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Volumn 107, Issue 4, 2010, Pages 1529-1534

Aromatic residues at the edge of the antibody combining site facilitate viral glycoprotein recognition through membrane interactions

Author keywords

4E10; gp41; HIV; Neutralizing antibody; Tryptophan

Indexed keywords

LIPOSOME; NEUTRALIZING ANTIBODY; VIRUS GLYCOPROTEIN;

EID: 76549125090     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0909680107     Document Type: Article
Times cited : (97)

References (50)
  • 1
    • 0037405488 scopus 로고    scopus 로고
    • Defining the protective antibody response for HIV-1
    • Mascola JR (2003) Defining the protective antibody response for HIV-1. Curr Mol Med 3:209-216.
    • (2003) Curr Mol Med , vol.3 , pp. 209-216
    • Mascola, J.R.1
  • 2
    • 1542317452 scopus 로고    scopus 로고
    • HIV vaccine design and the neutralizing antibody problem
    • Burton DR, et al. (2004) HIV vaccine design and the neutralizing antibody problem. Nat Immunol 5:233-236.
    • (2004) Nat Immunol , vol.5 , pp. 233-236
    • Burton, D.R.1
  • 3
    • 70349887757 scopus 로고    scopus 로고
    • Walker LM, et al.; Protocol G Principal Investigators (2009) Broad and potent neutralizing antibodies froman African donor reveal a new HIV-1 vaccine target. Science 326:285-289.
    • Walker LM, et al.; Protocol G Principal Investigators (2009) Broad and potent neutralizing antibodies froman African donor reveal a new HIV-1 vaccine target. Science 326:285-289.
  • 4
    • 8644251891 scopus 로고    scopus 로고
    • Comprehensive cross-clade neutralization analysis of a panel of anti-human immunodeficiency virus type 1 monoclonal antibodies
    • Binley JM, et al. (2004) Comprehensive cross-clade neutralization analysis of a panel of anti-human immunodeficiency virus type 1 monoclonal antibodies. J Virol 78:13232-13252.
    • (2004) J Virol , vol.78 , pp. 13232-13252
    • Binley, J.M.1
  • 5
    • 10044280760 scopus 로고    scopus 로고
    • Neutralization profiles of newly transmitted human immunodeficiency virus type 1 by monoclonal antibodies 2G12, 2F5, and 4E10
    • Mehandru S, et al. (2004) Neutralization profiles of newly transmitted human immunodeficiency virus type 1 by monoclonal antibodies 2G12, 2F5, and 4E10. J Virol 78:14039-14042.
    • (2004) J Virol , vol.78 , pp. 14039-14042
    • Mehandru, S.1
  • 6
    • 0034759882 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41
    • Zwick MB, et al. (2001) Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41. J Virol 75:10892-10905.
    • (2001) J Virol , vol.75 , pp. 10892-10905
    • Zwick, M.B.1
  • 7
    • 34247106331 scopus 로고    scopus 로고
    • An affinity-enhanced neutralizing antibody against the membrane-proximal external region of human immunodeficiency virus type 1 gp41 recognizes an epitope between those of 2F5 and 4E10
    • Nelson JD, et al. (2007) An affinity-enhanced neutralizing antibody against the membrane-proximal external region of human immunodeficiency virus type 1 gp41 recognizes an epitope between those of 2F5 and 4E10. J Virol 81:4033-4043.
    • (2007) J Virol , vol.81 , pp. 4033-4043
    • Nelson, J.D.1
  • 8
    • 0027378573 scopus 로고
    • A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1
    • Muster T, et al. (1993) A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1. J Virol 67:6642-6647.
    • (1993) J Virol , vol.67 , pp. 6642-6647
    • Muster, T.1
  • 9
    • 11144227042 scopus 로고    scopus 로고
    • Anti-human immunodeficiency virus type 1 (HIV-1) antibodies 2F5 and 4E10 require surprisingly few crucial residues in the membrane-proximal external region of glycoprotein gp41 to neutralize HIV-1
    • Zwick MB, et al. (2005) Anti-human immunodeficiency virus type 1 (HIV-1) antibodies 2F5 and 4E10 require surprisingly few crucial residues in the membrane-proximal external region of glycoprotein gp41 to neutralize HIV-1. J Virol 79:1252-1261.
    • (2005) J Virol , vol.79 , pp. 1252-1261
    • Zwick, M.B.1
  • 10
    • 33845995027 scopus 로고    scopus 로고
    • Structural basis of enhanced binding of extended and helically constrained peptide epitopes of the broadly neutralizing HIV-1 antibody 4E10
