메뉴 건너뛰기




Volumn 84, Issue 7, 2010, Pages 3382-3395

In-solution virus capture assay helps deconstruct heterogeneous antibody recognition of human immunodeficiency virus type 1

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN; GLYCOPROTEIN 160; GLYCOPROTEIN 41; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 2F5; MONOCLONAL ANTIBODY 4E10; MONOCLONAL ANTIBODY Z13E1; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN;

EID: 77949378988     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.02363-09     Document Type: Article
Times cited : (49)

References (101)
  • 1
    • 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, S. M., M. McAdams, D. Boren, M. Rak, R. M. Scearce, F. Gao, Z. T. Camacho, D. Gewirth, G. Kelsoe, P. Chen, and B. F. Haynes. 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    McAdams, M.2    Boren, D.3    Rak, M.4    Scearce, R.M.5    Gao, F.6    Camacho, Z.T.7    Gewirth, D.8    Kelsoe, G.9    Chen, P.10    Haynes, B.F.11
  • 4
    • 45749138808 scopus 로고    scopus 로고
    • A glycoconjugate antigen based on the recognition motif of a broadly neutralizing human immunodeficiency virus antibody, 2G12, is immunogenic but elicits antibodies unable to bind to the self glycans of gp120
    • Astronomo, R. D., H. K. Lee, C. N. Scanlan, R. Pantophlet, C. Y. Huang, I. A. Wilson, O. Blixt, R. A. Dwek, C. H. Wong, and D. R. Burton. 2008. A glycoconjugate antigen based on the recognition motif of a broadly neutralizing human immunodeficiency virus antibody, 2G12, is immunogenic but elicits antibodies unable to bind to the self glycans of gp120. J. Virol. 82: 6359-6368.
    • (2008) J. Virol , vol.82 , pp. 6359-6368
    • Astronomo, R.D.1    Lee, H.K.2    Scanlan, C.N.3    Pantophlet, R.4    Huang, C.Y.5    Wilson, I.A.6    Blixt, O.7    Dwek, R.A.8    Wong, C.H.9    Burton, D.R.10
  • 5
    • 0031592573 scopus 로고    scopus 로고
    • Microvesicles are a source of contaminating cellular proteins found in purified HIV-1 preparations
    • Bess, J. W., Jr., R. J. Gorelick, W. J. Bosche, L. E. Henderson, and L. O. Arthur. 1997. Microvesicles are a source of contaminating cellular proteins found in purified HIV-1 preparations. Virology 230:134-144.
    • (1997) Virology , vol.230 , pp. 134-144
    • Bess Jr., J.W.1    Gorelick, R.J.2    Bosche, W.J.3    Henderson, L.E.4    Arthur, L.O.5
  • 7
    • 33846614277 scopus 로고    scopus 로고
    • Monoclonal antibodies to phosphatidylinositol phosphate neutralize human immunodeficiency virus type 1: Role of phosphate-binding subsites
    • Brown, B. K., N. Karasavvas, Z. Beck, G. R. Matyas, D. L. Birx, V. R. Polonis, and C. R. Alving. 2007. Monoclonal antibodies to phosphatidylinositol phosphate neutralize human immunodeficiency virus type 1: role of phosphate-binding subsites. J. Virol. 81:2087-2091.
    • (2007) J. Virol , vol.81 , pp. 2087-2091
    • Brown, B.K.1    Karasavvas, N.2    Beck, Z.3    Matyas, G.R.4    Birx, D.L.5    Polonis, V.R.6    Alving, C.R.7
  • 9
    • 13544252604 scopus 로고    scopus 로고
    • Neutralizing as well as non-neutralizing polyclonal immunoglobulin (Ig)G from infected patients capture HIV-1 via antibodies directed against the principal immunodominant domain of gp41
    • Burrer, R., S. Haessig-Einius, A. M. Aubertin, and C. Moog. 2005. Neutralizing as well as non-neutralizing polyclonal immunoglobulin (Ig)G from infected patients capture HIV-1 via antibodies directed against the principal immunodominant domain of gp41. Virology 333:102-113.
    • (2005) Virology , vol.333 , pp. 102-113
