    • (2009) J Virol , vol.83 , pp. 8925-8937
    • Gray, E.S.1    Taylor, N.2    Wycuff, D.3    Moore, P.L.4    Tomaras, G.D.5    Wibmer, C.K.6
  • 19
    • 71049141219 scopus 로고    scopus 로고
    • Epitopes for broad and potent neutralizing antibody responses during chronic infection with human immunodeficiency virus type 1
    • Nandi A., Lavine C.L., Wang P., Lipchina I., Goepfert P.A., Shaw G.M., et al. Epitopes for broad and potent neutralizing antibody responses during chronic infection with human immunodeficiency virus type 1. Virology 2010, 396:339-348.
    • (2010) Virology , vol.396 , pp. 339-348
    • Nandi, A.1    Lavine, C.L.2    Wang, P.3    Lipchina, I.4    Goepfert, P.A.5    Shaw, G.M.6
  • 20
    • 68349160853 scopus 로고    scopus 로고
    • Effective, low-titer antibody protection against low-dose repeated mucosal SHIV challenge in macaques
    • Hessell A.J., Poignard P., Hunter M., Hangartner L., Tehrani D.M., Bleeker W.K., et al. Effective, low-titer antibody protection against low-dose repeated mucosal SHIV challenge in macaques. Nat Med 2009, 15:951-954.
    • (2009) Nat Med , vol.15 , pp. 951-954
    • Hessell, A.J.1    Poignard, P.2    Hunter, M.3    Hangartner, L.4    Tehrani, D.M.5    Bleeker, W.K.6
  • 21
    • 34548496893 scopus 로고    scopus 로고
    • Fc receptor but not complement binding is important in antibody protection against HIV
    • Hessell A.J., Hangartner L., Hunter M., Havenith C.E., Beurskens F.J., Bakker J.M., et al. Fc receptor but not complement binding is important in antibody protection against HIV. Nature 2007, 449:101-104.
    • (2007) Nature , vol.449 , pp. 101-104
    • Hessell, A.J.1    Hangartner, L.2    Hunter, M.3    Havenith, C.E.4    Beurskens, F.J.5    Bakker, J.M.6
  • 22
    • 0034864776 scopus 로고    scopus 로고
    • Antibody protects macaques against vaginal challenge with a pathogenic R5 simian/human immunodeficiency virus at serum levels giving complete neutralization in vitro
    • Parren P.W., Marx P.A., Hessell A.J., Luckay A., Harouse J., Cheng-Mayer C., et al. Antibody protects macaques against vaginal challenge with a pathogenic R5 simian/human immunodeficiency virus at serum levels giving complete neutralization in vitro. J Virol 2001, 75:8340-8347.
    • (2001) J Virol , vol.75 , pp. 8340-8347
    • Parren, P.W.1    Marx, P.A.2    Hessell, A.J.3    Luckay, A.4    Harouse, J.5    Cheng-Mayer, C.6
  • 23
    • 79960585840 scopus 로고    scopus 로고
    • Limited or no protection by weakly or nonneutralizing antibodies against vaginal SHIV challenge of macaques compared with a strongly neutralizing antibody
    • Burton D.R., Hessell A.J., Keele B.F., Klasse P.J., Ketas T.A., Moldt B., et al. Limited or no protection by weakly or nonneutralizing antibodies against vaginal SHIV challenge of macaques compared with a strongly neutralizing antibody. Proc Natl Acad Sci U S A 2011, 108:11181-11186.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 11181-11186
    • Burton, D.R.1    Hessell, A.J.2    Keele, B.F.3    Klasse, P.J.4    Ketas, T.A.5    Moldt, B.6
  • 24
    • 77957820631 scopus 로고    scopus 로고
    • Passive neutralizing antibody controls SHIV viremia and enhances B cell responses in infant macaques
    • Ng C.T., Jaworski J.P., Jayaraman P., Sutton W.F., Delio P., Kuller L., et al. Passive neutralizing antibody controls SHIV viremia and enhances B cell responses in infant macaques. Nat Med 2010, 16:1117-1119.
