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Volumn 10, Issue 3, 2015, Pages 151-159

Antibody engineering for increased potency, breadth and half-life

Author keywords

bispecific reagents; breadth; HIV 1; Keywords antibody engineering; polyreactivity; potency

Indexed keywords

BISPECIFIC ANTIBODY; FC RECEPTOR; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; REAGENT; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY;

EID: 84928564663     PISSN: 1746630X     EISSN: 17466318     Source Type: Journal    
DOI: 10.1097/COH.0000000000000148     Document Type: Review
Times cited : (44)

References (112)
  • 1
    • 84890859441 scopus 로고    scopus 로고
    • Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer
    • Lyumkis D, Julien JP, de Val N, et al. Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer. Science 2013; 342:1484-1490.
    • (2013) Science , vol.342 , pp. 1484-1490
    • Lyumkis, D.1    Julien, J.P.2    De Val, N.3
  • 2
    • 84890858459 scopus 로고    scopus 로고
    • Crystal structure of a soluble cleaved HIV-1 envelope trimer
    • Julien JP, Cupo A, Sok D, et al. Crystal structure of a soluble cleaved HIV-1 envelope trimer. Science 2013; 342:1477-1483.
    • (2013) Science , vol.342 , pp. 1477-1483
    • Julien, J.P.1    Cupo, A.2    Sok, D.3
  • 3
    • 23144441143 scopus 로고    scopus 로고
    • GlyProt: In silico glycosylation of proteins
    • Bohne-Lang A, von der Lieth CW. GlyProt: in silico glycosylation of proteins. Nucleic Acids Res 2005; 33:W214-219.
    • (2005) Nucleic Acids Res , vol.33 , pp. W214-219
    • Bohne-Lang, A.1    Von Der Lieth, C.W.2
  • 4
    • 84909640954 scopus 로고    scopus 로고
    • Structure and immune recognition of trimeric prefusion HIV-1 Env
    • Pancera M, Zhou T, Druz A, et al. Structure and immune recognition of trimeric prefusion HIV-1 Env. Nature 2014; 514:455-461.
    • (2014) Nature , vol.514 , pp. 455-461
    • Pancera, M.1    Zhou, T.2    Druz, A.3
  • 5
    • 0037456827 scopus 로고    scopus 로고
    • Antibody neutralization and escape by HIV-1
    • Wei X, Decker JM, Wang S, et al. Antibody neutralization and escape by HIV-1. Nature 2003; 422:307-312.
    • (2003) Nature , vol.422 , pp. 307-312
    • Wei, X.1    Decker, J.M.2    Wang, S.3
  • 6
    • 0037069682 scopus 로고    scopus 로고
    • HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites
    • Kwong PD, Doyle ML, Casper DJ, et al. HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites. Nature 2002; 420:678-682.
    • (2002) Nature , vol.420 , pp. 678-682
    • Kwong, P.D.1    Doyle, M.L.2    Casper, D.J.3
  • 7
    • 0141521564 scopus 로고    scopus 로고
    • Access of antibody molecules to the conserved coreceptor binding site on glycoprotein gp120 is sterically restricted on primary human immunodeficiency virus type 1
    • Labrijn AF, Poignard P, Raja A, et al. Access of antibody molecules to the conserved coreceptor binding site on glycoprotein gp120 is sterically restricted on primary human immunodeficiency virus type 1. J Virol 2003; 77:10557-10565.
    • (2003) J Virol , vol.77 , pp. 10557-10565
    • Labrijn, A.F.1    Poignard, P.2    Raja, A.3
  • 8
    • 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, Wyatt R, Robinson J, et al. 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
  • 9
    • 0030730243 scopus 로고    scopus 로고
    • Analysis of the interaction of the human immunodeficiency virus type 1 gp120 envelope glycoprotein with the gp41 transmembrane glycoprotein
    • Wyatt R, Desjardin E, Olshevsky U, et al. Analysis of the interaction of the human immunodeficiency virus type 1 gp120 envelope glycoprotein with the gp41 transmembrane glycoprotein. J Virol 1997; 71:9722-9731.
    • (1997) J Virol , vol.71 , pp. 9722-9731
    • Wyatt, R.1    Desjardin, E.2    Olshevsky, U.3
  • 10
    • 0030043169 scopus 로고    scopus 로고
    • Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein
    • Moore JP, 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
  • 11
    • 0022459886 scopus 로고
    • Identification and characterization of conserved and variable regions in the envelope gene of HTLV-III/LAV, the retrovirus of AIDS
    • Starcich BR, Hahn BH, Shaw GM, et al. Identification and characterization of conserved and variable regions in the envelope gene of HTLV-III/LAV, the retrovirus of AIDS. Cell 1986; 45:637-648.
    • (1986) Cell , vol.45 , pp. 637-648
    • Starcich, B.R.1    Hahn, B.H.2    Shaw, G.M.3
  • 12
    • 77954042425 scopus 로고    scopus 로고
    • Few and far between: How HIV may be evading antibody avidity
    • Klein JS, Bjorkman PJ. Few and far between: how HIV may be evading antibody avidity. PLoS Pathog 2010; 6:e1000908.
    • (2010) PLoS Pathog , vol.6 , pp. e1000908
    • Klein, J.S.1    Bjorkman, P.J.2
  • 13
    • 84922224963 scopus 로고    scopus 로고
    • Intra-spike crosslinking overcomes antibody evasion by HIV-1
    • Galimidi RP, Klein JS, Politzer MS, et al. Intra-spike crosslinking overcomes antibody evasion by HIV-1. Cell 2015; 160:433-446.
    • (2015) Cell , vol.160 , pp. 433-446
    • Galimidi, R.P.1    Klein, J.S.2    Politzer, M.S.3
  • 14
    • 70349887757 scopus 로고    scopus 로고
    • Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target
    • Walker LM, Phogat SK, Chan-Hui PY, et al. Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 2009; 326:285-289.
    • (2009) Science , vol.326 , pp. 285-289
    • Walker, L.M.1    Phogat, S.K.2    Chan-Hui, P.Y.3
  • 15
    • 77954920017 scopus 로고    scopus 로고
    • Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1
    • Wu X, Yang ZY, Li Y, 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
  • 16
    • 63849131879 scopus 로고    scopus 로고
    • Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals
    • Scheid JF, Mouquet H, Feldhahn N, et al. Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals. Nature 2009; 458:636-640.
    • (2009) Nature , vol.458 , pp. 636-640
    • Scheid, J.F.1    Mouquet, H.2    Feldhahn, N.3
  • 17
    • 0033952103 scopus 로고    scopus 로고
    • Human neutralizing monoclonal antibodies of the IgG1 subtype protect against mucosal simian-human immunodeficiency virus infection
    • Baba TW, Liska V, Hofmann-Lehmann R, et al. Human neutralizing monoclonal antibodies of the IgG1 subtype protect against mucosal simian-human immunodeficiency virus infection. Nat Med 2000; 6:200-206.