    • Cardoso RM, et al. (2007) Structural basis of enhanced binding of extended and helically constrained peptide epitopes of the broadly neutralizing HIV-1 antibody 4E10. J Mol Biol 365:1533-1544.
    • (2007) J Mol Biol , vol.365 , pp. 1533-1544
    • Cardoso, R.M.1
  • 11
    • 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
  • 12
    • 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
  • 13
    • 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
  • 14
    • 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
  • 15
    • 27544481277 scopus 로고    scopus 로고
    • The membrane-proximal external region of HIV-1 gp41: A vaccine target worth exploring
    • Zwick MB (2005) The membrane-proximal external region of HIV-1 gp41: A vaccine target worth exploring. AIDS 19:1725-1737.
    • (2005) AIDS , vol.19 , pp. 1725-1737
    • Zwick, M.B.1
  • 16
    • 0032980413 scopus 로고    scopus 로고
    • A conserved tryptophan-rich motif in the membrane proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for Env-mediated fusion and virus infectivity
    • Salzwedel K, West JT, Hunter E (1999) A conserved tryptophan-rich motif in the membrane proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for Env-mediated fusion and virus infectivity. J Virol 73:2469-2480.
    • (1999) J Virol , vol.73 , pp. 2469-2480
    • Salzwedel, K.1    West, J.T.2    Hunter, E.3
  • 17
    • 0034284386 scopus 로고    scopus 로고
    • How proteins adapt to a membrane-water interface
    • Killian JA, von Heijne G (2000) How proteins adapt to a membrane-water interface. Trends Biochem Sci 25:429-434.
    • (2000) Trends Biochem Sci , vol.25 , pp. 429-434
    • Killian, J.A.1    von Heijne, G.2
  • 18
    • 0038418536 scopus 로고    scopus 로고
    • The pre-transmembrane region of the human immunodeficiency virus type-1 glycoprotein: A novel fusogenic sequence
    • Suárez T, Nir S, Goñi FM, Saéz-Cirión A, Nieva JL (2000) The pre-transmembrane region of the human immunodeficiency virus type-1 glycoprotein: A novel fusogenic sequence. FEBS Lett 477:145-149.
    • (2000) FEBS Lett , vol.477 , pp. 145-149
    • Suárez, T.1    Nir, S.2    Goñi, F.M.3    Saéz-Cirión, A.4    Nieva, J.L.5
  • 19
    • 0035859948 scopus 로고    scopus 로고
    • The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles
    • Schibli DJ, Montelaro RC, Vogel HJ (2001) The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles. Biochemistry 40:9570-9578.
    • (2001) Biochemistry , vol.40 , pp. 9570-9578
    • Schibli, D.J.1    Montelaro, R.C.2    Vogel, H.J.3
  • 20
    • 67049156802 scopus 로고    scopus 로고
    • Broadly neutralizing anti-HIV-1 antibodies disrupt a hinge-related function of gp41 at the membrane interface
    • Song L, et al. (2009) Broadly neutralizing anti-HIV-1 antibodies disrupt a hinge-related function of gp41 at the membrane interface. Proc Natl Acad Sci USA 106:9057-9062.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9057-9062
    • Song, L.1
  • 21
    • 37849000389 scopus 로고    scopus 로고
    • HIV-1 broadly neutralizing antibody extracts its epitope from a kinked gp41 ectodomain region on the viral membrane
    • Sun ZY, et al. (2008) HIV-1 broadly neutralizing antibody extracts its epitope from a kinked gp41 ectodomain region on the viral membrane. Immunity 28:52-63.
    • (2008) Immunity , vol.28 , pp. 52-63
    • Sun, Z.Y.1
  • 22
    • 0036121261 scopus 로고    scopus 로고
    • Solid-phase proteoliposomes containing human immunodeficiency virus envelope glycoproteins
    • Grundner C, Mirzabekov T, Sodroski J, Wyatt R (2002) Solid-phase proteoliposomes containing human immunodeficiency virus envelope glycoproteins. J Virol 76:3511-3521.
    • (2002) J Virol , vol.76 , pp. 3511-3521
    • Grundner, C.1    Mirzabekov, T.2    Sodroski, J.3    Wyatt, R.4
  • 23
    • 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, et al. (2007) 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 178:4424-4435.
    • (2007) J Immunol , vol.178 , pp. 4424-4435
    • Alam, S.M.1
  • 24
    • 50949104097 scopus 로고    scopus 로고
    • The broadly neutralizing anti-human immunodeficiency virus type 1 4E10 monoclonal antibody is better adapted to membrane-bound epitope recognition and blocking than 2F5
