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Volumn 24, Issue 1, 2018, Pages 25-33

Immune Correlate-Guided HIV Vaccine Design

Author keywords

[No Author keywords available]

Indexed keywords

HUMAN IMMUNODEFICIENCY VIRUS ANTIGEN; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; NEUTRALIZING ANTIBODY; POLYCLONAL ANTIBODY; VIRUS ANTIBODY; VIRUS ENVELOPE PROTEIN;

EID: 85049346187     PISSN: 19313128     EISSN: 19346069     Source Type: Journal    
DOI: 10.1016/j.chom.2018.06.012     Document Type: Review
Times cited : (37)

References (117)
  • 3
    • 84925226149 scopus 로고    scopus 로고
    • Cell-associated HIV mucosal transmission: the neglected pathway
    • Anderson, D.J., Le Grand, R., Cell-associated HIV mucosal transmission: the neglected pathway. J. Infect. Dis. 210:Suppl 3 (2014), S606–S608.
    • (2014) J. Infect. Dis. , vol.210 , pp. S606-S608
    • Anderson, D.J.1    Le Grand, R.2
  • 12
    • 85010901238 scopus 로고    scopus 로고
    • Immunologic characteristics of HIV-infected individuals who make broadly neutralizing antibodies
    • Borrow, P., Moody, M.A., Immunologic characteristics of HIV-infected individuals who make broadly neutralizing antibodies. Immunol. Rev. 275 (2017), 62–78.
    • (2017) Immunol. Rev. , vol.275 , pp. 62-78
    • Borrow, P.1    Moody, M.A.2
  • 13
    • 84908077691 scopus 로고    scopus 로고
    • Broadly neutralizing anti-HIV-1 antibodies require Fc effector functions for in vivo activity
    • Bournazos, S., Klein, F., Pietzsch, J., Seaman, M.S., Nussenzweig, M.C., Ravetch, J.V., Broadly neutralizing anti-HIV-1 antibodies require Fc effector functions for in vivo activity. Cell 158 (2014), 1243–1253.
    • (2014) Cell , vol.158 , pp. 1243-1253
    • Bournazos, S.1    Klein, F.2    Pietzsch, J.3    Seaman, M.S.4    Nussenzweig, M.C.5    Ravetch, J.V.6
  • 14
    • 85010900171 scopus 로고    scopus 로고
    • Anti-retroviral antibody FcγR-mediated effector functions
    • Bournazos, S., Ravetch, J.V., Anti-retroviral antibody FcγR-mediated effector functions. Immunol. Rev. 275 (2017), 285–295.
    • (2017) Immunol. Rev. , vol.275 , pp. 285-295
    • Bournazos, S.1    Ravetch, J.V.2
  • 17
    • 84969835812 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies to HIV and their role in vaccine design
    • Burton, D.R., Hangartner, L., Broadly neutralizing antibodies to HIV and their role in vaccine design. Annu. Rev. Immunol. 34 (2016), 635–659.
    • (2016) Annu. Rev. Immunol. , vol.34 , pp. 635-659
    • Burton, D.R.1    Hangartner, L.2
  • 18
  • 19
    • 84929896699 scopus 로고    scopus 로고
    • Antibody responses to envelope glycoproteins in HIV-1 infection
    • Burton, D.R., Mascola, J.R., Antibody responses to envelope glycoproteins in HIV-1 infection. Nat. Immunol. 16 (2015), 571–576.
    • (2015) Nat. Immunol. , vol.16 , pp. 571-576
    • Burton, D.R.1    Mascola, J.R.2
  • 21
    • 84906100246 scopus 로고    scopus 로고
    • Vaccine focusing to cross-subtype HIV-1 gp120 variable loop epitopes
    • Cardozo, T., Wang, S., Jiang, X., Kong, X.P., Hioe, C., Krachmarov, C., Vaccine focusing to cross-subtype HIV-1 gp120 variable loop epitopes. Vaccine 32 (2014), 4916–4924.
    • (2014) Vaccine , vol.32 , pp. 4916-4924
    • Cardozo, T.1    Wang, S.2    Jiang, X.3    Kong, X.P.4    Hioe, C.5    Krachmarov, C.6
  • 27
    • 77958498224 scopus 로고    scopus 로고
    • Vaccine adjuvants: putting innate immunity to work
    • Coffman, R.L., Sher, A., Seder, R.A., Vaccine adjuvants: putting innate immunity to work. Immunity 33 (2010), 492–503.