    • (2000) Nat Med , vol.6 , pp. 200-206
    • Baba, T.W.1    Liska, V.2    Hofmann-Lehmann, R.3
  • 18
    • 84855466746 scopus 로고    scopus 로고
    • Antibody-based protection against HIV infection by vectored immunoprophylaxis
    • Balazs AB, Chen J, Hong CM, et al. Antibody-based protection against HIV infection by vectored immunoprophylaxis. Nature 2012; 48:81-88.
    • (2012) Nature , vol.48 , pp. 81-88
    • Balazs, A.B.1    Chen, J.2    Hong, C.M.3
  • 19
    • 68349150945 scopus 로고    scopus 로고
    • Vector-mediated gene transfer engenders long-lived neutralizing activity and protection against SIV infection in monkeys
    • Johnson PR, Schnepp BC, Zhang JC, et al. Vector-mediated gene transfer engenders long-lived neutralizing activity and protection against SIV infection in monkeys. Nat Med 2009; 15:901-906.
    • (2009) Nat Med , vol.15 , pp. 901-906
    • Johnson, P.R.1    Schnepp, B.C.2    Zhang, J.C.3
  • 20
    • 0033951746 scopus 로고    scopus 로고
    • Protection of macaques against vaginal transmission of a pathogenic HIV-1/SIV chimeric virus by passive infusion of neutralizing antibodies
    • Mascola JR, Stiegler G, VanCott TC, et al. Protection of macaques against vaginal transmission of a pathogenic HIV-1/SIV chimeric virus by passive infusion of neutralizing antibodies. Nat Med 2000; 6:207-210.
    • (2000) Nat Med , vol.6 , pp. 207-210
    • Mascola, J.R.1    Stiegler, G.2    Vancott, T.C.3
  • 21
    • 84887626950 scopus 로고    scopus 로고
    • Therapeutic efficacy of potent neutralizing HIV-1-specific monoclonal antibodies in SHIV-infected rhesus monkeys
    • Barouch DH, Whitney JB, Moldt B, et al. Therapeutic efficacy of potent neutralizing HIV-1-specific monoclonal antibodies in SHIV-infected rhesus monkeys. Nature 2013; 503:224-228.
    • (2013) Nature , vol.503 , pp. 224-228
    • Barouch, D.H.1    Whitney, J.B.2    Moldt, B.3
  • 22
    • 84870562234 scopus 로고    scopus 로고
    • HIV therapy by a combination of broadly neutralizing antibodies in humanized mice
    • Klein F, Halper-Stromberg A, Horwitz JA, et al. HIV therapy by a combination of broadly neutralizing antibodies in humanized mice. Nature 2012; 492:118-122.
    • (2012) Nature , vol.492 , pp. 118-122
    • Klein, F.1    Halper-Stromberg, A.2    Horwitz, J.A.3
  • 23
    • 84887627657 scopus 로고    scopus 로고
    • Antibody-mediated immunotherapy of macaques chronically infected with SHIV suppresses viraemia
    • Shingai M, Nishimura Y, Klein F, et al. Antibody-mediated immunotherapy of macaques chronically infected with SHIV suppresses viraemia. Nature 2013; 503:277-280.
    • (2013) Nature , vol.503 , pp. 277-280
    • Shingai, M.1    Nishimura, Y.2    Klein, F.3
  • 24
    • 84907379431 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies and viral inducers decrease rebound from HIV-1 latent reservoirs in humanized mice
    • Halper-Stromberg A, Lu CL, Klein F, et al. Broadly neutralizing antibodies and viral inducers decrease rebound from HIV-1 latent reservoirs in humanized mice. Cell 2014; 158:989-999.
    • (2014) Cell , vol.158 , pp. 989-999
    • Halper-Stromberg, A.1    Lu, C.L.2    Klein, F.3
  • 25
    • 84866495323 scopus 로고    scopus 로고
    • Human antibodies that neutralize HIV-1: Identification, structures, and B cell ontogenies
    • Kwong PD, Mascola JR. Human antibodies that neutralize HIV-1: identification, structures, and B cell ontogenies. Immunity 2012; 37:412-425.
    • (2012) Immunity , vol.37 , pp. 412-425
    • Kwong, P.D.1    Mascola, J.R.2
  • 26
    • 84899909771 scopus 로고    scopus 로고
    • Antibody 8ANC195 reveals a site of broad vulnerability on the HIV-1 envelope spike
    • Scharf L, Scheid JF, Lee JH, et al. Antibody 8ANC195 reveals a site of broad vulnerability on the HIV-1 envelope spike. Cell Rep 2014; 7:785-795.
    • (2014) Cell Rep , vol.7 , pp. 785-795
    • Scharf, L.1    Scheid, J.F.2    Lee, J.H.3
  • 27
    • 84900467984 scopus 로고    scopus 로고
    • Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers
    • Blattner C, Lee JH, Sliepen K, et al. Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers. Immunity 2014; 40:669-680.
    • (2014) Immunity , vol.40 , pp. 669-680
    • Blattner, C.1    Lee, J.H.2    Sliepen, K.3
  • 28
    • 84900517557 scopus 로고    scopus 로고
    • Broadly neutralizing HIV antibodies define a glycan-dependent epitope on the prefusion conformation of gp41 on cleaved envelope trimers
    • Falkowska E, Le KM, Ramos A, et al. Broadly neutralizing HIV antibodies define a glycan-dependent epitope on the prefusion conformation of gp41 on cleaved envelope trimers. Immunity 2014; 40:657-668.
    • (2014) Immunity , vol.40 , pp. 657-668
    • Falkowska, E.1    Le, K.M.2    Ramos, A.3
  • 29
    • 84870724432 scopus 로고    scopus 로고
    • Identification and characterization of a broadly cross-reactive HIV-1 human monoclonal antibody that binds to both gp120 and gp41
    • Zhang MY, Yuan T, Li J, et al. Identification and characterization of a broadly cross-reactive HIV-1 human monoclonal antibody that binds to both gp120 and gp41. PLoS One 2012; 7:e44241.
    • (2012) PLoS One , vol.7 , pp. e44241
    • Zhang, M.Y.1    Yuan, T.2    Li, J.3
  • 30
    • 84921607768 scopus 로고    scopus 로고
    • Broad and potent HIV-1 neutralization by a human antibody that binds the gp41-gp120 interface
    • Huang J, Kang BH, Pancera M, et al. Broad and potent HIV-1 neutralization by a human antibody that binds the gp41-gp120 interface. Nature 2014; 515:138-142.
