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Volumn 107, Issue 25, 2010, Pages 11483-11488

Structure and function of broadly reactive antibody PG16 reveal an H3 subdomain that mediates potent neutralization of HIV-1

Author keywords

Env; gp120; Neutralizing antibody; PG9; Sulfotyrosine

Indexed keywords

ENVELOPE PROTEIN; GLYCAN; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY PG16; MONOCLONAL ANTIBODY PG19; TYROSINE; UNCLASSIFIED DRUG; ANTIGEN; DRUG DERIVATIVE; GLYCOPROTEIN GP 120; NEUTRALIZING ANTIBODY; TYROSINE O-SULFATE; TYROSINE SULFATE;

EID: 77954912140     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1004600107     Document Type: Article
Times cited : (173)

References (49)
  • 1
    • 19144365910 scopus 로고    scopus 로고
    • Immunization with envelope subunit vaccine products elicits neutralizing antibodies against laboratory-adapted but not primary isolates of human immunodeficiency virus type 1
    • The National Institute of Allergy and Infectious Diseases AIDS Vaccine Evaluation Group
    • Mascola JR, et al; The National Institute of Allergy and Infectious Diseases AIDS Vaccine Evaluation Group (1996) Immunization with envelope subunit vaccine products elicits neutralizing antibodies against laboratory-adapted but not primary isolates of human immunodeficiency virus type 1. J Infect Dis 173:340-348.
    • (1996) J Infect Dis , vol.173 , pp. 340-348
    • Mascola, J.R.1
  • 2
    • 13944254982 scopus 로고    scopus 로고
    • Placebo-controlled phase 3 trial of a recombinant glycoprotein 120 vaccine to prevent HIV-1 infection
    • rgp120 HIV Vaccine Study Group
    • Flynn NM, et al.; rgp120 HIV Vaccine Study Group (2005) Placebo-controlled phase 3 trial of a recombinant glycoprotein 120 vaccine to prevent HIV-1 infection. J Infect Dis 191:654-665.
    • (2005) J Infect Dis , vol.191 , pp. 654-665
    • Flynn, N.M.1
  • 4
    • 0028917784 scopus 로고
    • Primary isolates of human immunodeficiency virus type 1 are relatively resistant to neutralization by monoclonal antibodies to gp120, and their neutralization is not predicted by studies with monomeric gp120
    • Moore JP, et al. (1995) Primary isolates of human immunodeficiency virus type 1 are relatively resistant to neutralization by monoclonal antibodies to gp120, and their neutralization is not predicted by studies with monomeric gp120. J Virol 69:101-109. (Pubitemid 24378783)
    • (1995) Journal of Virology , vol.69 , Issue.1 , pp. 101-109
    • Moore, J.P.1    Cao, Y.2    Qing, L.3    Sattentau, Q.J.4    Pyati, J.5    Koduri, R.6    Robinson, J.7    Barbas III, C.F.8    Burton, D.R.9    Ho, D.D.10
  • 5
    • 33845433434 scopus 로고    scopus 로고
    • Randomized, double-blind, placebo-controlled efficacy trial of a bivalent recombinant glycoprotein 120 HIV-1 vaccine among injection drug users in Bangkok, Thailand
    • Bangkok Vaccine Evaluation Group
    • Pitisuttithum P, et al.; Bangkok Vaccine Evaluation Group (2006) Randomized, double-blind, placebo-controlled efficacy trial of a bivalent recombinant glycoprotein 120 HIV-1 vaccine among injection drug users in Bangkok, Thailand. J Infect Dis 194: 1661-1671.