    • (2010) Immunity , vol.33 , pp. 492-503
    • Coffman, R.L.1    Sher, A.2    Seder, R.A.3
  • 29
    • 58149136160 scopus 로고    scopus 로고
    • Post-step modifications for research on HIV vaccines
    • Corey, L., McElrath, M.J., Kublin, J.G., Post-step modifications for research on HIV vaccines. AIDS 23 (2009), 3–8.
    • (2009) AIDS , vol.23 , pp. 3-8
    • Corey, L.1    McElrath, M.J.2    Kublin, J.G.3
  • 30
    • 84923770324 scopus 로고    scopus 로고
    • A brief history of T cell help to B cells
    • Crotty, S., A brief history of T cell help to B cells. Nat. Rev. Immunol. 15 (2015), 185–189.
    • (2015) Nat. Rev. Immunol. , vol.15 , pp. 185-189
    • Crotty, S.1
  • 32
    • 55549114992 scopus 로고    scopus 로고
    • Structure-based antigen design: a strategy for next generation vaccines
    • Dormitzer, P.R., Ulmer, J.B., Rappuoli, R., Structure-based antigen design: a strategy for next generation vaccines. Trends Biotechnol. 26 (2008), 659–667.
    • (2008) Trends Biotechnol. , vol.26 , pp. 659-667
    • Dormitzer, P.R.1    Ulmer, J.B.2    Rappuoli, R.3
  • 40
    • 84989882721 scopus 로고    scopus 로고
    • Boosting of ALVAC-SIV vaccine-primed macaques with the CD4-SIVgp120 fusion protein elicits antibodies to V2 associated with a decreased risk of SIVmac251 acquisition
    • Gordon, S.N., Liyanage, N.P., Doster, M.N., Vaccari, M., Vargas-Inchaustegui, D.A., Pegu, P., Schifanella, L., Shen, X., Tomaras, G.D., Rao, M., et al. Boosting of ALVAC-SIV vaccine-primed macaques with the CD4-SIVgp120 fusion protein elicits antibodies to V2 associated with a decreased risk of SIVmac251 acquisition. J. Immunol. 197 (2016), 2726–2737.
    • (2016) J. Immunol. , vol.197 , pp. 2726-2737
    • Gordon, S.N.1    Liyanage, N.P.2    Doster, M.N.3    Vaccari, M.4    Vargas-Inchaustegui, D.A.5    Pegu, P.6    Schifanella, L.7    Shen, X.8    Tomaras, G.D.9    Rao, M.10
  • 47
    • 84860759632 scopus 로고    scopus 로고
    • B-cell-lineage immunogen design in vaccine development with HIV-1 as a case study
    • Haynes, B.F., Kelsoe, G., Harrison, S.C., Kepler, T.B., B-cell-lineage immunogen design in vaccine development with HIV-1 as a case study. Nat. Biotechnol. 30 (2012), 423–433.
    • (2012) Nat. Biotechnol. , vol.30 , pp. 423-433
    • Haynes, B.F.1    Kelsoe, G.2    Harrison, S.C.3    Kepler, T.B.4
  • 49
    • 67249131966 scopus 로고    scopus 로고
    • Broadly neutralizing human anti-HIV antibody 2G12 is effective in protection against mucosal SHIV challenge even at low serum neutralizing titers
    • Hessell, A.J., Rakasz, E.G., Poignard, P., Hangartner, L., Landucci, G., Forthal, D.N., Koff, W.C., Watkins, D.I., Burton, D.R., Broadly neutralizing human anti-HIV antibody 2G12 is effective in protection against mucosal SHIV challenge even at low serum neutralizing titers. PLoS Pathog., 5, 2009, e1000433.
    • (2009) PLoS Pathog. , vol.5 , pp. e1000433
    • Hessell, A.J.1    Rakasz, E.G.2    Poignard, P.3    Hangartner, L.4    Landucci, G.5    Forthal, D.N.6    Koff, W.C.7    Watkins, D.I.8    Burton, D.R.9
  • 53
    • 85016568747 scopus 로고    scopus 로고
    • The immunoregulatory roles of antibody glycosylation
    • Jennewein, M.F., Alter, G., The immunoregulatory roles of antibody glycosylation. Trends Immunol. 38 (2017), 358–372.