    • Huarte N, et al. (2008) The broadly neutralizing anti-human immunodeficiency virus type 1 4E10 monoclonal antibody is better adapted to membrane-bound epitope recognition and blocking than 2F5. J Virol 82:8986-8996.
    • (2008) J Virol , vol.82 , pp. 8986-8996
    • Huarte, N.1
  • 25
    • 21344434534 scopus 로고    scopus 로고
    • Cardiolipin polyspecific autoreactivity in two broadly neutralizing HIV-1 antibodies
    • Haynes BF, et al. (2005) Cardiolipin polyspecific autoreactivity in two broadly neutralizing HIV-1 antibodies. Science 308:1906-1908.
    • (2005) Science , vol.308 , pp. 1906-1908
    • Haynes, B.F.1
  • 27
    • 37349058177 scopus 로고    scopus 로고
    • Difficulties in eliciting broadly neutralizing anti-HIV antibodies are not explained by cardiolipin autoreactivity
    • Scherer EM, Zwick MB, Teyton L, Burton DR (2007) Difficulties in eliciting broadly neutralizing anti-HIV antibodies are not explained by cardiolipin autoreactivity. AIDS 21:2131-2139.
    • (2007) AIDS , vol.21 , pp. 2131-2139
    • Scherer, E.M.1    Zwick, M.B.2    Teyton, L.3    Burton, D.R.4
  • 28
    • 37349086800 scopus 로고    scopus 로고
    • Reassessment of autoreactivity of the broadly neutralizing HIV antibodies 4E10 and 2F5 and retrospective analysis of clinical safety data
    • Vcelar B, et al. (2007) Reassessment of autoreactivity of the broadly neutralizing HIV antibodies 4E10 and 2F5 and retrospective analysis of clinical safety data. AIDS 21:2161-2170.
    • (2007) AIDS , vol.21 , pp. 2161-2170
    • Vcelar, B.1
  • 29
    • 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 (2009) Lipid binding properties of 4E10, 2F5, and WR304 monoclonal antibodies that neutralize HIV-1. Biochim Biophys Acta 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
  • 30
    • 0033711628 scopus 로고    scopus 로고
    • Diversity in the CDR3 region of V(H) is sufficient for most antibody specificities
    • Xu JL, Davis MM (2000) Diversity in the CDR3 region of V(H) is sufficient for most antibody specificities. Immunity 13:37-45.
    • (2000) Immunity , vol.13 , pp. 37-45
    • Xu, J.L.1    Davis, M.M.2
  • 31
    • 43149113443 scopus 로고    scopus 로고
    • 4E10 and 2F5 monoclonal antibodies: Binding specificities to phospholipids, tolerance, and clinical safety issues
    • Alving CR (2008) 4E10 and 2F5 monoclonal antibodies: Binding specificities to phospholipids, tolerance, and clinical safety issues. AIDS 22:649-651.
    • (2008) AIDS , vol.22 , pp. 649-651
    • Alving, C.R.1
  • 32
    • 12144285761 scopus 로고    scopus 로고
    • The long third complementarity-determining region of the heavy chain is important in the activity of the broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2F5
    • Zwick MB, et al. (2004) The long third complementarity-determining region of the heavy chain is important in the activity of the broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2F5. J Virol 78:3155-3161.
    • (2004) J Virol , vol.78 , pp. 3155-3161
    • Zwick, M.B.1
  • 33
    • 33745268875 scopus 로고    scopus 로고
    • Membrane-transferring sequences of the HIV-1 Gp41 ectodomain assemble into an immunogenic complex
    • Lorizate M, Gómara MJ, de la Torre BG, Andreu D, Nieva JL (2006) Membrane-transferring sequences of the HIV-1 Gp41 ectodomain assemble into an immunogenic complex. J Mol Biol 360:45-55.
    • (2006) J Mol Biol , vol.360 , pp. 45-55
    • Lorizate, M.1    Gómara, M.J.2    de la Torre, B.G.3    Andreu, D.4    Nieva, J.L.5
  • 34
    • 0031740601 scopus 로고    scopus 로고
    • Hydrophobic interactions of peptides with membrane interfaces
    • White SH, Wimley WC (1998) Hydrophobic interactions of peptides with membrane interfaces. Biochim Biophys Acta 1376:339-352.
    • (1998) Biochim Biophys Acta , vol.1376 , pp. 339-352
    • White, S.H.1    Wimley, W.C.2
  • 36
    • 14744283551 scopus 로고
    • High-level expression of a recombinant antibody from myeloma cells using a glutamine synthetase gene as an amplifiable selectable marker
    • Bebbington CR, et al. (1992) High-level expression of a recombinant antibody from myeloma cells using a glutamine synthetase gene as an amplifiable selectable marker. Biotechnology (N Y) 10:169-175.