    • (2006) J Infect Dis , vol.194 , pp. 1661-1671
    • Pitisuttithum, P.1
  • 6
    • 33846172297 scopus 로고    scopus 로고
    • Rational modifications of HIV-1 envelope glycoproteins for immunogen design
    • DOI 10.2174/138161207779313632
    • Phogat S, Wyatt R (2007) Rational modifications of HIV-1 envelope glycoproteins for immunogen design. Curr Pharm Des 13:213-227. (Pubitemid 46085294)
    • (2007) Current Pharmaceutical Design , vol.13 , Issue.2 , pp. 213-227
    • Phogat, S.1    Wyatt, R.2
  • 7
    • 40849136223 scopus 로고    scopus 로고
    • The membrane-proximal external region of the human immunodeficiency virus type 1 envelope: Dominant site of antibody neutralization and target for vaccine design
    • DOI 10.1128/MMBR.00020-07
    • Montero M, van Houten NE, Wang X, Scott JK (2008) The membrane-proximal external region of the human immunodeficiency virus type 1 envelope: Dominant site of antibody neutralization and target for vaccine design. Microbiol Mol Biol Rev 72: 54-84. (Pubitemid 351398055)
    • (2008) Microbiology and Molecular Biology Reviews , vol.72 , Issue.1 , pp. 54-84
    • Montero, M.1    Van Houten, N.E.2    Wang, X.3    Scott, J.K.4
  • 8
    • 34247636624 scopus 로고    scopus 로고
    • Exploiting the defensive sugars of HIV-1 for drug and vaccine design
    • DOI 10.1038/nature05818, PII NATURE05818
    • Scanlan CN, Offer J, Zitzmann N, Dwek RA (2007) Exploiting the defensive sugars of HIV-1 for drug and vaccine design. Nature 446:1038-1045. (Pubitemid 46676066)
    • (2007) Nature , vol.446 , Issue.7139 , pp. 1038-1045
    • Scanlan, C.N.1    Offer, J.2    Zitzmann, N.3    Dwek, R.A.4
  • 9
    • 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, et al. (2010) Analysis of memory B cell responses and isolation of novel monoclonal antibodies with neutralizing breadth from HIV-1-infected individuals. PLoS ONE 5:e8805.
    • (2010) PLoS ONE , vol.5
    • Corti, D.1
  • 10
    • 58149517700 scopus 로고    scopus 로고
    • Analysis of neutralization specificities in polyclonal sera derived from human immunodeficiency virus type 1-infected individuals
    • Li Y, et al. (2009) Analysis of neutralization specificities in polyclonal sera derived from human immunodeficiency virus type 1-infected individuals. J Virol 83: 1045-1059.
    • (2009) J Virol , vol.83 , pp. 1045-1059
    • Li, Y.1
  • 11
    • 58149487645 scopus 로고    scopus 로고
    • Factors associated with the development of cross-reactive neutralizing antibodies during human immunodeficiency virus type 1 infection
    • Sather DN, et al. (2009) Factors associated with the development of cross-reactive neutralizing antibodies during human immunodeficiency virus type 1 infection. J Virol 83:757-769.
    • (2009) J Virol , vol.83 , pp. 757-769
    • Sather, D.N.1
  • 12
    • 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 JM, et al. (2008) 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 82:11651-11668.
    • (2008) J Virol , vol.82 , pp. 11651-11668
    • Binley, J.M.1
  • 13
    • 70350320582 scopus 로고    scopus 로고
    • Broad neutralization of human immunodeficiency virus type 1 mediated by plasma antibodies against the gp41 membrane proximal external region
    • Gray ES, et al. (2009) Broad neutralization of human immunodeficiency virus type 1 mediated by plasma antibodies against the gp41 membrane proximal external region. J Virol 83:11265-11274.
    • (2009) J Virol , vol.83 , pp. 11265-11274
    • Gray, E.S.1
  • 14
    • 34249950588 scopus 로고    scopus 로고
    • Dissecting the neutralizing antibody specificities of broadly neutralizing sera from human immunodeficiency virus type 1-infected donors
    • Dhillon AK, et al. (2007) Dissecting the neutralizing antibody specificities of broadly neutralizing sera from human immunodeficiency virus type 1-infected donors. J Virol 81:6548-6562.
    • (2007) J Virol , vol.81 , pp. 6548-6562
    • Dhillon, A.K.1
  • 16
    • 0027985431 scopus 로고
    • Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody
    • Burton DR, et al. (1994) Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody. Science 266:1024-1027.