    • (2010) Nat Med , vol.16 , pp. 1117-1119
    • Ng, C.T.1    Jaworski, J.P.2    Jayaraman, P.3    Sutton, W.F.4    Delio, P.5    Kuller, L.6
  • 25
    • 77954920017 scopus 로고    scopus 로고
    • Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1
    • Wu X., Yang Z.-Y., Li Y., Hogerkorp C.-M., Schief W.R., Seaman M.S., et al. Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1. Science 2010, 329:856-861.
    • (2010) Science , vol.329 , pp. 856-861
    • Wu, X.1    Yang, Z.-Y.2    Li, Y.3    Hogerkorp, C.-M.4    Schief, W.R.5    Seaman, M.S.6
  • 26
    • 77954943648 scopus 로고    scopus 로고
    • Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01
    • Zhou T., Georgiev I., Wu X., Yang Z.-Y., Dai K., Finzi A., et al. Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01. Science 2010, 29:811-817.
    • (2010) Science , vol.29 , pp. 811-817
    • Zhou, T.1    Georgiev, I.2    Wu, X.3    Yang, Z.-Y.4    Dai, K.5    Finzi, A.6
  • 27
    • 70450182950 scopus 로고    scopus 로고
    • Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120
    • Chen L., Do Kwon Y., Zhou T., Wu X., O'Dell S., Cavacini L., et al. Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120. Science 2009, 326:1123-1127.
    • (2009) Science , vol.326 , pp. 1123-1127
    • Chen, L.1    Do Kwon, Y.2    Zhou, T.3    Wu, X.4    O'Dell, S.5    Cavacini, L.6
  • 28
    • 0037213247 scopus 로고    scopus 로고
    • Fine mapping of the interaction of neutralizing and nonneutralizing monoclonal antibodies with the CD4 binding site of human immunodeficiency virus type 1 gp120
    • Pantophlet R., Ollmann Saphire E., Poignard P., Parren P.W., Wilson I.A., Burton D.R. Fine mapping of the interaction of neutralizing and nonneutralizing monoclonal antibodies with the CD4 binding site of human immunodeficiency virus type 1 gp120. J Virol 2003, 77:642-658.
    • (2003) J Virol , vol.77 , pp. 642-658
    • Pantophlet, R.1    Ollmann Saphire, E.2    Poignard, P.3    Parren, P.W.4    Wilson, I.A.5    Burton, D.R.6
  • 29
    • 0038032955 scopus 로고    scopus 로고
    • Molecular features of the broadly neutralizing immunoglobulin G1 b12 required for recognition of human immunodeficiency virus type 1 gp120
    • Zwick M.B., Parren P.W., Saphire E.O., Church S., Wang M., Scott J.K., et al. Molecular features of the broadly neutralizing immunoglobulin G1 b12 required for recognition of human immunodeficiency virus type 1 gp120. J Virol 2003, 77:5863-5876.
    • (2003) J Virol , vol.77 , pp. 5863-5876
    • Zwick, M.B.1    Parren, P.W.2    Saphire, E.O.3    Church, S.4    Wang, M.5    Scott, J.K.6
  • 30
    • 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., Zhou T., O'Dell S., Wyatt R.T., Kwong P.D., Mascola J.R. Mechanism of human immunodeficiency virus type 1 resistance to monoclonal antibody b12 that effectively targets the site of CD4 attachment. J Virol 2009, 83:10892-10907.
    • (2009) J Virol , vol.83 , pp. 10892-10907
    • Wu, X.1    Zhou, T.2    O'Dell, S.3    Wyatt, R.T.4    Kwong, P.D.5    Mascola, J.R.6
  • 31
    • 66149132686 scopus 로고    scopus 로고
    • Examination of the contributions of size and avidity to the neutralization mechanisms of the anti-HIV antibodies b12 and 4E10
    • Klein J.S., Gnanapragasam P.N.P., Galimidi R.P., Foglesong C.P., West A.P., Bjorkman P.J. Examination of the contributions of size and avidity to the neutralization mechanisms of the anti-HIV antibodies b12 and 4E10. Proc Natl Acad Sci U S A 2009, 106:7385-7390.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 7385-7390
    • Klein, J.S.1    Gnanapragasam, P.N.P.2    Galimidi, R.P.3    Foglesong, C.P.4    West, A.P.5    Bjorkman, P.J.6
  • 32
    • 77953543379 scopus 로고    scopus 로고
    • Rational antibody-based HIV-1 vaccine design: current approaches and future directions
    • Walker L.M., Burton D.R. Rational antibody-based HIV-1 vaccine design: current approaches and future directions. Curr Opin Immunol 2010, 22:358-366.