    • (1992) Biotechnology (N Y) , vol.10 , pp. 169-175
    • Bebbington, C.R.1
  • 37
    • 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
  • 39
    • 0027325411 scopus 로고
    • Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes
    • Aloia RC, Tian H, Jensen FC (1993) Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes. Proc Natl Acad Sci USA 90:5181-5185.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5181-5185
    • Aloia, R.C.1    Tian, H.2    Jensen, F.C.3
  • 40
    • 33644539188 scopus 로고    scopus 로고
    • The HIV lipidome: A raft with an unusual composition
    • Brügger B, et al. (2006) The HIV lipidome: A raft with an unusual composition. Proc Natl Acad Sci USA 103:2641-2646.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 2641-2646
    • Brügger, B.1
  • 41
    • 0031986075 scopus 로고    scopus 로고
    • Characterization of highly purified, inactivated HIV-1 particles isolated by anion exchange chromatography
    • Richieri SP, et al. (1998) Characterization of highly purified, inactivated HIV-1 particles isolated by anion exchange chromatography. Vaccine 16:119-129.
    • (1998) Vaccine , vol.16 , pp. 119-129
    • Richieri, S.P.1
  • 42
    • 51449112852 scopus 로고    scopus 로고
    • Cardiolipin synthesis for the assembly of bacterial and mitochondrial membranes
    • Schlame M (2008) Cardiolipin synthesis for the assembly of bacterial and mitochondrial membranes. J Lipid Res 49:1607-1620.
    • (2008) J Lipid Res , vol.49 , pp. 1607-1620
    • Schlame, M.1
  • 44
    • 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
    • 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.
    • (2008) Microbiol Mol Biol Rev , vol.72 , pp. 54-84
    • Montero, M.1    van Houten, N.E.2    Wang, X.3    Scott, J.K.4
  • 45
    • 67349188801 scopus 로고    scopus 로고
    • Structure of the Fab fragment of therapeutic antibody Ofatumumab provides insights into the recognition mechanism with CD20
    • Du J, Yang H, Guo Y, Ding J (2009) Structure of the Fab fragment of therapeutic antibody Ofatumumab provides insights into the recognition mechanism with CD20. Mol Immunol 46:2419-2423.
    • (2009) Mol Immunol , vol.46 , pp. 2419-2423
    • Du, J.1    Yang, H.2    Guo, Y.3    Ding, J.4
  • 46
    • 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
  • 47
    • 0028155283 scopus 로고
    • Generation of human monoclonal antibodies against HIV-1 proteins: Electrofusion and Epstein-Barr virus transformation for peripheral blood lymphocyte immortalization
    • Buchacher A, et al. (1994) Generation of human monoclonal antibodies against HIV-1 proteins: Electrofusion and Epstein-Barr virus transformation for peripheral blood lymphocyte immortalization. AIDS Res Hum Retroviruses 10:359-369.
    • (1994) AIDS Res Hum Retroviruses , vol.10 , pp. 359-369
    • Buchacher, A.1
  • 48
    • 3843139398 scopus 로고    scopus 로고
    • Characterization of molecular features, antigen-binding, and in vitro properties of IgG and IgM variants of 4E10, an anti-HIV type 1 neutralizing monoclonal antibody
    • Kunert R, Wolbank S, Stiegler G, Weik R, Katinger H (2004) Characterization of molecular features, antigen-binding, and in vitro properties of IgG and IgM variants of 4E10, an anti-HIV type 1 neutralizing monoclonal antibody. AIDS Res Hum Retroviruses 20:755-762.
    • (2004) AIDS Res Hum Retroviruses , vol.20 , pp. 755-762
    • Kunert, R.1    Wolbank, S.2    Stiegler, G.3    Weik, R.4    Katinger, H.5
  • 49
    • 34248559599 scopus 로고    scopus 로고
    • Gene splicing and mutagenesis by PCR-driven overlap extension
    • Heckman KL, Pease LR (2007) Gene splicing and mutagenesis by PCR-driven overlap extension. Nat Protoc 2:924-932.
    • (2007) Nat Protoc , vol.2 , pp. 924-932
    • Heckman, K.L.1    Pease, L.R.2
  • 50
    • 0037389643 scopus 로고    scopus 로고
    • Rapid evolution of the neutralizing antibody response to HIV type 1 infection
    • Richman DD, Wrin T, Little SJ, Petropoulos CJ (2003) Rapid evolution of the neutralizing antibody response to HIV type 1 infection. Proc Natl Acad Sci USA 100: 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


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