메뉴 건너뛰기




Volumn 165, Issue 7, 2016, Pages 1609-1620

Bispecific Anti-HIV-1 Antibodies with Enhanced Breadth and Potency

Author keywords

[No Author keywords available]

Indexed keywords

ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; ANTIBODY; BISPECIFIC ANTIBODY; HUMAN IMMUNODEFICIENCY VIRUS 1 ANTIBODY; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN G1; IMMUNOGLOBULIN G1 ANTIBODY; IMMUNOGLOBULIN G3; IMMUNOGLOBULIN G3 ANTIBODY; NEUTRALIZING ANTIBODY; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN; VIRUS ENVELOPE PROTEIN ANTIBODY; EPITOPE; GLYCOPROTEIN GP 120; IMMUNOGLOBULIN G;

EID: 84975270914     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2016.04.050     Document Type: Article
Times cited : (125)

References (52)
  • 4
    • 84945295233 scopus 로고    scopus 로고
    • Fcγ receptor pathways during active and passive immunization
    • S. Bournazos, and J.V. Ravetch Fcγ receptor pathways during active and passive immunization Immunol. Rev. 268 2015 88 103
    • (2015) Immunol. Rev. , vol.268 , pp. 88-103
    • Bournazos, S.1    Ravetch, J.V.2
  • 5
    • 84908077691 scopus 로고    scopus 로고
    • Broadly neutralizing anti-HIV-1 antibodies require Fc effector functions for in vivo activity
    • S. Bournazos, F. Klein, J. Pietzsch, M.S. Seaman, M.C. Nussenzweig, and J.V. Ravetch 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
  • 6
    • 84956963019 scopus 로고    scopus 로고
    • The role of Fc-FcγR interactions in IgG-mediated microbial neutralization
    • S. Bournazos, D.J. DiLillo, and J.V. Ravetch The role of Fc-FcγR interactions in IgG-mediated microbial neutralization J. Exp. Med. 212 2015 1361 1369
    • (2015) J. Exp. Med. , vol.212 , pp. 1361-1369
    • Bournazos, S.1    DiLillo, D.J.2    Ravetch, J.V.3
  • 7
    • 84929896699 scopus 로고    scopus 로고
    • Antibody responses to envelope glycoproteins in HIV-1 infection
    • D.R. Burton, and J.R. Mascola 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
  • 9
    • 77951523463 scopus 로고    scopus 로고
    • Bispecific antibodies for cancer therapy: The light at the end of the tunnel?
    • P. Chames, and D. Baty Bispecific antibodies for cancer therapy: the light at the end of the tunnel? MAbs 1 2009 539 547
    • (2009) MAbs , vol.1 , pp. 539-547
    • Chames, P.1    Baty, D.2
  • 19
    • 84878519611 scopus 로고    scopus 로고
    • Broadly neutralizing antibody PGT121 allosterically modulates CD4 binding via recognition of the HIV-1 gp120 V3 base and multiple surrounding glycans
    • J.P. Julien, D. Sok, R. Khayat, J.H. Lee, K.J. Doores, L.M. Walker, A. Ramos, D.C. Diwanji, R. Pejchal, A. Cupo, and et al. Broadly neutralizing antibody PGT121 allosterically modulates CD4 binding via recognition of the HIV-1 gp120 V3 base and multiple surrounding glycans PLoS Pathog. 9 2013 e1003342
    • (2013) PLoS Pathog. , vol.9 , pp. e1003342
    • Julien, J.P.1    Sok, D.2    Khayat, R.3    Lee, J.H.4    Doores, K.J.5    Walker, L.M.6    Ramos, A.7    Diwanji, D.C.8    Pejchal, R.9    Cupo, A.10
  • 20
    • 77954042425 scopus 로고    scopus 로고
    • Few and far between: How HIV may be evading antibody avidity
    • J.S. Klein, and P.J. Bjorkman Few and far between: how HIV may be evading antibody avidity PLoS Pathog. 6 2010 e1000908
    • (2010) PLoS Pathog. , vol.6 , pp. e1000908
    • Klein, J.S.1    Bjorkman, P.J.2
  • 21
    • 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
    • J.S. Klein, P.N. Gnanapragasam, R.P. Galimidi, C.P. Foglesong, A.P. West Jr., and P.J. Bjorkman Examination of the contributions of size and avidity to the neutralization mechanisms of the anti-HIV antibodies b12 and 4E10 Proc. Natl. Acad. Sci. USA 106 2009 7385 7390
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 7385-7390
    • Klein, J.S.1    Gnanapragasam, P.N.2    Galimidi, R.P.3    Foglesong, C.P.4    West, A.P.5    Bjorkman, P.J.6
  • 22
    • 84866443327 scopus 로고    scopus 로고