    • (2017) Trends Immunol. , vol.38 , pp. 358-372
    • Jennewein, M.F.1    Alter, G.2
  • 55
    • 85030100552 scopus 로고    scopus 로고
    • Protective efficacy of broadly neutralizing antibodies with incomplete neutralization activity against simian-human immunodeficiency virus in rhesus monkeys
    • e01187-17
    • Julg, B., Sok, D., Schmidt, S.D., Abbink, P., Newman, R.M., Broge, T., Linde, C., Nkolola, J., Le, K., Su, D., et al. Protective efficacy of broadly neutralizing antibodies with incomplete neutralization activity against simian-human immunodeficiency virus in rhesus monkeys. J. Virol., 91, 2017 e01187-17.
    • (2017) J. Virol. , vol.91
    • Julg, B.1    Sok, D.2    Schmidt, S.D.3    Abbink, P.4    Newman, R.M.5    Broge, T.6    Linde, C.7    Nkolola, J.8    Le, K.9    Su, D.10
  • 56
    • 33845590523 scopus 로고    scopus 로고
    • Comparison of biological activity among nonfucosylated therapeutic IgG1 antibodies with three different N-linked Fc oligosaccharides: the high-mannose, hybrid, and complex types
    • Kanda, Y., Yamada, T., Mori, K., Okazaki, A., Inoue, M., Kitajima-Miyama, K., Kuni-Kamochi, R., Nakano, R., Yano, K., Kakita, S., et al. Comparison of biological activity among nonfucosylated therapeutic IgG1 antibodies with three different N-linked Fc oligosaccharides: the high-mannose, hybrid, and complex types. Glycobiology 17 (2007), 104–118.
    • (2007) Glycobiology , vol.17 , pp. 104-118
    • Kanda, Y.1    Yamada, T.2    Mori, K.3    Okazaki, A.4    Inoue, M.5    Kitajima-Miyama, K.6    Kuni-Kamochi, R.7    Nakano, R.8    Yano, K.9    Kakita, S.10
  • 58
    • 85037581111 scopus 로고    scopus 로고
    • IgG subclass and vaccination stimulus determine changes in antigen specific antibody glycosylation in mice
    • Kao, D., Lux, A., Schaffert, A., Lang, R., Altmann, F., Nimmerjahn, F., IgG subclass and vaccination stimulus determine changes in antigen specific antibody glycosylation in mice. Eur. J. Immunol. 47 (2017), 2070–2079.
    • (2017) Eur. J. Immunol. , vol.47 , pp. 2070-2079
    • Kao, D.1    Lux, A.2    Schaffert, A.3    Lang, R.4    Altmann, F.5    Nimmerjahn, F.6
  • 61
    • 84875759341 scopus 로고    scopus 로고
    • Somatic mutations of the immunoglobulin framework are generally required for broad and potent HIV-1 neutralization
    • Klein, F., Diskin, R., Scheid, J.F., Gaebler, C., Mouquet, H., Georgiev, I.S., Pancera, M., Zhou, T., Incesu, R.B., Fu, B.Z., et al. Somatic mutations of the immunoglobulin framework are generally required for broad and potent HIV-1 neutralization. Cell 153 (2013), 126–138.
    • (2013) Cell , vol.153 , pp. 126-138
    • Klein, F.1    Diskin, R.2    Scheid, J.F.3    Gaebler, C.4    Mouquet, H.5    Georgiev, I.S.6    Pancera, M.7    Zhou, T.8    Incesu, R.B.9    Fu, B.Z.10
  • 62
    • 84863724161 scopus 로고    scopus 로고
    • Fucose content of monoclonal antibodies can be controlled by culture medium osmolality for high antibody-dependent cellular cytotoxicity
    • Konno, Y., Kobayashi, Y., Takahashi, K., Takahashi, E., Sakae, S., Wakitani, M., Yamano, K., Suzawa, T., Yano, K., Ohta, T., et al. Fucose content of monoclonal antibodies can be controlled by culture medium osmolality for high antibody-dependent cellular cytotoxicity. Cytotechnology 64 (2012), 249–265.