    • (2014) Nature , vol.515 , pp. 138-142
    • Huang, J.1    Kang, B.H.2    Pancera, M.3
  • 31
    • 84892373125 scopus 로고    scopus 로고
    • Protein engineering strategies for the development of viral vaccines and immunotherapeutics
    • Koellhoffer JF, Higgins CD, Lai JR. Protein engineering strategies for the development of viral vaccines and immunotherapeutics. FEBS Lett 2014; 588:298-307.
    • (2014) FEBS Lett , vol.588 , pp. 298-307
    • Koellhoffer, J.F.1    Higgins, C.D.2    Lai, J.R.3
  • 32
    • 79955665534 scopus 로고    scopus 로고
    • Engineering the variable region of therapeutic IgG antibodies
    • Igawa T, Tsunoda H, Kuramochi T, et al. Engineering the variable region of therapeutic IgG antibodies. MAbs 2011; 3:243-252.
    • (2011) MAbs , vol.3 , pp. 243-252
    • Igawa, T.1    Tsunoda, H.2    Kuramochi, T.3
  • 33
    • 0037246095 scopus 로고    scopus 로고
    • Further improvement of broad specificity hapten recognition with protein engineering
    • Korpimaki T, Rosenberg J, Virtanen P, et al. Further improvement of broad specificity hapten recognition with protein engineering. Protein Eng 2003; 16:37-46.
    • (2003) Protein Eng , vol.16 , pp. 37-46
    • Korpimaki, T.1    Rosenberg, J.2    Virtanen, P.3
  • 34
    • 33846138044 scopus 로고    scopus 로고
    • Molecular evolution of antibody cross-reactivity for two subtypes of type A botulinum neurotoxin
    • Garcia-Rodriguez C, Levy R, Arndt JW, et al. Molecular evolution of antibody cross-reactivity for two subtypes of type A botulinum neurotoxin. Nat Biotechnol 2007; 25:107-116.
    • (2007) Nat Biotechnol , vol.25 , pp. 107-116
    • Garcia-Rodriguez, C.1    Levy, R.2    Arndt, J.W.3
  • 35
    • 57149089660 scopus 로고    scopus 로고
    • Broadening of neutralization activity to directly block a dominant antibody-driven SARS-coronavirus evolution pathway
    • Sui J, Aird DR, Tamin A, et al. Broadening of neutralization activity to directly block a dominant antibody-driven SARS-coronavirus evolution pathway. PLoS Pathog 2008; 4:e1000197.
    • (2008) PLoS Pathog , vol.4 , pp. e1000197
    • Sui, J.1    Aird, D.R.2    Tamin, A.3
  • 36
    • 33646146483 scopus 로고    scopus 로고
    • Affinity enhancement of an in vivo matured therapeutic antibody using structure-based computational design
    • Clark LA, Boriack-Sjodin PA, Eldredge J, et al. Affinity enhancement of an in vivo matured therapeutic antibody using structure-based computational design. Protein Sci 2006; 15:949-960.
    • (2006) Protein Sci , vol.15 , pp. 949-960
    • Clark, L.A.1    Boriack-Sjodin, P.A.2    Eldredge, J.3
  • 37
    • 48249111382 scopus 로고    scopus 로고
    • Affinity maturation of antibodies assisted by in silico modeling
    • Barderas R, Desmet J, Timmerman P, et al. Affinity maturation of antibodies assisted by in silico modeling. Proc Natl Acad Sci U S A 2008; 105:9029-9034.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 9029-9034
    • Barderas, R.1    Desmet, J.2    Timmerman, P.3
  • 38
    • 34548528158 scopus 로고    scopus 로고
    • Progress in computational protein design
    • Lippow SM, Tidor B. Progress in computational protein design. Curr Opin Biotechnol 2007; 18:305-311.
    • (2007) Curr Opin Biotechnol , vol.18 , pp. 305-311
    • Lippow, S.M.1    Tidor, B.2
  • 39
    • 35148855712 scopus 로고    scopus 로고
    • Computational design of antibody-affinity improvement beyond in vivo maturation
    • Lippow SM, Wittrup KD, Tidor B. Computational design of antibody-affinity improvement beyond in vivo maturation. Nat Biotechnol 2007; 25:1171-1176.
    • (2007) Nat Biotechnol , vol.25 , pp. 1171-1176
    • Lippow, S.M.1    Wittrup, K.D.2    Tidor, B.3
  • 40
    • 0029564921 scopus 로고
    • CDR walking mutagenesis for the affinity maturation of a potent human anti-HIV-1 antibody into the picomolar range
    • Yang WP, Green K, Pinz-Sweeney S, et al. CDR walking mutagenesis for the affinity maturation of a potent human anti-HIV-1 antibody into the picomolar range. J Mol Biol 1995; 254:392-403.
    • (1995) J Mol Biol , vol.254 , pp. 392-403
    • Yang, W.P.1    Green, K.2    Pinz-Sweeney, S.3
  • 41
    • 0028348564 scopus 로고
    • In vitro evolution of a neutralizing human antibody to human immunodeficiency virus type 1 to enhance affinity and broaden strain cross-reactivity
    • Barbas CF 3rd, Hu D, Dunlop N, et al. In vitro evolution of a neutralizing human antibody to human immunodeficiency virus type 1 to enhance affinity and broaden strain cross-reactivity. Proc Natl Acad Sci U S A 1994; 91:3809-3813.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 3809-3813
    • Barbas, C.F.1    Hu, D.2    Dunlop, N.3
  • 42
    • 0344255655 scopus 로고    scopus 로고
    • Improved breadth and potency of an HIV-1-neutralizing human single-chain antibody by random mutagenesis and sequential antigen panning
    • Zhang MY, Shu Y, Rudolph D, et al. Improved breadth and potency of an HIV-1-neutralizing human single-chain antibody by random mutagenesis and sequential antigen panning. J Mol Biol 2004; 335:209-219.
    • (2004) J Mol Biol , vol.335 , pp. 209-219
    • Zhang, M.Y.1    Shu, Y.2    Rudolph, D.3
  • 43
    • 84883187027 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies and the search for an HIV-1 vaccine: The end of the beginning
    • Kwong PD, Mascola JR, Nabel GJ. Broadly neutralizing antibodies and the search for an HIV-1 vaccine: The end of the beginning. Nat Rev Immunol 2013; 13:693-701.
    • (2013) Nat Rev Immunol , vol.13 , pp. 693-701
    • Kwong, P.D.1    Mascola, J.R.2    Nabel, G.J.3
  • 44
    • 84894173514 scopus 로고    scopus 로고
    • Structural insights on the role of antibodies in HIV-1 vaccine and therapy
    • West AP Jr, Scharf L, Scheid JF, et al. Structural insights on the role of antibodies in HIV-1 vaccine and therapy. Cell 2014; 156:633-648.