    • (2010) Curr Opin Immunol , vol.22 , pp. 358-366
    • Walker, L.M.1    Burton, D.R.2
  • 33
    • 33846172297 scopus 로고    scopus 로고
    • Rational modifications of HIV-1 envelope glycoproteins for immunogen design
    • Phogat S., Wyatt R. Rational modifications of HIV-1 envelope glycoproteins for immunogen design. Curr Pharm Des 2007, 13:213-227.
    • (2007) Curr Pharm Des , vol.13 , pp. 213-227
    • Phogat, S.1    Wyatt, R.2
  • 34
    • 70349249520 scopus 로고    scopus 로고
    • Selective expansion of HIV-1 envelope glycoprotein-specific B cell subsets recognizing distinct structural elements following immunization
    • Dosenovic P., Chakrabarti B., Soldemo M., Douagi I., Forsell M.N., Li Y., et al. Selective expansion of HIV-1 envelope glycoprotein-specific B cell subsets recognizing distinct structural elements following immunization. J Immunol 2009, 183:3373-3382.
    • (2009) J Immunol , vol.183 , pp. 3373-3382
    • Dosenovic, P.1    Chakrabarti, B.2    Soldemo, M.3    Douagi, I.4    Forsell, M.N.5    Li, Y.6
  • 35
    • 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., Forsell M.N.E., Sundling C., O'Dell S., Feng Y., Dosenovic P., et al. Influence of novel CD4 binding-defective HIV-1 envelope glycoprotein immunogens on neutralizing antibody and T-cell responses in nonhuman primates. J Virol 2010, 84:1683-1695.
    • (2010) J Virol , vol.84 , pp. 1683-1695
    • Douagi, I.1    Forsell, M.N.E.2    Sundling, C.3    O'Dell, S.4    Feng, Y.5    Dosenovic, P.6
  • 36
    • 77956261658 scopus 로고    scopus 로고
    • Soluble HIV-1 Env trimers in adjuvant elicit potent and diverse functional B cell responses in primates
    • Sundling C., Forsell M.N.E., O'Dell S., Feng Y., Chakrabarti B., Rao S.S., et al. Soluble HIV-1 Env trimers in adjuvant elicit potent and diverse functional B cell responses in primates. J Exp Med 2010, 207:2003-2017.
    • (2010) J Exp Med , vol.207 , pp. 2003-2017
    • Sundling, C.1    Forsell, M.N.E.2    O'Dell, S.3    Feng, Y.4    Chakrabarti, B.5    Rao, S.S.6
  • 37
    • 65349196678 scopus 로고    scopus 로고
    • Enhanced exposure of the CD4-binding site to neutralizing antibodies by structural design of a membrane-anchored human immunodeficiency virus type 1 gp120 domain
    • Wu L., Zhou T., Yang Z-y Svehla K., O'Dell S., Louder M.K., et al. Enhanced exposure of the CD4-binding site to neutralizing antibodies by structural design of a membrane-anchored human immunodeficiency virus type 1 gp120 domain. J Virol 2009, 83:5077-5086.
    • (2009) J Virol , vol.83 , pp. 5077-5086
    • Wu, L.1    Zhou, T.2    Yang Z-y Svehla, K.3    O'Dell, S.4    Louder, M.K.5
  • 38
    • 0038414622 scopus 로고    scopus 로고
    • Hyperglycosylated mutants of human immunodeficiency virus (HIV) type 1 monomeric gp120 as novel antigens for HIV vaccine design
    • Pantophlet R., Wilson I.A., Burton D.R. Hyperglycosylated mutants of human immunodeficiency virus (HIV) type 1 monomeric gp120 as novel antigens for HIV vaccine design. J Virol 2003, 77:5889-5901.