    • (2012) Cytotechnology , vol.64 , pp. 249-265
    • Konno, Y.1    Kobayashi, Y.2    Takahashi, K.3    Takahashi, E.4    Sakae, S.5    Wakitani, M.6    Yamano, K.7    Suzawa, T.8    Yano, K.9    Ohta, T.10
  • 63
    • 84923154103 scopus 로고    scopus 로고
    • Stable, uncleaved HIV-1 envelope glycoprotein gp140 forms a tightly folded trimer with a native-like structure
    • Kovacs, J.M., Noeldeke, E., Ha, H.J., Peng, H., Rits-Volloch, S., Harrison, S.C., Chen, B., Stable, uncleaved HIV-1 envelope glycoprotein gp140 forms a tightly folded trimer with a native-like structure. Proc. Natl. Acad. Sci. USA 111 (2014), 18542–18547.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 18542-18547
    • Kovacs, J.M.1    Noeldeke, E.2    Ha, H.J.3    Peng, H.4    Rits-Volloch, S.5    Harrison, S.C.6    Chen, B.7
  • 64
    • 84869022421 scopus 로고    scopus 로고
    • Adenovirus serotype 26 utilizes CD46 as a primary cellular receptor and only transiently activates T lymphocytes following vaccination of rhesus monkeys
    • Li, H., Rhee, E.G., Masek-Hammerman, K., Teigler, J.E., Abbink, P., Barouch, D.H., Adenovirus serotype 26 utilizes CD46 as a primary cellular receptor and only transiently activates T lymphocytes following vaccination of rhesus monkeys. J. Virol. 86 (2012), 10862–10865.
    • (2012) J. Virol. , vol.86 , pp. 10862-10865
    • Li, H.1    Rhee, E.G.2    Masek-Hammerman, K.3    Teigler, J.E.4    Abbink, P.5    Barouch, D.H.6
  • 65
    • 37849026069 scopus 로고    scopus 로고
    • Removal of a single N-linked glycan in human immunodeficiency virus type 1 gp120 results in an enhanced ability to induce neutralizing antibody responses
    • Li, Y., Cleveland, B., Klots, I., Travis, B., Richardson, B.A., Anderson, D., Montefiori, D., Polacino, P., Hu, S.L., Removal of a single N-linked glycan in human immunodeficiency virus type 1 gp120 results in an enhanced ability to induce neutralizing antibody responses. J. Virol. 82 (2008), 638–651.
    • (2008) J. Virol. , vol.82 , pp. 638-651
    • Li, Y.1    Cleveland, B.2    Klots, I.3    Travis, B.4    Richardson, B.A.5    Anderson, D.6    Montefiori, D.7    Polacino, P.8    Hu, S.L.9
  • 69
  • 70
    • 85039066883 scopus 로고    scopus 로고
    • Beyond binding: antibody effector functions in infectious diseases
    • Lu, L.L., Suscovich, T.J., Fortune, S.M., Alter, G., Beyond binding: antibody effector functions in infectious diseases. Nat. Rev. Immunol. 18 (2018), 46–61.
    • (2018) Nat. Rev. Immunol. , vol.18 , pp. 46-61
    • Lu, L.L.1    Suscovich, T.J.2    Fortune, S.M.3    Alter, G.4
  • 74
    • 84878626061 scopus 로고    scopus 로고
    • Engineering HIV envelope protein to activate germline B cell receptors of broadly neutralizing anti-CD4 binding site antibodies
    • McGuire, A.T., Hoot, S., Dreyer, A.M., Lippy, A., Stuart, A., Cohen, K.W., Jardine, J., Menis, S., Scheid, J.F., West, A.P., et al. Engineering HIV envelope protein to activate germline B cell receptors of broadly neutralizing anti-CD4 binding site antibodies. J. Exp. Med. 210 (2013), 655–663.