    • Broad neutralization by a combination of antibodies recognizing the CD4 binding site and a new conformational epitope on the HIV-1 envelope protein
    • F. Klein, C. Gaebler, H. Mouquet, D.N. Sather, C. Lehmann, J.F. Scheid, Z. Kraft, Y. Liu, J. Pietzsch, A. Hurley, and et al. Broad neutralization by a combination of antibodies recognizing the CD4 binding site and a new conformational epitope on the HIV-1 envelope protein J. Exp. Med. 209 2012 1469 1479
    • (2012) J. Exp. Med. , vol.209 , pp. 1469-1479
    • Klein, F.1    Gaebler, C.2    Mouquet, H.3    Sather, D.N.4    Lehmann, C.5    Scheid, J.F.6    Kraft, Z.7    Liu, Y.8    Pietzsch, J.9    Hurley, A.10
  • 26
    • 84922982202 scopus 로고    scopus 로고
    • Improving neutralization potency and breadth by combining broadly reactive HIV-1 antibodies targeting major neutralization epitopes
    • R. Kong, M.K. Louder, K. Wagh, R.T. Bailer, A. deCamp, K. Greene, H. Gao, J.D. Taft, A. Gazumyan, C. Liu, and et al. Improving neutralization potency and breadth by combining broadly reactive HIV-1 antibodies targeting major neutralization epitopes J. Virol. 89 2015 2659 2671
    • (2015) J. Virol. , vol.89 , pp. 2659-2671
    • Kong, R.1    Louder, M.K.2    Wagh, K.3    Bailer, R.T.4    DeCamp, A.5    Greene, K.6    Gao, H.7    Taft, J.D.8    Gazumyan, A.9    Liu, C.10
  • 31
    • 45849125030 scopus 로고    scopus 로고
    • Evaluating neutralizing antibodies against HIV, SIV, and SHIV in luciferase reporter gene assays
    • Unit 12.11
    • D.C. Montefiori Evaluating neutralizing antibodies against HIV, SIV, and SHIV in luciferase reporter gene assays Curr. Protoc. Immunol. 12 2005 Unit 12.11
    • (2005) Curr. Protoc. Immunol. , vol.12
    • Montefiori, D.C.1
  • 38
    • 0029946383 scopus 로고    scopus 로고
    • Knobs-into-holes engineering of antibody CH3 domains for heavy chain heterodimerization
    • J.B. Ridgway, L.G. Presta, and P. Carter 'Knobs-into-holes' engineering of antibody CH3 domains for heavy chain heterodimerization Protein Eng. 9 1996 617 621
    • (1996) Protein Eng. , vol.9 , pp. 617-621
    • Ridgway, J.B.1    Presta, L.G.2    Carter, P.3
  • 40
    • 0032532015 scopus 로고    scopus 로고
    • Comparisons of the ability of human IgG3 hinge mutants, IgM, IgE, and IgA2, to form small immune complexes: A role for flexibility and geometry
    • K.H. Roux, L. Strelets, O.H. Brekke, I. Sandlie, and T.E. Michaelsen Comparisons of the ability of human IgG3 hinge mutants, IgM, IgE, and IgA2, to form small immune complexes: a role for flexibility and geometry J. Immunol. 161 1998 4083 4090
    • (1998) J. Immunol. , vol.161 , pp. 4083-4090
    • Roux, K.H.1    Strelets, L.2    Brekke, O.H.3    Sandlie, I.4    Michaelsen, T.E.5
  • 42
    • 84941363719 scopus 로고    scopus 로고
    • Broadly neutralizing antibody 8ANC195 recognizes closed and open states of HIV-1 Env
    • L. Scharf, H. Wang, H. Gao, S. Chen, A.W. McDowall, and P.J. Bjorkman Broadly neutralizing antibody 8ANC195 recognizes closed and open states of HIV-1 Env Cell 162 2015 1379 1390
    • (2015) Cell , vol.162 , pp. 1379-1390
    • Scharf, L.1    Wang, H.2    Gao, H.3    Chen, S.4    McDowall, A.W.5    Bjorkman, P.J.6
  • 46
    • 84926348347 scopus 로고    scopus 로고
    • Alternative molecular formats and therapeutic applications for bispecific antibodies
    • C. Spiess, Q. Zhai, and P.J. Carter Alternative molecular formats and therapeutic applications for bispecific antibodies Mol. Immunol. 67 2 Pt A 2015 95 106
    • (2015) Mol. Immunol. , vol.67 , Issue.2 PT A , pp. 95-106
    • Spiess, C.1    Zhai, Q.2    Carter, P.J.3
  • 50
    • 84921606536 scopus 로고    scopus 로고
    • Insights into the trimeric HIV-1 envelope glycoprotein structure
    • A.B. Ward, and I.A. Wilson Insights into the trimeric HIV-1 envelope glycoprotein structure Trends Biochem. Sci. 40 2015 101 107
    • (2015) Trends Biochem. Sci. , vol.40 , pp. 101-107
    • Ward, A.B.1    Wilson, I.A.2
  • 51


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.