    • (2003) J Virol , vol.77 , pp. 5889-5901
    • Pantophlet, R.1    Wilson, I.A.2    Burton, D.R.3
  • 39
    • 77956247505 scopus 로고    scopus 로고
    • Design of a non-glycosylated outer domain-derived HIV-1 gp120 immunogen that binds to cd4 and induces neutralizing antibodies
    • Bhattacharyya S., Rajan R.E., Swarupa Y., Rathore U., Verma A., Udaykumar R., et al. Design of a non-glycosylated outer domain-derived HIV-1 gp120 immunogen that binds to cd4 and induces neutralizing antibodies. J Biol Chem 2010, 285:27100-27110.
    • (2010) J Biol Chem , vol.285 , pp. 27100-27110
    • Bhattacharyya, S.1    Rajan, R.E.2    Swarupa, Y.3    Rathore, U.4    Verma, A.5    Udaykumar, R.6
  • 40
    • 12444337649 scopus 로고    scopus 로고
    • Improved design of an antigen with enhanced specificity for the broadly HIV-neutralizing antibody b12
    • Pantophlet R., Wilson I.A., Burton D.R. Improved design of an antigen with enhanced specificity for the broadly HIV-neutralizing antibody b12. Protein Eng Des Sel 2004, 17:749-758.
    • (2004) Protein Eng Des Sel , vol.17 , pp. 749-758
    • Pantophlet, R.1    Wilson, I.A.2    Burton, D.R.3
  • 41
    • 77956237048 scopus 로고    scopus 로고
    • Human anti-HIV-neutralizing antibodies frequently target a conserved epitope essential for viral fitness
    • Pietzsch J., Scheid J.F., Mouquet H., Klein F., Seaman M.S., Jankovic M., et al. Human anti-HIV-neutralizing antibodies frequently target a conserved epitope essential for viral fitness. J Exp Med 2010, 207:1995-2002.
    • (2010) J Exp Med , vol.207 , pp. 1995-2002
    • Pietzsch, J.1    Scheid, J.F.2    Mouquet, H.3    Klein, F.4    Seaman, M.S.5    Jankovic, M.6
  • 43
    • 0031404534 scopus 로고    scopus 로고
    • Can epitope-focused vaccines select advantageous immune responses
    • Delves P.J., Lund T., Roitt I.M. Can epitope-focused vaccines select advantageous immune responses. Mol Med Today 1997, 3:55-60.
    • (1997) Mol Med Today , vol.3 , pp. 55-60
    • Delves, P.J.1    Lund, T.2    Roitt, I.M.3
  • 44
    • 0031180974 scopus 로고    scopus 로고
    • Refocusing neutralizing antibody response by targeted dampening of an immunodominant epitope
    • Garrity R.R., Rimmelzwaan G., Minassian A., Tsai W.P., Lin G., de Jong J.J., et al. Refocusing neutralizing antibody response by targeted dampening of an immunodominant epitope. J Immunol 1997, 159:279-289.
    • (1997) J Immunol , vol.159 , pp. 279-289
    • Garrity, R.R.1    Rimmelzwaan, G.2    Minassian, A.3    Tsai, W.P.4    Lin, G.5    de Jong, J.J.6
  • 46
    • 78650425411 scopus 로고    scopus 로고
    • How can vaccines against influenza and other viral diseases be made more effective?
    • Nara P.L., Tobin G.J., Chaudhuri A.R., Trujillo J.D., Lin G., Cho M.W., et al. How can vaccines against influenza and other viral diseases be made more effective?. PLoS Biol 2010, 8:e1000571.
    • (2010) PLoS Biol , vol.8
    • Nara, P.L.1    Tobin, G.J.2    Chaudhuri, A.R.3    Trujillo, J.D.4    Lin, G.5    Cho, M.W.6
  • 47
    • 79951991406 scopus 로고    scopus 로고
    • Novel adjuvants and delivery systems for enhancing immune responses induced by immunogens
    • Dey A.K., Srivastava I.K. Novel adjuvants and delivery systems for enhancing immune responses induced by immunogens. Expert Rev Vaccines 2011, 10:227-251.