    • (2013) J. Exp. Med. , vol.210 , pp. 655-663
    • McGuire, A.T.1    Hoot, S.2    Dreyer, A.M.3    Lippy, A.4    Stuart, A.5    Cohen, K.W.6    Jardine, J.7    Menis, S.8    Scheid, J.F.9    West, A.P.10
  • 76
  • 82
    • 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., Moore, J.P., Burton, D.R., Antibody protects macaques against vaginal challenge with a pathogenic R5 simian/human immunodeficiency virus at serum levels giving complete neutralization in vitro. J. Virol. 75 (2001), 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    Moore, J.P.7    Burton, D.R.8
  • 83
    • 17644416719 scopus 로고    scopus 로고
    • Targeting the innate immune response with improved vaccine adjuvants
    • Pashine, A., Valiante, N.M., Ulmer, J.B., Targeting the innate immune response with improved vaccine adjuvants. Nat. Med. 11:4, Suppl (2005), S63–S68.
    • (2005) Nat. Med. , vol.11 , Issue.4 , pp. S63-S68
    • Pashine, A.1    Valiante, N.M.2    Ulmer, J.B.3
  • 84
    • 47549116006 scopus 로고    scopus 로고
    • Vaccines: correlates of vaccine-induced immunity
    • Plotkin, S.A., Vaccines: correlates of vaccine-induced immunity. Clin. Infect. Dis. 47 (2008), 401–409.
    • (2008) Clin. Infect. Dis. , vol.47 , pp. 401-409
    • Plotkin, S.A.1
  • 85
    • 84969565501 scopus 로고    scopus 로고
    • Enhancement of antibody-dependent cell mediated cytotoxicity: a new era in cancer treatment
    • Rajasekaran, N., Chester, C., Yonezawa, A., Zhao, X., Kohrt, H.E., Enhancement of antibody-dependent cell mediated cytotoxicity: a new era in cancer treatment. ImmunoTargets Ther. 4 (2015), 91–100.
    • (2015) ImmunoTargets Ther. , vol.4 , pp. 91-100
    • Rajasekaran, N.1    Chester, C.2    Yonezawa, A.3    Zhao, X.4    Kohrt, H.E.5
  • 86
    • 79957627493 scopus 로고    scopus 로고
    • A 2020 vision for vaccines against HIV, tuberculosis and malaria
    • Rappuoli, R., Aderem, A., A 2020 vision for vaccines against HIV, tuberculosis and malaria. Nature 473 (2011), 463–469.
    • (2011) Nature , vol.473 , pp. 463-469
    • Rappuoli, R.1    Aderem, A.2
  • 89
    • 0037389643 scopus 로고    scopus 로고
    • Rapid evolution of the neutralizing antibody response to HIV type 1 infection
    • Richman, D.D., Wrin, T., Little, S.J., Petropoulos, C.J., Rapid evolution of the neutralizing antibody response to HIV type 1 infection. Proc. Natl. Acad. Sci. USA 100 (2003), 4144–4149.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4144-4149
    • Richman, D.D.1    Wrin, T.2    Little, S.J.3    Petropoulos, C.J.4
  • 93
    • 84940771125 scopus 로고    scopus 로고
    • Human non-neutralizing HIV-1 envelope monoclonal antibodies limit the number of founder viruses during SHIV mucosal infection in Rhesus Macaques
    • Santra, S., Tomaras, G.D., Warrier, R., Nicely, N.I., Liao, H.X., Pollara, J., Liu, P., Alam, S.M., Zhang, R., Cocklin, S.L., et al. Human non-neutralizing HIV-1 envelope monoclonal antibodies limit the number of founder viruses during SHIV mucosal infection in Rhesus Macaques. PLoS Pathog., 11, 2015, e1005042.
    • (2015) PLoS Pathog. , vol.11 , pp. e1005042
    • Santra, S.1    Tomaras, G.D.2    Warrier, R.3    Nicely, N.I.4    Liao, H.X.5    Pollara, J.6    Liu, P.7    Alam, S.M.8    Zhang, R.9    Cocklin, S.L.10
  • 95
    • 84875410765 scopus 로고    scopus 로고
    • Intravenous immunoglobulin therapy: how does IgG modulate the immune system?
    • Schwab, I., Nimmerjahn, F., Intravenous immunoglobulin therapy: how does IgG modulate the immune system?. Nat. Rev. Immunol. 13 (2013), 176–189.
