메뉴 건너뛰기




Volumn 6, Issue 236, 2014, Pages

Promiscuous glycan site recognition by antibodies to the high-mannose patch of gp120 broadens neutralization of HIV

Author keywords

[No Author keywords available]

Indexed keywords

BROADLY NEUTRALIZING MONOCLONAL ANTIBODY; EPITOPE; GLYCAN; GLYCOPROTEIN GP 120; MANNOSE; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; UNCLASSIFIED DRUG; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; IMMUNOGLOBULIN G; POLYSACCHARIDE;

EID: 84901236516     PISSN: 19466234     EISSN: 19466242     Source Type: Journal    
DOI: 10.1126/scitranslmed.3008104     Document Type: Article
Times cited : (155)

References (44)
  • 2
    • 69149083668 scopus 로고    scopus 로고
    • Neutralizing antibodies generated during natural HIV-1 infection: Good news for an HIV-1 vaccine?
    • L. Stamatatos, L. Morris, D. R. Burton, J. R. Mascola, Neutralizing antibodies generated during natural HIV-1 infection: Good news for an HIV-1 vaccine? Nat. Med. 15, 866-870 (2009).
    • (2009) Nat. Med. , vol.15 , pp. 866-870
    • Stamatatos, L.1    Morris, L.2    Burton, D.R.3    Mascola, J.R.4
  • 3
  • 13
    • 84866495323 scopus 로고    scopus 로고
    • Human antibodies that neutralize HIV-1: Identification, structures, and B cell ontogenies
    • P. D. Kwong, J. R. Mascola, Human antibodies that neutralize HIV-1: identification, structures, and B cell ontogenies. Immunity 37, 412-425 (2012).
    • (2012) Immunity , vol.37 , pp. 412-425
    • Kwong, P.D.1    Mascola, J.R.2
  • 14
    • 84875551472 scopus 로고    scopus 로고
    • Broadly neutralizing antiviral antibodies
    • D. Corti, A. Lanzavecchia, Broadly neutralizing antiviral antibodies. Annu. Rev. Immunol. 31, 705-742 (2013).
    • (2013) Annu. Rev. Immunol. , vol.31 , pp. 705-742
    • Corti, D.1    Lanzavecchia, A.2
  • 20
    • 45549101708 scopus 로고    scopus 로고
    • Glycosylation site-specific analysis of HIV envelope proteins (JR-FL and CON-S) reveals major differences in glycosylation site occupancy, glycoform profiles, and antigenic epitopes' accessibility
    • E. P. Go, J. Irungu, Y. Zhang, D. S. Dalpathado, H. X. Liao, L. L. Sutherland, S. M. Alam, B. F. Haynes, H. Desaire, Glycosylation site-specific analysis of HIV envelope proteins (JR-FL and CON-S) reveals major differences in glycosylation site occupancy, glycoform profiles, and antigenic epitopes' accessibility. J. Proteome Res. 7, 1660-1674 (2008).
    • (2008) J. Proteome Res. , vol.7 , pp. 1660-1674
    • Go, E.P.1    Irungu, J.2    Zhang, Y.3    Dalpathado, D.S.4    Liao, H.X.5    Sutherland, L.L.6    Alam, S.M.7    Haynes, B.F.8    Desaire, H.9
  • 21
    • 33646146379 scopus 로고    scopus 로고
    • GP120: Target for neutralizing HIV-1 antibodies
    • R. Pantophlet, D. R. Burton, GP120: Target for neutralizing HIV-1 antibodies. Annu. Rev. Immunol. 24, 739-769 (2006).
    • (2006) Annu. Rev. Immunol. , vol.24 , pp. 739-769
    • Pantophlet, R.1    Burton, D.R.2
  • 26
    • 0036637385 scopus 로고    scopus 로고
    • The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120
    • R. W. Sanders, M. Venturi, L. Schiffner, R. Kalyanaraman, H. Katinger, K. O. Lloyd, P. D. Kwong, J. P. Moore, The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120. J. Virol. 76, 7293-7305 (2002).