    • (2014) Cell , vol.156 , pp. 633-648
    • West, A.P.1    Scharf, L.2    Scheid, J.F.3
  • 45
    • 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 JF, et al. Somatic mutations of the immunoglobulin framework are generally required for broad and potent HIV-1 neutralization. Cell 2013; 153:126-138.
    • (2013) Cell , vol.153 , pp. 126-138
    • Klein, F.1    Diskin, R.2    Scheid, J.F.3
  • 46
    • 80052925616 scopus 로고    scopus 로고
    • Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding
    • Scheid JF, Mouquet H, Ueberheide B, et al. Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding. Science 2011; 333:1633-1637.
    • (2011) Science , vol.333 , pp. 1633-1637
    • Scheid, J.F.1    Mouquet, H.2    Ueberheide, B.3
  • 47
    • 80053132436 scopus 로고    scopus 로고
    • Broad neutralization coverage of HIV by multiple highly potent antibodies
    • Walker LM, Huber M, Doores KJ, 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
  • 48
    • 77954943648 scopus 로고    scopus 로고
    • Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01
    • Zhou T, Georgiev I, Wu X, et al. Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01. Science 2010; 329:811-817.
    • (2010) Science , vol.329 , pp. 811-817
    • Zhou, T.1    Georgiev, I.2    Wu, X.3
  • 49
    • 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 JP, Hinz A, 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 , pp. e8805
    • Corti, D.1    Langedijk, J.P.2    Hinz, A.3
  • 50
    • 80052942203 scopus 로고    scopus 로고
    • Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing
    • Wu X, Zhou T, Zhu J, 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
  • 51
    • 77953655567 scopus 로고    scopus 로고
    • Maturation pathways of cross-reactive HIV-1 neutralizing antibodies
    • Xiao X, Chen W, Feng Y, Dimitrov DS. Maturation pathways of cross-reactive HIV-1 neutralizing antibodies. Viruses 2009; 1:802-817.
    • (2009) Viruses , vol.1 , pp. 802-817
    • Xiao, X.1    Chen, W.2    Feng, Y.3    Dimitrov, D.S.4
  • 52
    • 84893352067 scopus 로고    scopus 로고
    • Antibodies VRC01 and 10E8 neutralize HIV-1 with high breadth and potency even with Ig-framework regions substantially reverted to germline
    • Georgiev IS, Rudicell RS, Saunders KO, et al. Antibodies VRC01 and 10E8 neutralize HIV-1 with high breadth and potency even with Ig-framework regions substantially reverted to germline. J Immunol 2014; 192:1100-1106.
    • (2014) J Immunol , vol.192 , pp. 1100-1106
    • Georgiev, I.S.1    Rudicell, R.S.2    Saunders, K.O.3
  • 53
    • 84864363185 scopus 로고    scopus 로고
    • Structural basis for germ-line 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. Structural basis for germ-line gene usage of a potent class of antibodies targeting the CD4-binding site of HIV-1 gp120. Proc Natl Acad Sci U S A 2012; 109:E2083-E2090.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. E2083-E2090
    • West, A.P.1    Diskin, R.2    Nussenzweig, M.C.3    Bjorkman, P.J.4
  • 54
    • 84907971356 scopus 로고    scopus 로고
    • Enhanced potency of a broadly neutralizing HIV-1 antibody in vitro improves protection against lentiviral infection in vivo
    • Rudicell RS, Kwon YD, Ko SY, et al. Enhanced potency of a broadly neutralizing HIV-1 antibody in vitro improves protection against lentiviral infection in vivo. J Virol 2014; 88:12669-12682.
    • (2014) J Virol , vol.88 , pp. 12669-12682
    • Rudicell, R.S.1    Kwon, Y.D.2    Ko, S.Y.3
  • 55
    • 82755184131 scopus 로고    scopus 로고
    • Increasing the potency and breadth of an HIV antibody by using structure-based rational design
    • Diskin R, Scheid JF, Marcovecchio PM, et al. Increasing the potency and breadth of an HIV antibody by using structure-based rational design. Science 2011; 334:1289-1293.
    • (2011) Science , vol.334 , pp. 1289-1293
    • Diskin, R.1    Scheid, J.F.2    Marcovecchio, P.M.3
  • 56
    • 84879523938 scopus 로고    scopus 로고
    • Restricting HIV-1 pathways for escape using rationally designed anti-HIV-1 antibodies
    • Diskin R, Klein F, Horwitz JA, et al. Restricting HIV-1 pathways for escape using rationally designed anti-HIV-1 antibodies. J Exp Med 2013; 210:1235-1249.
    • (2013) J Exp Med , vol.210 , pp. 1235-1249
    • Diskin, R.1    Klein, F.2    Horwitz, J.A.3
  • 57
    • 84869831194 scopus 로고    scopus 로고
    • Complex-type N-glycan recognition by potent broadly neutralizing HIV antibodies
    • Mouquet H, Scharf L, Euler Z, et al. Complex-type N-glycan recognition by potent broadly neutralizing HIV antibodies. Proc Natl Acad Sci U S A 2012; 109:E3268-E3277.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. E3268-E3277
    • Mouquet, H.1    Scharf, L.2    Euler, Z.3
  • 58
    • 84907527916 scopus 로고    scopus 로고
    • Structural evolution of glycan recognition by a family of potent HIV antibodies
    • Garces F, Sok D, Kong L, et al. Structural evolution of glycan recognition by a family of potent HIV antibodies. Cell 2014; 159:69-79.
    • (2014) Cell , vol.159 , pp. 69-79
    • Garces, F.1    Sok, D.2    Kong, L.3
  • 59
    • 84917705974 scopus 로고    scopus 로고
    • Recombinant HIV envelope trimer selects for quaternary-dependent antibodies targeting the trimer apex
    • Sok D, van Gils MJ, Pauthner M, et al. Recombinant HIV envelope trimer selects for quaternary-dependent antibodies targeting the trimer apex. Proc Natl Acad Sci U S A 2014; 111:17624-17629.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 17624-17629
    • Sok, D.1    Van Gils, M.J.2    Pauthner, M.3
  • 60
    • 80052287270 scopus 로고    scopus 로고
    • Mechanism of neutralization by the broadly neutralizing HIV-1 monoclonal antibody VRC01
    • Li Y, O'Dell S, Walker LM, et al. Mechanism of neutralization by the broadly neutralizing HIV-1 monoclonal antibody VRC01. J Virol 2011; 85:8954-8967.