    • (2011) Expert Rev Vaccines , vol.10 , pp. 227-251
    • Dey, A.K.1    Srivastava, I.K.2
  • 50
    • 80052410152 scopus 로고    scopus 로고
    • The development of recombinant subunit envelope-based vaccines to protect against dengue virus induced disease
    • Coller B.-A.G., Clements D.E., Bett A.J., Sagar S.L., Ter Meulen J.H. The development of recombinant subunit envelope-based vaccines to protect against dengue virus induced disease. Vaccine 2011, 29:7267-7275.
    • (2011) Vaccine , vol.29 , pp. 7267-7275
    • Coller, B.-A.G.1    Clements, D.E.2    Bett, A.J.3    Sagar, S.L.4    Ter Meulen, J.H.5
  • 51
    • 42649083976 scopus 로고    scopus 로고
    • Addition of CpG ODN to recombinant Pseudomonas aeruginosa ExoProtein A conjugates of AMA1 and Pfs25 greatly increases the number of responders
    • Qian F., Rausch K.M., Muratova O., Zhou H., Song G., Diouf A., et al. Addition of CpG ODN to recombinant Pseudomonas aeruginosa ExoProtein A conjugates of AMA1 and Pfs25 greatly increases the number of responders. Vaccine 2008, 26:2521-2527.
    • (2008) Vaccine , vol.26 , pp. 2521-2527
    • Qian, F.1    Rausch, K.M.2    Muratova, O.3    Zhou, H.4    Song, G.5    Diouf, A.6
  • 52
    • 34250821634 scopus 로고    scopus 로고
    • Enhanced antibody production in mice to the malaria antigen AMA1 by CPG 7909 requires physical association of CpG and antigen
    • Mullen G.E., Aebig J.A., Dobrescu G., Rausch K., Lambert L., Long C.A., et al. Enhanced antibody production in mice to the malaria antigen AMA1 by CPG 7909 requires physical association of CpG and antigen. Vaccine 2007, 25:5343-5347.
    • (2007) Vaccine , vol.25 , pp. 5343-5347
    • Mullen, G.E.1    Aebig, J.A.2    Dobrescu, G.3    Rausch, K.4    Lambert, L.5    Long, C.A.6
  • 54
    • 37449022593 scopus 로고    scopus 로고
    • Structure of antibody F425-B4e8 in complex with a V3 peptide reveals a new binding mode for HIV-1 neutralization
    • Bell C.H., Pantophlet R., Schiefner A., Cavacini L.A., Stanfield R.L., Burton D.R., et al. Structure of antibody F425-B4e8 in complex with a V3 peptide reveals a new binding mode for HIV-1 neutralization. J Mol Biol 2008, 375:969-978.
    • (2008) J Mol Biol , vol.375 , pp. 969-978
    • Bell, C.H.1    Pantophlet, R.2    Schiefner, A.3    Cavacini, L.A.4    Stanfield, R.L.5    Burton, D.R.6
  • 55
    • 0035202616 scopus 로고    scopus 로고
    • Neutralization synergy of human immunodeficiency virus type 1 primary isolates by cocktails of broadly neutralizing antibodies
    • Zwick M.B., Wang M., Poignard P., Stiegler G., Katinger H., Burton D.R., et al. Neutralization synergy of human immunodeficiency virus type 1 primary isolates by cocktails of broadly neutralizing antibodies. J Virol 2001, 75:12198-12208.
    • (2001) J Virol , vol.75 , pp. 12198-12208
    • Zwick, M.B.1    Wang, M.2    Poignard, P.3    Stiegler, G.4    Katinger, H.5    Burton, D.R.6
  • 56
    • 33847101745 scopus 로고    scopus 로고
    • Structural definition of a conserved neutralization epitope on HIV-1 gp120
    • Zhou T., Xu L., Dey B., Hessell A.J., Van Ryk D., Xiang S.H., et al. Structural definition of a conserved neutralization epitope on HIV-1 gp120. Nature 2007, 445:732-737.