    • (2002) J. Virol. , vol.76 , pp. 7293-7305
    • Sanders, R.W.1    Venturi, M.2    Schiffner, L.3    Kalyanaraman, R.4    Katinger, H.5    Lloyd, K.O.6    Kwong, P.D.7    Moore, J.P.8
  • 28
    • 79955389756 scopus 로고    scopus 로고
    • The neutralization breadth of HIV-1 develops incrementally over four years and is associated with CD4+ T cell decline and high viral load during acute infection
    • CAPRISA002 Study Team
    • E. S. Gray, M. C. Madiga, T. Hermanus, P. L. Moore, C. K. Wibmer, N. L. Tumba, L. Werner, K.Mlisana, S. Sibeko, C. Williamson, S. S. Abdool Karim, L. Morris; CAPRISA002 Study Team, The neutralization breadth of HIV-1 develops incrementally over four years and is associated with CD4+ T cell decline and high viral load during acute infection. J. Virol. 85, 4828-4840 (2011).
    • (2011) J. Virol. , vol.85 , pp. 4828-4840
    • Gray, E.S.1    Madiga, M.C.2    Hermanus, T.3    Moore, P.L.4    Wibmer, C.K.5    Tumba, N.L.6    Werner, L.7    Mlisana, K.8    Sibeko, S.9    Williamson, C.10    Abdool Karim, S.S.11    Morris, L.12
  • 32
    • 77957201600 scopus 로고    scopus 로고
    • Very few substitutions in a germ line antibody are required to initiate significant domain exchange
    • M. Huber, K. M. Le, K. J. Doores, Z. Fulton, R. L. Stanfield, I. A. Wilson, D. R. Burton, Very few substitutions in a germ line antibody are required to initiate significant domain exchange. J. Virol. 84, 10700-10707 (2010).
    • (2010) J. Virol. , vol.84 , pp. 10700-10707
    • Huber, M.1    Le, K.M.2    Doores, K.J.3    Fulton, Z.4    Stanfield, R.L.5    Wilson, I.A.6    Burton, D.R.7
  • 40
    • 34247636624 scopus 로고    scopus 로고
    • Exploiting the defensive sugars of HIV-1 for drug and vaccine design
    • C. N. Scanlan, J. Offer, N. Zitzmann, R. A. Dwek, Exploiting the defensive sugars of HIV-1 for drug and vaccine design. Nature 446, 1038-1045 (2007).
    • (2007) Nature , vol.446 , pp. 1038-1045
    • Scanlan, C.N.1    Offer, J.2    Zitzmann, N.3    Dwek, R.A.4
  • 43
    • 1342327544 scopus 로고    scopus 로고
    • Statistical analysis of the protein environment of N-glycosylation sites: Implications for occupancy, structure, and folding
    • A. J. Petrescu, A. L. Milac, S. M. Petrescu, R. A. Dwek, M. R. Wormald, Statistical analysis of the protein environment of N-glycosylation sites: Implications for occupancy, structure, and folding. Glycobiology 14, 103-114 (2004).
    • (2004) Glycobiology , vol.14 , pp. 103-114
    • Petrescu, A.J.1    Milac, A.L.2    Petrescu, S.M.3    Dwek, R.A.4    Wormald, M.R.5
  • 44
    • 0036462598 scopus 로고    scopus 로고
    • Conformational studies of oligosaccharides and glycopeptides: Complementarity of NMR, X-ray crystallography, and molecular modelling
    • M. R. Wormald, A. J. Petrescu, Y. L. Pao, A. Glithero, T. Elliott, R. A. Dwek, Conformational studies of oligosaccharides and glycopeptides: Complementarity of NMR, X-ray crystallography, and molecular modelling. Chem. Rev. 102, 371-386 (2002).
    • (2002) Chem. Rev. , vol.102 , pp. 371-386
    • Wormald, M.R.1    Petrescu, A.J.2    Pao, Y.L.3    Glithero, A.4    Elliott, T.5    Dwek, R.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.