    • (2011) J Virol , vol.85 , pp. 8954-8967
    • Li, Y.1    O'dell, S.2    Walker, L.M.3
  • 61
    • 76349123565 scopus 로고    scopus 로고
    • Enhanced antibody half-life improves in vivo activity
    • Zalevsky J, Chamberlain AK, Horton HM, et al. Enhanced antibody half-life improves in vivo activity. Nat Biotechnol 2010; 28:157-159.
    • (2010) Nat Biotechnol , vol.28 , pp. 157-159
    • Zalevsky, J.1    Chamberlain, A.K.2    Horton, H.M.3
  • 62
    • 84880149399 scopus 로고    scopus 로고
    • Structural basis for diverse N-glycan recognition by HIV-1-neutralizing V1-V2-directed antibody PG16
    • Pancera M, Shahzad-Ul-Hussan S, Doria-Rose NA, et al. Structural basis for diverse N-glycan recognition by HIV-1-neutralizing V1-V2-directed antibody PG16. Nat Struct Mol Biol 2013; 20:804-813.
    • (2013) Nat Struct Mol Biol , vol.20 , pp. 804-813
    • Pancera, M.1    Shahzad-Ul-Hussan, S.2    Doria-Rose, N.A.3
  • 63
    • 84891680667 scopus 로고    scopus 로고
    • Mechanism of HIV-1 neutralization by antibodies targeting a membrane-proximal region of gp41
    • Chen J, Frey G, Peng H, et al. Mechanism of HIV-1 neutralization by antibodies targeting a membrane-proximal region of gp41. J Virol 2014; 88:1249-1258.
    • (2014) J Virol , vol.88 , pp. 1249-1258
    • Chen, J.1    Frey, G.2    Peng, H.3
  • 64
    • 78651076742 scopus 로고    scopus 로고
    • Evolving concepts of specificity in immune reactions
    • Eisen HN, Chakraborty AK. Evolving concepts of specificity in immune reactions. Proc Natl Acad Sci U S A 2010; 107:22373-22380.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 22373-22380
    • Eisen, H.N.1    Chakraborty, A.K.2
  • 65
    • 84862314634 scopus 로고    scopus 로고
    • Polyreactive antibodies in adaptive immune responses to viruses
    • Mouquet H, Nussenzweig MC. Polyreactive antibodies in adaptive immune responses to viruses. Cell Mol Life Sci 2012; 69:1435-1445.
    • (2012) Cell Mol Life Sci , vol.69 , pp. 1435-1445
    • Mouquet, H.1    Nussenzweig, M.C.2
  • 66
    • 1642315560 scopus 로고    scopus 로고
    • Polyreactivity of antibody molecules
    • Notkins AL. Polyreactivity of antibody molecules. Trends Immunol 2004; 25:174-179.
    • (2004) Trends Immunol , vol.25 , pp. 174-179
    • Notkins, A.L.1
  • 67
    • 20444485767 scopus 로고    scopus 로고
    • Cellular and genetic mechanisms of self tolerance and autoimmunity
    • Goodnow CC, Sprent J, Fazekas de St Groth B, Vinuesa CG. Cellular and genetic mechanisms of self tolerance and autoimmunity. Nature 2005; 435:590-597.
    • (2005) Nature , vol.435 , pp. 590-597
    • Goodnow, C.C.1    Sprent, J.2    Fazekas De St Groth, B.3    Vinuesa, C.G.4
  • 68
    • 33344465620 scopus 로고    scopus 로고
    • A checkpoint for autoreactivity in human IgM memory B cell development
    • Tsuiji M, Yurasov S, Velinzon K, et al. A checkpoint for autoreactivity in human IgM memory B cell development. J Exp Med 2006; 203:393-400.
    • (2006) J Exp Med , vol.203 , pp. 393-400
    • Tsuiji, M.1    Yurasov, S.2    Velinzon, K.3
  • 69
    • 0041689676 scopus 로고    scopus 로고
    • Predominant autoantibody production by early human B cell precursors
    • Wardemann H, Yurasov S, Schaefer A, et al. Predominant autoantibody production by early human B cell precursors. Science 2003; 301:1374-1377.
    • (2003) Science , vol.301 , pp. 1374-1377
    • Wardemann, H.1    Yurasov, S.2    Schaefer, A.3
  • 70
    • 84894503603 scopus 로고    scopus 로고
    • Polyreactive antibodies plus complement enhance the phagocytosis of cells made apoptotic by UV-light or HIV
    • Zhou ZH, Wild T, Xiong Y, et al. Polyreactive antibodies plus complement enhance the phagocytosis of cells made apoptotic by UV-light or HIV. Sci Rep 2013; 3:2271.
    • (2013) Sci Rep , vol.3 , pp. 2271
    • Zhou, Z.H.1    Wild, T.2    Xiong, Y.3
  • 71
    • 33947721996 scopus 로고    scopus 로고
    • The broad antibacterial activity of the natural antibody repertoire is due to polyreactive antibodies
    • Zhou ZH, Zhang Y, Hu YF, et al. The broad antibacterial activity of the natural antibody repertoire is due to polyreactive antibodies. Cell Host Microbe 2007; 1:51-61.
    • (2007) Cell Host Microbe , vol.1 , pp. 51-61
    • Zhou, Z.H.1    Zhang, Y.2    Hu, Y.F.3
  • 73
    • 0023912169 scopus 로고
    • Association of human immunodeficiency virus infection and autoimmune phenomena
    • Kopelman RG, Zolla-Pazner S. Association of human immunodeficiency virus infection and autoimmune phenomena. Am J Med 1988; 84:82-88.
    • (1988) Am J Med , vol.84 , pp. 82-88
    • Kopelman, R.G.1    Zolla-Pazner, S.2
  • 74
    • 0023870864 scopus 로고
    • Acquired immune deficiency syndrome (AIDS) and autoimmunity-mutually exclusive entities
    • Solinger AM, Adams LE, Friedman-Kien AE, Hess EV. Acquired immune deficiency syndrome (AIDS) and autoimmunity-mutually exclusive entities? J Clin Immunol 1988; 8:32-42.
    • (1988) J Clin Immunol , vol.8 , pp. 32-42
    • Solinger, A.M.1    Adams, L.E.2    Friedman-Kien, A.E.3    Hess, E.V.4
  • 75
    • 21344434534 scopus 로고    scopus 로고
    • Cardiolipin polyspecific autoreactivity in two broadly neutralizing HIV-1 antibodies
    • Haynes BF, Fleming J, St Clair EW, et al. Cardiolipin polyspecific autoreactivity in two broadly neutralizing HIV-1 antibodies. Science 2005; 308:1906-1908.