    • Burrer, R.1    Haessig-Einius, S.2    Aubertin, A.M.3    Moog, C.4
  • 12
    • 50949128891 scopus 로고    scopus 로고
    • Discrimination between exosomes and HIV-1: Purification of both vesicles from cell-free supernatants
    • Cantin, R., J. Diou, D. Belanger, A. M. Tremblay, and C. Gilbert. 2008. Discrimination between exosomes and HIV-1: purification of both vesicles from cell-free supernatants. J. Immunol. Methods 338:21-30.
    • (2008) J. Immunol. Methods , vol.338 , pp. 21-30
    • Cantin, R.1    Diou, J.2    Belanger, D.3    Tremblay, A.M.4    Gilbert, C.5
  • 13
    • 0037471318 scopus 로고    scopus 로고
    • Conformational changes in Env oligomer induced by an antibody dependent on the V3 loop base
    • Cavacini, L., M. Duval, L. Song, R. Sangster, S. H. Xiang, J. Sodroski, and M. Posner. 2003. Conformational changes in Env oligomer induced by an antibody dependent on the V3 loop base. AIDS 17:685-689.
    • (2003) AIDS , vol.17 , pp. 685-689
    • Cavacini, L.1    Duval, M.2    Song, L.3    Sangster, R.4    Xiang, S.H.5    Sodroski, J.6    Posner, M.7
  • 14
    • 2342580675 scopus 로고    scopus 로고
    • Native HIV type 1 virion surface structures: Relationships between antibody binding and neutralization or lessons from the viral capture assay
    • Cavacini, L., and M. Posner. 2004. Native HIV type 1 virion surface structures: relationships between antibody binding and neutralization or lessons from the viral capture assay. AIDS Res. Hum. Retrovir. 20:435-441.
    • (2004) AIDS Res. Hum. Retrovir , vol.20 , pp. 435-441
    • Cavacini, L.1    Posner, M.2
  • 15
    • 0037032903 scopus 로고    scopus 로고
    • Interactions of human antibodies, epitope exposure, antibody binding and neutralization of primary isolate HIV-1 virions
    • Cavacini, L. A., M. Duval, J. Robinson, and M. R. Posner. 2002. Interactions of human antibodies, epitope exposure, antibody binding and neutralization of primary isolate HIV-1 virions. AIDS 16:2409-2417.
    • (2002) AIDS , vol.16 , pp. 2409-2417
    • Cavacini, L.A.1    Duval, M.2    Robinson, J.3    Posner, M.R.4
  • 16
    • 0032552454 scopus 로고    scopus 로고
    • Functional and molecular characterization of human monoclonal antibody reactive with the immunodominant region of HIV type 1 glycoprotein 41
    • Cavacini, L. A., C. L. Emes, A. V. Wisnewski, J. Power, G. Lewis, D. Montefiori, and M. R. Posner. 1998. Functional and molecular characterization of human monoclonal antibody reactive with the immunodominant region of HIV type 1 glycoprotein 41. AIDS Res. Hum. Retrovir. 14:1271-1280.
    • (1998) AIDS Res. Hum. Retrovir , vol.14 , pp. 1271-1280
    • Cavacini, L.A.1    Emes, C.L.2    Wisnewski, A.V.3    Power, J.4    Lewis, G.5    Montefiori, D.6    Posner, M.R.7
  • 19
    • 1242342052 scopus 로고    scopus 로고
    • Binding of the 2F5 monoclonal antibody to native and fusion-intermediate forms of human immunodeficiency virus type 1 gp41: Implications for fusion-inducing conformational changes
    • de Rosny, E., R. Vassell, S. Jiang, R. Kunert, and C. D. Weiss. 2004. Binding of the 2F5 monoclonal antibody to native and fusion-intermediate forms of human immunodeficiency virus type 1 gp41: implications for fusion-inducing conformational changes. J. Virol. 78:2627-2631.
    • (2004) J. Virol , vol.78 , pp. 2627-2631
    • de Rosny, E.1    Vassell, R.2    Jiang, S.3    Kunert, R.4    Weiss, C.D.5
  • 20
    • 0032935035 scopus 로고    scopus 로고
    • Highly purified human immunodeficiency virus type 1 reveals a virtual absence of Vif in virions