    • (1994) Science , vol.266 , pp. 1024-1027
    • Burton, D.R.1
  • 17
    • 0028593629 scopus 로고
    • A broadly neutralizing human monoclonal antibody against gp41 of human immunodeficiency virus type 1
    • Purtscher M, et al. (1994) A broadly neutralizing human monoclonal antibody against gp41 of human immunodeficiency virus type 1. AIDS Res Hum Retroviruses 10: 1651-1658.
    • (1994) AIDS Res Hum Retroviruses , vol.10 , pp. 1651-1658
    • Purtscher, M.1
  • 20
    • 70349887757 scopus 로고    scopus 로고
    • Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target
    • (2009) Protocol G Principal Investigators
    • Walker LM, et al. (2009) Protocol G Principal Investigators (2009) Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 326:285-289.
    • (2009) Science , vol.326 , pp. 285-289
    • Walker, L.M.1
  • 22
    • 0032947286 scopus 로고    scopus 로고
    • Protection of macaques against pathogenic simian/human immunodeficiency virus 89.6PD by passive transfer of neutralizing antibodies
    • Mascola JR, et al. (1999) Protection of macaques against pathogenic simian/human immunodeficiency virus 89.6PD by passive transfer of neutralizing antibodies. J Virol 73:4009-4018.
    • (1999) J Virol , vol.73 , pp. 4009-4018
    • Mascola, J.R.1
  • 23
    • 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, et al. (2000) Protection of macaques against vaginal transmission of a pathogenic HIV-1/SIV chimeric virus by passive infusion of neutralizing antibodies. Nat Med 6:207-210.
    • (2000) Nat Med , vol.6 , pp. 207-210
    • Mascola, J.R.1
  • 24
    • 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 PW, et al. (2001) Antibody protects macaques against vaginal challenge with a pathogenic R5 simian/human immunodeficiency virus at serum levels giving complete neutralization in vitro. J Virol 75:8340-8347.
    • (2001) J Virol , vol.75 , pp. 8340-8347
    • Parren, P.W.1
  • 26
    • 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 AJ, et al. (2009) Broadly neutralizing human anti-HIV antibody 2G12 is effective in protection against mucosal SHIV challenge even at low serum neutralizing titers. PLoS Pathog 5:e1000433.
    • (2009) PLoS Pathog , vol.5
    • Hessell, A.J.1
  • 27
    • 73949154006 scopus 로고    scopus 로고
    • Broadly neutralizing monoclonal antibodies 2F5 and 4E10 directed against the human immunodeficiency virus type 1 gp41 membrane-proximal external region protect against mucosal challenge by simian-human immunodeficiency virus SHIVBa-L
    • Hessell AJ, et al. (2010) Broadly neutralizing monoclonal antibodies 2F5 and 4E10 directed against the human immunodeficiency virus type 1 gp41 membrane-proximal external region protect against mucosal challenge by simian-human immunodeficiency virus SHIVBa-L. J Virol 84:1302-1313.
    • (2010) J Virol , vol.84 , pp. 1302-1313
    • Hessell, A.J.1
  • 28
    • 12444291017 scopus 로고    scopus 로고
    • Antibody domain exchange is an immunological solution to carbohydrate cluster recognition
    • Calarese DA, et al. (2003) Antibody domain exchange is an immunological solution to carbohydrate cluster recognition. Science 300:2065-2071.
    • (2003) Science , vol.300 , pp. 2065-2071
    • Calarese, D.A.1
  • 29
    • 13844255333 scopus 로고    scopus 로고
    • Broadly neutralizing anti-HIV antibody 4E10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41
    • Cardoso RM, et al. (2005) Broadly neutralizing anti-HIV antibody 4E10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41. Immunity 22:163-173.