    • (2013) Nat. Rev. Immunol. , vol.13 , pp. 176-189
    • Schwab, I.1    Nimmerjahn, F.2
  • 97
    • 38749096240 scopus 로고    scopus 로고
    • The failed HIV Merck vaccine study: a step back or a launching point for future vaccine development?
    • Sekaly, R.P., The failed HIV Merck vaccine study: a step back or a launching point for future vaccine development?. J. Exp. Med. 205 (2008), 7–12.
    • (2008) J. Exp. Med. , vol.205 , pp. 7-12
    • Sekaly, R.P.1
  • 98
    • 85042688690 scopus 로고    scopus 로고
    • Integrating linear optimization with structural modeling to increase HIV neutralization breadth
    • Sevy, A.M., Panda, S., Crowe, J.E. Jr., Meiler, J., Vorobeychik, Y., Integrating linear optimization with structural modeling to increase HIV neutralization breadth. PLoS Comput. Biol., 14, 2018, e1005999.
    • (2018) PLoS Comput. Biol. , vol.14 , pp. e1005999
    • Sevy, A.M.1    Panda, S.2    Crowe, J.E.3    Meiler, J.4    Vorobeychik, Y.5
  • 101
    • 48949089988 scopus 로고    scopus 로고
    • Analysis of immunoglobulin glycosylation by LC-ESI-MS of glycopeptides and oligosaccharides
    • Stadlmann, J., Pabst, M., Kolarich, D., Kunert, R., Altmann, F., Analysis of immunoglobulin glycosylation by LC-ESI-MS of glycopeptides and oligosaccharides. Proteomics 8 (2008), 2858–2871.
    • (2008) Proteomics , vol.8 , pp. 2858-2871
    • Stadlmann, J.1    Pabst, M.2    Kolarich, D.3    Kunert, R.4    Altmann, F.5
  • 102
    • 37549033167 scopus 로고    scopus 로고
    • One step forward, two steps back—will there ever be an AIDS vaccine?
    • Steinbrook, R., One step forward, two steps back—will there ever be an AIDS vaccine?. N. Engl. J. Med. 357 (2007), 2653–2655.
    • (2007) N. Engl. J. Med. , vol.357 , pp. 2653-2655
    • Steinbrook, R.1
  • 103
    • 84879290459 scopus 로고    scopus 로고
    • A global approach to HIV-1 vaccine development
    • Stephenson, K.E., Barouch, D.H., A global approach to HIV-1 vaccine development. Immunol. Rev. 254 (2013), 295–304.
    • (2013) Immunol. Rev. , vol.254 , pp. 295-304
    • Stephenson, K.E.1    Barouch, D.H.2
  • 107
    • 84866152532 scopus 로고    scopus 로고
    • Vaccination with adenovirus serotypes 35, 26, and 48 elicits higher levels of innate cytokine responses than adenovirus serotype 5 in rhesus monkeys
    • Teigler, J.E., Iampietro, M.J., Barouch, D.H., Vaccination with adenovirus serotypes 35, 26, and 48 elicits higher levels of innate cytokine responses than adenovirus serotype 5 in rhesus monkeys. J. Virol. 86 (2012), 9590–9598.
    • (2012) J. Virol. , vol.86 , pp. 9590-9598
    • Teigler, J.E.1    Iampietro, M.J.2    Barouch, D.H.3
  • 108
    • 84906351273 scopus 로고    scopus 로고
    • Late endosomal trafficking of alternative serotype adenovirus vaccine vectors augments antiviral innate immunity
    • Teigler, J.E., Kagan, J.C., Barouch, D.H., Late endosomal trafficking of alternative serotype adenovirus vaccine vectors augments antiviral innate immunity. J. Virol. 88 (2014), 10354–10363.
    • (2014) J. Virol. , vol.88 , pp. 10354-10363
    • Teigler, J.E.1    Kagan, J.C.2    Barouch, D.H.3
  • 110
    • 84883348588 scopus 로고    scopus 로고
    • Induction of HIV-1 broad neutralizing antibodies in 2F5 knock-in mice: selection against membrane proximal external region-associated autoreactivity limits T-dependent responses
    • Verkoczy, L., Chen, Y., Zhang, J., Bouton-Verville, H., Newman, A., Lockwood, B., Scearce, R.M., Montefiori, D.C., Dennison, S.M., Xia, S.M., et al. Induction of HIV-1 broad neutralizing antibodies in 2F5 knock-in mice: selection against membrane proximal external region-associated autoreactivity limits T-dependent responses. J. Immunol. 191 (2013), 2538–2550.