    • (2005) Science , vol.308 , pp. 1906-1908
    • Haynes, B.F.1    Fleming, J.2    St Clair, E.W.3
  • 76
    • 80053584837 scopus 로고    scopus 로고
    • Isolation of a human anti-HIV gp41 membrane proximal region neutralizing antibody by antigen-specific single B cell sorting
    • Morris L, Chen X, Alam M, et al. Isolation of a human anti-HIV gp41 membrane proximal region neutralizing antibody by antigen-specific single B cell sorting. PLoS One 2011; 6:e23532.
    • (2011) PLoS One , vol.6 , pp. e23532
    • Morris, L.1    Chen, X.2    Alam, M.3
  • 77
    • 80055118908 scopus 로고    scopus 로고
    • Initial antibodies binding to HIV-1 gp41 in acutely infected subjects are polyreactive and highly mutated
    • Liao HX, Chen X, Munshaw S, et al. Initial antibodies binding to HIV-1 gp41 in acutely infected subjects are polyreactive and highly mutated. J Exp Med 2011; 208:2237-2249.
    • (2011) J Exp Med , vol.208 , pp. 2237-2249
    • Liao, H.X.1    Chen, X.2    Munshaw, S.3
  • 78
    • 33947635198 scopus 로고    scopus 로고
    • The role of antibody polyspecificity and lipid reactivity in binding of broadly neutralizing anti-HIV-1 envelope human monoclonal antibodies 2F5 and 4E10 to glycoprotein 41 membrane proximal envelope epitopes
    • Alam SM, McAdams M, Boren D, et al. The role of antibody polyspecificity and lipid reactivity in binding of broadly neutralizing anti-HIV-1 envelope human monoclonal antibodies 2F5 and 4E10 to glycoprotein 41 membrane proximal envelope epitopes. J Immunol 2007; 178:4424-4435.
    • (2007) J Immunol , vol.178 , pp. 4424-4435
    • Alam, S.M.1    McAdams, M.2    Boren, D.3
  • 79
    • 60549089534 scopus 로고    scopus 로고
    • Lipid binding properties of 4E10, 2F5, and WR304 monoclonal antibodies that neutralize HIV-1
    • Matyas GR, Beck Z, Karasavvas N, Alving CR. Lipid binding properties of 4E10, 2F5, and WR304 monoclonal antibodies that neutralize HIV-1. Biochim Biophys Acta 2009; 1788:660-665.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 660-665
    • Matyas, G.R.1    Beck, Z.2    Karasavvas, N.3    Alving, C.R.4
  • 80
    • 78651388412 scopus 로고    scopus 로고
    • Nonneutralizing HIV-1 gp41 envelope cluster II human monoclonal antibodies show polyreactivity for binding to phospholipids and protein autoantigens
    • Dennison SM, Anasti K, Scearce RM, et al. Nonneutralizing HIV-1 gp41 envelope cluster II human monoclonal antibodies show polyreactivity for binding to phospholipids and protein autoantigens. J Virol 2011; 85:1340-1347.
    • (2011) J Virol , vol.85 , pp. 1340-1347
    • Dennison, S.M.1    Anasti, K.2    Scearce, R.M.3
  • 81
    • 4544379899 scopus 로고    scopus 로고
    • Structure and mechanistic analysis of the antihuman immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope
    • Ofek G, Tang M, Sambor A, et al. Structure and mechanistic analysis of the antihuman immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope. J Virol 2004; 78:10724-10737.
    • (2004) J Virol , vol.78 , pp. 10724-10737
    • Ofek, G.1    Tang, M.2    Sambor, A.3
  • 82
    • 84874562109 scopus 로고    scopus 로고
    • Identification of autoantigens recognized by the 2F5 and 4E10 broadly neutralizing HIV-1 antibodies
    • Yang G, Holl TM, Liu Y, et al. Identification of autoantigens recognized by the 2F5 and 4E10 broadly neutralizing HIV-1 antibodies. J Exp Med 2013; 210:241-256.
    • (2013) J Exp Med , vol.210 , pp. 241-256
    • Yang, G.1    Holl, T.M.2    Liu, Y.3
  • 83
    • 84884698156 scopus 로고    scopus 로고
    • Autoreactivity and exceptional CDR plasticity (but not unusual polyspecificity) hinder elicitation of the anti-HIV antibody 4E10
    • Finton KA, Larimore K, Larman HB, et al. Autoreactivity and exceptional CDR plasticity (but not unusual polyspecificity) hinder elicitation of the anti-HIV antibody 4E10. PLoS Pathog 2013; 9:e1003639.
    • (2013) PLoS Pathog , vol.9 , pp. e1003639
    • Finton, K.A.1    Larimore, K.2    Larman, H.B.3
  • 84
    • 84866493348 scopus 로고    scopus 로고
    • Broad and potent neutralization of HIV-1 by a gp41-specific human antibody
    • Huang J, Ofek G, Laub L, et al. Broad and potent neutralization of HIV-1 by a gp41-specific human antibody. Nature 2012; 491:406-412.
    • (2012) Nature , vol.491 , pp. 406-412
    • Huang, J.1    Ofek, G.2    Laub, L.3
  • 85
    • 84919430580 scopus 로고    scopus 로고
    • Polyreactivity and autoreactivity among HIV-1 antibodies
    • Liu M, Yang G,Wiehe K, et al. Polyreactivity and autoreactivity among HIV-1 antibodies. J Virol 2015; 89:784-798.
    • (2015) J Virol , vol.89 , pp. 784-798
    • Liu, M.1    Yang, G.2    Wiehe, K.3
  • 86
    • 77957355961 scopus 로고    scopus 로고
    • Polyreactivity increases the apparent affinity of anti-HIV antibodies by heteroligation
    • Mouquet H, Scheid JF, Zoller MJ, et al. Polyreactivity increases the apparent affinity of anti-HIV antibodies by heteroligation. Nature 2010; 467:591-595.
    • (2010) Nature , vol.467 , pp. 591-595
    • Mouquet, H.1    Scheid, J.F.2    Zoller, M.J.3
  • 87
    • 80052531336 scopus 로고    scopus 로고
    • Memory B cell antibodies to HIV-1 gp140 cloned from individuals infected with clade A and B viruses
    • Mouquet H, Klein F, Scheid JF, et al. Memory B cell antibodies to HIV-1 gp140 cloned from individuals infected with clade A and B viruses. PLoS One 2011; 6:e24078.
    • (2011) PLoS One , vol.6 , pp. e24078
    • Mouquet, H.1    Klein, F.2    Scheid, J.F.3
  • 88
    • 84869840045 scopus 로고    scopus 로고
    • A strategy for risk mitigation of antibodies with fast clearance
    • Hotzel I, Theil FP, Bernstein LJ, et al. A strategy for risk mitigation of antibodies with fast clearance. MAbs 2012; 4:753-760.