    • (2005) Immunity , vol.22 , pp. 163-173
    • Cardoso, R.M.1
  • 30
    • 54849416088 scopus 로고    scopus 로고
    • Structural details of HIV-1 recognition by the broadly neutralizing monoclonal antibody 2F5: Epitope conformation, antigen-recognition loop mobility, and anion-binding site
    • Julien JP, Bryson S, Nieva JL, Pai EF (2008) Structural details of HIV-1 recognition by the broadly neutralizing monoclonal antibody 2F5: Epitope conformation, antigen-recognition loop mobility, and anion-binding site. J Mol Biol 384:377-392.
    • (2008) J Mol Biol , vol.384 , pp. 377-392
    • Julien, J.P.1    Bryson, S.2    Nieva, J.L.3    Pai, E.F.4
  • 31
    • 65749107719 scopus 로고    scopus 로고
    • HIV-1 and influenza antibodies: Seeing antigens in new ways
    • Kwong PD, Wilson IA (2009) HIV-1 and influenza antibodies: Seeing antigens in new ways. Nat Immunol 10:573-578.
    • (2009) Nat Immunol , vol.10 , pp. 573-578
    • Kwong, P.D.1    Wilson, I.A.2
  • 33
    • 4544379899 scopus 로고    scopus 로고
    • Structure and mechanistic analysis of the anti-human immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope
    • Ofek G, et al. (2004) Structure and mechanistic analysis of the anti-human immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope. J Virol 78: 10724-10737.
    • (2004) J Virol , vol.78 , pp. 10724-10737
    • Ofek, G.1
  • 34
    • 69249220320 scopus 로고    scopus 로고
    • A conformational switch in human immunodeficiency virus gp41 revealed by the structures of overlapping epitopes recognized by neutralizing antibodies
    • Pejchal R, et al. (2009) A conformational switch in human immunodeficiency virus gp41 revealed by the structures of overlapping epitopes recognized by neutralizing antibodies. J Virol 83:8451-8462.
    • (2009) J Virol , vol.83 , pp. 8451-8462
    • Pejchal, R.1
  • 35
    • 17944380435 scopus 로고    scopus 로고
    • Crystal structure of a neutralizing human IGG against HIV-1: A template for vaccine design
    • Saphire EO, et al. (2001) Crystal structure of a neutralizing human IGG against HIV-1: A template for vaccine design. Science 293:1155-1159.
    • (2001) Science , vol.293 , pp. 1155-1159
    • Saphire, E.O.1
  • 36
    • 33847101745 scopus 로고    scopus 로고
    • Structural definition of a conserved neutralization epitope on HIV-1 gp120
    • Zhou T, et al. (2007) Structural definition of a conserved neutralization epitope on HIV-1 gp120. Nature 445:732-737.
    • (2007) Nature , vol.445 , pp. 732-737
    • Zhou, T.1
  • 37
  • 38
    • 33645049294 scopus 로고    scopus 로고
    • Antibody elbow angles are influenced by their light chain class
    • Stanfield RL, Zemla A,Wilson IA, Rupp B (2006) Antibody elbow angles are influenced by their light chain class. J Mol Biol 357:1566-1574.
    • (2006) J Mol Biol , vol.357 , pp. 1566-1574
    • Stanfield, R.L.1    Zemla, A.2    Wilson, I.A.3    Rupp, B.4
  • 39
    • 0031558798 scopus 로고    scopus 로고
    • Standard conformations for the canonical structures of immunoglobulins
    • Al-Lazikani B, Lesk AM, Chothia C (1997) Standard conformations for the canonical structures of immunoglobulins. J Mol Biol 273:927-948.
    • (1997) J Mol Biol , vol.273 , pp. 927-948
    • Al-Lazikani, B.1    Lesk, A.M.2    Chothia, C.3
  • 40
    • 34848868199 scopus 로고    scopus 로고
    • Structures of the CCR5 N terminus and of a tyrosine-sulfated antibody with HIV-1 gp120 and CD4
    • Huang CC, et al. (2007) Structures of the CCR5 N terminus and of a tyrosine-sulfated antibody with HIV-1 gp120 and CD4. Science 317:1930-1934.