    • (2013) J. Immunol. , vol.191 , pp. 2538-2550
    • Verkoczy, L.1    Chen, Y.2    Zhang, J.3    Bouton-Verville, H.4    Newman, A.5    Lockwood, B.6    Scearce, R.M.7    Montefiori, D.C.8    Dennison, S.M.9    Xia, S.M.10
  • 111
    • 79953667504 scopus 로고    scopus 로고
    • HIV-1 gp41 core with exposed membrane-proximal external region inducing broad HIV-1 neutralizing antibodies
    • Wang, J., Tong, P., Lu, L., Zhou, L., Xu, L., Jiang, S., Chen, Y.H., HIV-1 gp41 core with exposed membrane-proximal external region inducing broad HIV-1 neutralizing antibodies. PLoS One, 6, 2011, e18233.
    • (2011) PLoS One , vol.6 , pp. e18233
    • Wang, J.1    Tong, P.2    Lu, L.3    Zhou, L.4    Xu, L.5    Jiang, S.6    Chen, Y.H.7
  • 112
    • 84938493857 scopus 로고    scopus 로고
    • NK cell-mediated antibody-dependent cellular cytotoxicity in cancer immunotherapy
    • Wang, W., Erbe, A.K., Hank, J.A., Morris, Z.S., Sondel, P.M., NK cell-mediated antibody-dependent cellular cytotoxicity in cancer immunotherapy. Front. Immunol., 6, 2015, 368.
    • (2015) Front. Immunol. , vol.6 , pp. 368
    • Wang, W.1    Erbe, A.K.2    Hank, J.A.3    Morris, Z.S.4    Sondel, P.M.5
  • 115
    • 70449701456 scopus 로고    scopus 로고
    • 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
    • Xiao, X., Chen, W., Feng, Y., Zhu, Z., Prabakaran, P., Wang, Y., Zhang, M.Y., Longo, N.S., Dimitrov, D.S., 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 (2009), 404–409.
    • (2009) Biochem. Biophys. Res. Commun. , vol.390 , pp. 404-409
    • Xiao, X.1    Chen, W.2    Feng, Y.3    Zhu, Z.4    Prabakaran, P.5    Wang, Y.6    Zhang, M.Y.7    Longo, N.S.8    Dimitrov, D.S.9
  • 116
    • 85047980123 scopus 로고    scopus 로고
    • Epitope-based vaccine design yields fusion peptide-directed antibodies that neutralize diverse strains of HIV-1
    • Xu, K., Acharya, P., Kong, R., Cheng, C., Chuang, G.Y., Liu, K., Louder, M.K., O'Dell, S., Rawi, R., Sastry, M., et al. Epitope-based vaccine design yields fusion peptide-directed antibodies that neutralize diverse strains of HIV-1. Nat. Med. 24 (2018), 857–867.
    • (2018) Nat. Med. , vol.24 , pp. 857-867
    • Xu, K.1    Acharya, P.2    Kong, R.3    Cheng, C.4    Chuang, G.Y.5    Liu, K.6    Louder, M.K.7    O'Dell, S.8    Rawi, R.9    Sastry, M.10
  • 117
    • 84930418589 scopus 로고    scopus 로고
    • Structural repertoire of HIV-1-neutralizing antibodies targeting the CD4 supersite in 14 donors
    • Zhou, T., Lynch, R.M., Chen, L., Acharya, P., Wu, X., Doria-Rose, N.A., Joyce, M.G., Lingwood, D., Soto, C., Bailer, R.T., et al., NISC Comparative Sequencing Program. Structural repertoire of HIV-1-neutralizing antibodies targeting the CD4 supersite in 14 donors. Cell 161 (2015), 1280–1292.
    • (2015) Cell , vol.161 , pp. 1280-1292
    • Zhou, T.1    Lynch, R.M.2    Chen, L.3    Acharya, P.4    Wu, X.5    Doria-Rose, N.A.6    Joyce, M.G.7    Lingwood, D.8    Soto, C.9    Bailer, R.T.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.