    • (2007) Nature , vol.445 , pp. 732-737
    • Zhou, T.1    Xu, L.2    Dey, B.3    Hessell, A.J.4    Van Ryk, D.5    Xiang, S.H.6
  • 57
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong P.D., Wyatt R., Robinson J., Sweet R.W., Sodroski J., Hendrickson W.A. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 1998, 393:648-659.
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 61
    • 61349084783 scopus 로고    scopus 로고
    • Advances in saponin-based adjuvants
    • Sun H.X., Xie Y., Ye Y.P. Advances in saponin-based adjuvants. Vaccine 2009, 27:1787-1796.
    • (2009) Vaccine , vol.27 , pp. 1787-1796
    • Sun, H.X.1    Xie, Y.2    Ye, Y.P.3
  • 62
    • 0030043169 scopus 로고    scopus 로고
    • Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein
    • Moore J.P., Sodroski J. Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein. J Virol 1996, 70:1863-1872.
    • (1996) J Virol , vol.70 , pp. 1863-1872
    • Moore, J.P.1    Sodroski, J.2
  • 63
    • 84855462484 scopus 로고    scopus 로고
    • Abstract OA04.04 - characterization of CD4-binding site directed monoclonal antibodies isolated from HIV-1 gp140 Env immunized rhesus macaques. Abstracts from AIDS Vaccine 2011 Bangkok, Thailand, 12-15 September, 2011
    • Sundling C., Li Y., Huynh N., Wilson R., O'Dell S., Mascola J., et al. Abstract OA04.04 - characterization of CD4-binding site directed monoclonal antibodies isolated from HIV-1 gp140 Env immunized rhesus macaques. Abstracts from AIDS Vaccine 2011 Bangkok, Thailand, 12-15 September, 2011. AIDS Res Hum Retroviruses 2011, 27:A-1-A-148.
    • (2011) AIDS Res Hum Retroviruses , vol.27
    • Sundling, C.1    Li, Y.2    Huynh, N.3    Wilson, R.4    O'Dell, S.5    Mascola, J.6
  • 64
    • 26044480339 scopus 로고    scopus 로고
    • Similarity and divergence in the development and expression of the mouse and human antibody repertoires
    • Schroeder J.H.W. Similarity and divergence in the development and expression of the mouse and human antibody repertoires. Dev Comp Immunol 2006, 30:119-135.
    • (2006) Dev Comp Immunol , vol.30 , pp. 119-135
    • Schroeder, J.H.W.1
  • 65
    • 0037227422 scopus 로고    scopus 로고
    • Analysis of the antigen combining site: correlations between length and sequence composition of the hypervariable loops and the nature of the antigen
    • Collis A.V.J., Brouwer A.P., Martin A.C.R. Analysis of the antigen combining site: correlations between length and sequence composition of the hypervariable loops and the nature of the antigen. J Mol Biol 2003, 325:337-354.
    • (2003) J Mol Biol , vol.325 , pp. 337-354
    • Collis, A.V.J.1    Brouwer, A.P.2    Martin, A.C.R.3
  • 66
    • 0242551578 scopus 로고    scopus 로고
    • Expressed murine and human CDR-H3 intervals of equal length exhibit distinct repertoires that differ in their amino acid composition and predicted range of structures
    • Zemlin M., Klinger M., Link J., Zemlin C., Bauer K., Engler J.A., et al. Expressed murine and human CDR-H3 intervals of equal length exhibit distinct repertoires that differ in their amino acid composition and predicted range of structures. J Mol Biol 2003, 334:733-749.
    • (2003) J Mol Biol , vol.334 , pp. 733-749
    • Zemlin, M.1    Klinger, M.2    Link, J.3    Zemlin, C.4    Bauer, K.5    Engler, J.A.6
  • 67
    • 79953316880 scopus 로고    scopus 로고
    • Comparison of antibody repertoires produced by HIV-1 infection, other chronic and acute infections, and systemic autoimmune disease
    • Breden F., Lepik C., Longo N.S., Montero M., Lipsky P.E., Scott J.K. Comparison of antibody repertoires produced by HIV-1 infection, other chronic and acute infections, and systemic autoimmune disease. PLoS One 2011, 6:e16857.