    • (2007) Science , vol.317 , pp. 1930-1934
    • Huang, C.C.1
  • 41
    • 65549114651 scopus 로고    scopus 로고
    • Efficient recovery of high-affinity antibodies from a single-chain Fab yeast display library
    • Walker LM, Bowley DR, Burton DR (2009) Efficient recovery of high-affinity antibodies from a single-chain Fab yeast display library. J Mol Biol 389:365-375.
    • (2009) J Mol Biol , vol.389 , pp. 365-375
    • Walker, L.M.1    Bowley, D.R.2    Burton, D.R.3
  • 42
    • 0042855800 scopus 로고    scopus 로고
    • Tyrosine sulfation of human antibodies contributes to recognition of the CCR5 binding region of HIV-1 gp120
    • Choe H, et al. (2003) Tyrosine sulfation of human antibodies contributes to recognition of the CCR5 binding region of HIV-1 gp120. Cell 114:161-170.
    • (2003) Cell , vol.114 , pp. 161-170
    • Choe, H.1
  • 43
    • 12144290520 scopus 로고    scopus 로고
    • Structural basis of tyrosine sulfation and VH-gene usage in antibodies that recognize the HIV type 1 coreceptor-binding site on gp120
    • Huang CC, et al. (2004) Structural basis of tyrosine sulfation and VH-gene usage in antibodies that recognize the HIV type 1 coreceptor-binding site on gp120. Proc Natl Acad Sci USA 101:2706-2711.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2706-2711
    • Huang, C.C.1
  • 44
    • 67349111690 scopus 로고    scopus 로고
    • Tyrosine sulfation: An increasingly recognised post-translational modification of secreted proteins
    • Stone MJ, Chuang S, Hou X, Shoham M, Zhu JZ (2009) Tyrosine sulfation: An increasingly recognised post-translational modification of secreted proteins. N Biotechnol 25:299-317.
    • (2009) N Biotechnol , vol.25 , pp. 299-317
    • Stone, M.J.1    Chuang, S.2    Hou, X.3    Shoham, M.4    Zhu, J.Z.5
  • 45
    • 77949401834 scopus 로고    scopus 로고
    • A V3 loop-dependent gp120 element disrupted by CD4 binding stabilizes the human immunodeficiency virus (HIV-1) envelope glycoprotein trimer
    • Xiang SH, et al. (2010) A V3 loop-dependent gp120 element disrupted by CD4 binding stabilizes the human immunodeficiency virus (HIV-1) envelope glycoprotein trimer. J Virol 84:3147-3161.
    • (2010) J Virol , vol.84 , pp. 3147-3161
    • Xiang, S.H.1
  • 46
    • 77749329921 scopus 로고    scopus 로고
    • Topological layers in the HIV-1 gp120 inner domain regulate gp41 interaction and CD4-triggered conformational transitions
    • Finzi A, et al. (2010) Topological layers in the HIV-1 gp120 inner domain regulate gp41 interaction and CD4-triggered conformational transitions. Mol Cell 37:656-667.
    • (2010) Mol Cell , vol.37 , pp. 656-667
    • Finzi, A.1
  • 47
    • 75749133275 scopus 로고    scopus 로고
    • Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility
    • Pancera M, et al. (2010) Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility. Proc Natl Acad Sci USA 107:1166-1171.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 1166-1171
    • Pancera, M.1
  • 48
    • 67650453747 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 elite neutralizers: Individuals with broad and potent neutralizing activity identified by using a high-throughput neutralization assay together with an analytical selection algorithm
    • Simek MD, et al. (2009) Human immunodeficiency virus type 1 elite neutralizers: Individuals with broad and potent neutralizing activity identified by using a high-throughput neutralization assay together with an analytical selection algorithm. J Virol 83:7337-7348.
    • (2009) J Virol , vol.83 , pp. 7337-7348
    • Simek, M.D.1
  • 49
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • Reeves PJ, Callewaert N, Contreras R, Khorana HG (2002) Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N- acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. Proc Natl Acad Sci USA 99:13419-13424.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4


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