    • (2012) MAbs , vol.4 , pp. 753-760
    • Hotzel, I.1    Theil, F.P.2    Bernstein, L.J.3
  • 89
    • 0029927482 scopus 로고    scopus 로고
    • Abnormally short serum half-lives of IgG in beta 2-microglobulin-deficient mice
    • Ghetie V, Hubbard JG, Kim JK, et al. Abnormally short serum half-lives of IgG in beta 2-microglobulin-deficient mice. Eur J Immunol 1996; 26:690-696.
    • (1996) Eur J Immunol , vol.26 , pp. 690-696
    • Ghetie, V.1    Hubbard, J.G.2    Kim, J.K.3
  • 90
    • 0029856774 scopus 로고    scopus 로고
    • Increased clearance of IgG in mice that lack beta 2-microglobulin: Possible protective role of FcRn
    • Israel EJ, Wilsker DF, Hayes KC, et al. Increased clearance of IgG in mice that lack beta 2-microglobulin: possible protective role of FcRn. Immunology 1996; 89:573-578.
    • (1996) Immunology , vol.89 , pp. 573-578
    • Israel, E.J.1    Wilsker, D.F.2    Hayes, K.C.3
  • 91
    • 84907983318 scopus 로고    scopus 로고
    • Enhanced neonatal Fc receptor function improves protection against primate SHIV infection
    • Ko SY, Pegu A, Rudicell RS, et al. Enhanced neonatal Fc receptor function improves protection against primate SHIV infection. Nature 2014; 514:642-645.
    • (2014) Nature , vol.514 , pp. 642-645
    • Ko, S.Y.1    Pegu, A.2    Rudicell, R.S.3
  • 92
    • 34047143155 scopus 로고    scopus 로고
    • Development of motavizumab, an ultrapotent antibody for the prevention of respiratory syncytial virus infection in the upper and lower respiratory tract
    • Wu H, Pfarr DS, Johnson S, et al. Development of motavizumab, an ultrapotent antibody for the prevention of respiratory syncytial virus infection in the upper and lower respiratory tract. J Mol Biol 2007; 368:652-665.
    • (2007) J Mol Biol , vol.368 , pp. 652-665
    • Wu, H.1    Pfarr, D.S.2    Johnson, S.3
  • 93
    • 77951566536 scopus 로고    scopus 로고
    • Improving the solubility of anti-LINGO-1 monoclonal antibody Li33 by isotype switching and targeted mutagenesis
    • Pepinsky RB, Silvian L, Berkowitz SA, et al. Improving the solubility of anti-LINGO-1 monoclonal antibody Li33 by isotype switching and targeted mutagenesis. Protein Sci 2010; 19:954-966.
    • (2010) Protein Sci , vol.19 , pp. 954-966
    • Pepinsky, R.B.1    Silvian, L.2    Berkowitz, S.A.3
  • 94
    • 84928525428 scopus 로고    scopus 로고
    • Engineering antibodies to enhance activity and increase half-life
    • Sievers SA, Patel SN, Bennett K, et al. Engineering antibodies to enhance activity and increase half-life. AIDS Res Human Retroviruses 2014; 30:A210-A1210.
    • (2014) AIDS Res Human Retroviruses , vol.30 , pp. A210-A1210
    • Sievers, S.A.1    Patel, S.N.2    Bennett, K.3
  • 95
    • 67749111952 scopus 로고    scopus 로고
    • Design of therapeutic proteins with enhanced stability
    • Chennamsetty N, Voynov V, Kayser V, et al. Design of therapeutic proteins with enhanced stability. Proc Natl Acad Sci U S A 2009; 106:11937-11942.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 11937-11942
    • Chennamsetty, N.1    Voynov, V.2    Kayser, V.3
  • 96
    • 84867016746 scopus 로고    scopus 로고
    • Aggregationresistant domain antibodies engineered with charged mutations near the edges of the complementarity-determining regions
    • Perchiacca JM, Ladiwala AR, Bhattacharya M, Tessier PM. Aggregationresistant domain antibodies engineered with charged mutations near the edges of the complementarity-determining regions. Protein Eng Des Sel 2012; 25:591-601.
    • (2012) Protein Eng des Sel , vol.25 , pp. 591-601
    • Perchiacca, J.M.1    Ladiwala, A.R.2    Bhattacharya, M.3    Tessier, P.M.4
  • 97
    • 84892946282 scopus 로고    scopus 로고
    • Optimal charged mutations in the complementarity-determining regions that prevent domain antibody aggregation are dependent on the antibody scaffold
    • Perchiacca JM, Lee CC, Tessier PM. Optimal charged mutations in the complementarity-determining regions that prevent domain antibody aggregation are dependent on the antibody scaffold. Protein Eng Des Sel 2014; 27:29-39.
    • (2014) Protein Eng des Sel , vol.27 , pp. 29-39
    • Perchiacca, J.M.1    Lee, C.C.2    Tessier, P.M.3
  • 98
    • 84928546385 scopus 로고    scopus 로고
    • Enhancing the solubility of HIV-1-neutralizing Antibody 10E8
    • Kwon YD, Georgiev IS, Zhang B, et al. Enhancing the solubility of HIV-1-neutralizing Antibody 10E8. AIDS Res Human Retroviruses 2014; 30:A150-A1150.
    • (2014) AIDS Res Human Retroviruses , vol.30 , pp. A150-A1150
    • Kwon, Y.D.1    Georgiev, I.S.2    Zhang, B.3
  • 99
    • 84918544609 scopus 로고    scopus 로고
    • Dramatic potentiation of the antiviral activity of HIV antibodies by cholesterol conjugation
    • Lacek K, Urbanowicz RA, Troise F, et al. Dramatic potentiation of the antiviral activity of HIV antibodies by cholesterol conjugation. J Biol Chem 2014; 289:35015-35028.
    • (2014) J Biol Chem , vol.289 , pp. 35015-35028
    • Lacek, K.1    Urbanowicz, R.A.2    Troise, F.3
  • 100
    • 84876326554 scopus 로고    scopus 로고
    • Antibody conjugation approach enhances breadth and potency of neutralization of anti-HIV-1 antibodies and CD4-IgG
    • Gavrilyuk J, Ban H, Uehara H, et al. Antibody conjugation approach enhances breadth and potency of neutralization of anti-HIV-1 antibodies and CD4-IgG. J Virol 2013; 87:4985-4993.