    • (2011) PLoS One , vol.6
    • Breden, F.1    Lepik, C.2    Longo, N.S.3    Montero, M.4    Lipsky, P.E.5    Scott, J.K.6
  • 68
    • 0037225412 scopus 로고    scopus 로고
    • Rabbit immune repertoires as sources for therapeutic monoclonal antibodies: the impact of kappa allotype-correlated variation in cysteine content on antibody libraries selected by phage display
    • Popkov M., Mage R.G., Alexander C.B., Thundivalappil S., Barbas C.F., Rader C. Rabbit immune repertoires as sources for therapeutic monoclonal antibodies: the impact of kappa allotype-correlated variation in cysteine content on antibody libraries selected by phage display. J Mol Biol 2003, 325:325-335.
    • (2003) J Mol Biol , vol.325 , pp. 325-335
    • Popkov, M.1    Mage, R.G.2    Alexander, C.B.3    Thundivalappil, S.4    Barbas, C.F.5    Rader, C.6
  • 69
    • 26044450908 scopus 로고    scopus 로고
    • B cell and antibody repertoire development in rabbits: the requirement of gut-associated lymphoid tissues
    • Mage R.G., Lanning D., Knight K.L. B cell and antibody repertoire development in rabbits: the requirement of gut-associated lymphoid tissues. Dev Comp Immunol 2006, 30:137-153.
    • (2006) Dev Comp Immunol , vol.30 , pp. 137-153
    • Mage, R.G.1    Lanning, D.2    Knight, K.L.3
  • 70
    • 1842529304 scopus 로고    scopus 로고
    • Analysis of mutational lineage trees from sites of primary and secondary Ig gene diversification in rabbits and chickens
    • Mehr R., Edelman H., Sehgal D., Mage R. Analysis of mutational lineage trees from sites of primary and secondary Ig gene diversification in rabbits and chickens. J Immunol 2004, 172:4790-4796.
    • (2004) J Immunol , vol.172 , pp. 4790-4796
    • Mehr, R.1    Edelman, H.2    Sehgal, D.3    Mage, R.4
  • 71
    • 0033920322 scopus 로고    scopus 로고
    • Development of the antibody repertoire in rabbit: gut-associated lymphoid tissue, microbes, and selection
    • Dennis Lanning X.Z., Zhai S.-K., Katherine L.K. Development of the antibody repertoire in rabbit: gut-associated lymphoid tissue, microbes, and selection. Immunol Rev 2000, 175:214-228.
    • (2000) Immunol Rev , vol.175 , pp. 214-228
    • Dennis Lanning, X.Z.1    Zhai, S.-K.2    Katherine, L.K.3
  • 72
    • 80052314665 scopus 로고    scopus 로고
    • Putative rhesus macaque germline predecessors of human broadly HIV-neutralizing antibodies: Differences from the human counterparts and implications for HIV-1 vaccine development
    • Yuan T., Li J., Zhang Y., Wang Y., Streaker E., Dimitrov D.S., et al. Putative rhesus macaque germline predecessors of human broadly HIV-neutralizing antibodies: Differences from the human counterparts and implications for HIV-1 vaccine development. Vaccine 2011, 29:6903-6910.
    • (2011) Vaccine , vol.29 , pp. 6903-6910
    • Yuan, T.1    Li, J.2    Zhang, Y.3    Wang, Y.4    Streaker, E.5    Dimitrov, D.S.6
  • 73
    • 16844386973 scopus 로고    scopus 로고
    • Despite extensive similarity in germline DH and JH sequence, the adult Rhesus macaque CDR-H3 repertoire differs from human
    • Link J.M., Larson J.E., Schroeder H.W. Despite extensive similarity in germline DH and JH sequence, the adult Rhesus macaque CDR-H3 repertoire differs from human. Mol Immunol 2005, 42:943-955.
    • (2005) Mol Immunol , vol.42 , pp. 943-955
    • Link, J.M.1    Larson, J.E.2    Schroeder, H.W.3
  • 74
    • 31144451337 scopus 로고    scopus 로고
    • Characterization of antibody responses elicited by human immunodeficiency virus type 1 primary isolate trimeric and monomeric envelope glycoproteins in selected adjuvants
    • Li Y., Svehla K., Mathy N.L., Voss G., Mascola J.R., Wyatt R. Characterization of antibody responses elicited by human immunodeficiency virus type 1 primary isolate trimeric and monomeric envelope glycoproteins in selected adjuvants. J Virol 2006, 80:1414-1426.
    • (2006) J Virol , vol.80 , pp. 1414-1426
    • Li, Y.1    Svehla, K.2    Mathy, N.L.3    Voss, G.4    Mascola, J.R.5    Wyatt, R.6
  • 75
    • 77957271989 scopus 로고    scopus 로고
    • Expression-system-dependent modulation of HIV-1 envelope glycoprotein antigenicity and immunogenicity
    • Kong L., Sheppard N.C., Stewart-Jones G.B., Robson C.L., Chen H., Xu X., et al. Expression-system-dependent modulation of HIV-1 envelope glycoprotein antigenicity and immunogenicity. J Mol Biol 2010, 403:131-147.
    • (2010) J Mol Biol , vol.403 , pp. 131-147
    • Kong, L.1    Sheppard, N.C.2    Stewart-Jones, G.B.3    Robson, C.L.4    Chen, H.5    Xu, X.6
  • 76
    • 7544236606 scopus 로고    scopus 로고
    • Factors limiting the immunogenicity of HIV-1 gp120 envelope glycoproteins
    • Grundner C., Pancera M., Kang J.M., Koch M., Sodroski J., Wyatt R. Factors limiting the immunogenicity of HIV-1 gp120 envelope glycoproteins. Virology 2004, 330:233-248.
    • (2004) Virology , vol.330 , pp. 233-248
    • Grundner, C.1    Pancera, M.2    Kang, J.M.3    Koch, M.4    Sodroski, J.5    Wyatt, R.6
  • 77
    • 77954224920 scopus 로고    scopus 로고
    • Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition
    • Raska M., Takahashi K., Czernekova L., Zachova K., Hall S., Moldoveanu Z., et al. Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition. J Biol Chem 2010, 285:20860-20869.
    • (2010) J Biol Chem , vol.285 , pp. 20860-20869
    • Raska, M.1    Takahashi, K.2    Czernekova, L.3    Zachova, K.4    Hall, S.5    Moldoveanu, Z.6
  • 80
    • 79551556431 scopus 로고    scopus 로고
    • Heterologous epitope-scaffold prime-boosting immuno-focuses B cell responses to the HIV-1 gp41 2F5 neutralization determinant
    • Guenaga J., Dosenovic P., Ofek G., Baker D., Schief W.R., Kwong P.D., et al. Heterologous epitope-scaffold prime-boosting immuno-focuses B cell responses to the HIV-1 gp41 2F5 neutralization determinant. PLoS One 2011, 6:e16074.
    • (2011) PLoS One , vol.6
    • Guenaga, J.1    Dosenovic, P.2    Ofek, G.3    Baker, D.4    Schief, W.R.5    Kwong, P.D.6
  • 81
    • 19944423187 scopus 로고    scopus 로고
    • Evaluating neutralizing antibodies against HIV, SIV and SHIV in luciferase reporter gene assays
    • John Wiley & Sons, New York, J.E. Coligan, A.M. Kruisbeek, D.H. Margulies, E.M. Shevach, W. Strober, R. Coico (Eds.)
    • Montefiori D. Evaluating neutralizing antibodies against HIV, SIV and SHIV in luciferase reporter gene assays. Current protocol in immunology 2004, 12.1.1-12.1.5. John Wiley & Sons, New York. J.E. Coligan, A.M. Kruisbeek, D.H. Margulies, E.M. Shevach, W. Strober, R. Coico (Eds.).
    • (2004) Current protocol in immunology
    • Montefiori, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.