    • (2013) J Virol , vol.87 , pp. 4985-4993
    • Gavrilyuk, J.1    Ban, H.2    Uehara, H.3
  • 101
    • 0037372301 scopus 로고    scopus 로고
    • Neutralization of human immunodeficiency virus type 1 by sCD4-17b, a single-chain chimeric protein, based on sequential interaction of gp120 with CD4 and coreceptor
    • Dey B, Del Castillo CS, Berger EA. Neutralization of human immunodeficiency virus type 1 by sCD4-17b, a single-chain chimeric protein, based on sequential interaction of gp120 with CD4 and coreceptor. J Virol 2003; 77:2859-2865.
    • (2003) J Virol , vol.77 , pp. 2859-2865
    • Dey, B.1    Del Castillo, C.S.2    Berger, E.A.3
  • 102
    • 84928565675 scopus 로고    scopus 로고
    • Towards a functional cure of HIV Infection using a novel CD4-based chimeric antigen receptor
    • Dey B, Liu L, Patel B, et al. Towards a functional cure of HIV Infection using a novel CD4-based chimeric antigen receptor. J Antivir Antiretrovir 2014; 6:72.
    • (2014) J Antivir Antiretrovir , vol.6 , pp. 72
    • Dey, B.1    Liu, L.2    Patel, B.3
  • 103
    • 72849116535 scopus 로고    scopus 로고
    • Evaluation of CD4-CD4i antibody architectures yields potent, broadly cross-reactive antihuman immunodeficiency virus reagents
    • West AP Jr, Galimidi RP, Foglesong CP, et al. Evaluation of CD4-CD4i antibody architectures yields potent, broadly cross-reactive antihuman immunodeficiency virus reagents. J Virol 2010; 84:261-269.
    • (2010) J Virol , vol.84 , pp. 261-269
    • West, A.P.1    Galimidi, R.P.2    Foglesong, C.P.3
  • 104
    • 0029062687 scopus 로고
    • Expression and characterization of CD4-IgG2, a novel heterotetramer that neutralizes primary HIV type 1 isolates
    • Allaway GP, Davis-Bruno KL, Beaudry GA, et al. Expression and characterization of CD4-IgG2, a novel heterotetramer that neutralizes primary HIV type 1 isolates. AIDS Res Hum Retroviruses 1995; 11:533-539.
    • (1995) AIDS Res Hum Retroviruses , vol.11 , pp. 533-539
    • Allaway, G.P.1    Davis-Bruno, K.L.2    Beaudry, G.A.3
  • 105
    • 84891697346 scopus 로고    scopus 로고
    • Exceptionally potent and broadly crossreactive, bispecific multivalent HIV-1 inhibitors based on single human CD4 and antibody domains
    • ChenW, Feng Y, Prabakaran P, et al. Exceptionally potent and broadly crossreactive, bispecific multivalent HIV-1 inhibitors based on single human CD4 and antibody domains. J Virol 2014; 88:1125-1139.
    • (2014) J Virol , vol.88 , pp. 1125-1139
    • Chen, W.1    Feng, Y.2    Prabakaran, P.3
  • 106
    • 55949131238 scopus 로고    scopus 로고
    • Humandomain antibodies to conserved sterically restricted regions on gp120 as exceptionally potent cross-reactive HIV-1 neutralizers
    • Chen W, Zhu Z, Feng Y, Dimitrov DS. Humandomain antibodies to conserved sterically restricted regions on gp120 as exceptionally potent cross-reactive HIV-1 neutralizers. Proc Natl Acad Sci U S A 2008; 105:17121-17126.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 17121-17126
    • Chen, W.1    Zhu, Z.2    Feng, Y.3    Dimitrov, D.S.4
  • 107
    • 79960592856 scopus 로고    scopus 로고
    • Immunoglobulin domain crossover as a generic approach for the production of bispecific IgG antibodies
    • Schaefer W, Regula JT, Bahner M, et al. Immunoglobulin domain crossover as a generic approach for the production of bispecific IgG antibodies. Proc Natl Acad Sci U S A 2011; 108:11187-11192.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 11187-11192
    • Schaefer, W.1    Regula, J.T.2    Bahner, M.3
  • 108
    • 84867136866 scopus 로고    scopus 로고
    • Anti-HIV double variable domain immunoglobulins binding both gp41 and gp120 for targeted delivery of immunoconjugates
    • Craig RB, Summa CM, Corti M, Pincus SH. Anti-HIV double variable domain immunoglobulins binding both gp41 and gp120 for targeted delivery of immunoconjugates. PLoS One 2012; 7:e46778.
    • (2012) PLoS One , vol.7 , pp. e46778
    • Craig, R.B.1    Summa, C.M.2    Corti, M.3    Pincus, S.H.4
  • 109
    • 84894552045 scopus 로고    scopus 로고
    • A double-mimetic peptide efficiently neutralizes HIV-1 by bridging the CD4-and coreceptor-binding sites of gp120
    • Quinlan BD, Joshi VR, Gardner MR, et al. A double-mimetic peptide efficiently neutralizes HIV-1 by bridging the CD4-and coreceptor-binding sites of gp120. J Virol 2014; 88:3353-3358.
    • (2014) J Virol , vol.88 , pp. 3353-3358
    • Quinlan, B.D.1    Joshi, V.R.2    Gardner, M.R.3
  • 110
    • 84882404868 scopus 로고    scopus 로고
    • Bispecific antibodies directed to CD4 domain 2 and HIV envelope exhibit exceptional breadth and picomolar potency against HIV-1
    • Pace CS, Song R, Ochsenbauer C, et al. Bispecific antibodies directed to CD4 domain 2 and HIV envelope exhibit exceptional breadth and picomolar potency against HIV-1. Proc Natl Acad Sci U S A 2013; 110:13540-13545.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 13540-13545
    • Pace, C.S.1    Song, R.2    Ochsenbauer, C.3
  • 111
    • 84904463520 scopus 로고    scopus 로고
    • Rational design and characterization of the novel, broad and potent bispecific HIV-1 neutralizing antibody iMabm36
    • Sun M, Pace CS, Yao X, et al. Rational design and characterization of the novel, broad and potent bispecific HIV-1 neutralizing antibody iMabm36. J Acquir Immune Defic Syndr 2014; 66:473-483.
    • (2014) J Acquir Immune Defic Syndr , vol.66 , pp. 473-483
    • Sun, M.1    Pace, C.S.2    Yao, X.3
  • 112
    • 84898540554 scopus 로고    scopus 로고
    • Adeno-associated virus delivery of broadly neutralizing antibodies
    • Schnepp BC, Johnson PR. Adeno-associated virus delivery of broadly neutralizing antibodies. Curr Opin HIV AIDS 2014; 9:250-256.
    • (2014) Curr Opin HIV AIDS , vol.9 , pp. 250-256
    • Schnepp, B.C.1    Johnson, P.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.