    • Dettenhofer, M., and X. F. Yu. 1999. Highly purified human immunodeficiency virus type 1 reveals a virtual absence of Vif in virions. J. Virol. 73:1460-1467.
    • (1999) J. Virol , vol.73 , pp. 1460-1467
    • Dettenhofer, M.1    Yu, X.F.2
  • 21
    • 38949090023 scopus 로고    scopus 로고
    • N-terminal substitutions in HIV-1 gp41 reduce the expression of non-trimeric envelope glycoproteins on the virus
    • Dey, A. K., K. B. David, N. Ray, T. J. Ketas, P. J. Klasse, R. W. Doms, and J. P. Moore. 2008. N-terminal substitutions in HIV-1 gp41 reduce the expression of non-trimeric envelope glycoproteins on the virus. Virology 372: 187-200.
    • (2008) Virology , vol.372 , pp. 187-200
    • Dey, A.K.1    David, K.B.2    Ray, N.3    Ketas, T.J.4    Klasse, P.J.5    Doms, R.W.6    Moore, J.P.7
  • 22
    • 0029015314 scopus 로고
    • Analysis of the cleavage site of the human immunodeficiency virus type 1 glycoprotein: Requirement of precursor cleavage for glycoprotein incorporation
    • Dubay, J. W., S. R. Dubay, H. J. Shin, and E. Hunter. 1995. Analysis of the cleavage site of the human immunodeficiency virus type 1 glycoprotein: requirement of precursor cleavage for glycoprotein incorporation. J. Virol. 69:4675-4682.
    • (1995) J. Virol , vol.69 , pp. 4675-4682
    • Dubay, J.W.1    Dubay, S.R.2    Shin, H.J.3    Hunter, E.4
  • 23
    • 0030997127 scopus 로고    scopus 로고
    • Epitope map of human immunodeficiency virus type 1 gp41 derived from 47 monoclonal antibodies produced by immunization with oligomeric envelope protein
    • Earl, P. L., C. C. Broder, R. W. Doms, and B. Moss. 1997. Epitope map of human immunodeficiency virus type 1 gp41 derived from 47 monoclonal antibodies produced by immunization with oligomeric envelope protein. J. Virol. 71:2674-2684.
    • (1997) J. Virol , vol.71 , pp. 2674-2684
    • Earl, P.L.1    Broder, C.C.2    Doms, R.W.3    Moss, B.4
  • 25
    • 0031592609 scopus 로고    scopus 로고
    • Cell membrane vesicles are a major contaminant of gradient-enriched human immunodeficiency virus type-1 preparations
    • Gluschankof, P., I. Mondor, H. R. Gelderblom, and Q. J. Sattentau. 1997. Cell membrane vesicles are a major contaminant of gradient-enriched human immunodeficiency virus type-1 preparations. Virology 230:125-133.
    • (1997) Virology , vol.230 , pp. 125-133
    • Gluschankof, P.1    Mondor, I.2    Gelderblom, H.R.3    Sattentau, Q.J.4
  • 27
    • 0036121261 scopus 로고    scopus 로고
    • Solid-phase proteoliposomes containing human immunodeficiency virus envelope glycoproteins
    • Grundner, C., T. Mirzabekov, J. Sodroski, and R. Wyatt. 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
  • 28
    • 0025352039 scopus 로고
    • The carboxy terminus of human immunodeficiency virus type 1 gp160 limits its proteolytic processing and transport in transfected cell lines
    • Haffar, O. K., G. R. Nakamura, and P. W. Berman. 1990. The carboxy terminus of human immunodeficiency virus type 1 gp160 limits its proteolytic processing and transport in transfected cell lines. J. Virol. 64:3100-3103.
    • (1990) J. Virol , vol.64 , pp. 3100-3103
    • Haffar, O.K.1    Nakamura, G.R.2    Berman, P.W.3
  • 29
    • 26944466459 scopus 로고    scopus 로고
    • Mechanism of membrane fusion by viral envelope proteins
    • Harrison, S. C. 2005. Mechanism of membrane fusion by viral envelope proteins. Adv. Virus Res. 64:231-261.
    • (2005) Adv. Virus Res , vol.64 , pp. 231-261
    • Harrison, S.C.1
  • 30
    • 14844360667 scopus 로고    scopus 로고
    • V3: HIV's switch-hitter. AIDS Res. Hum. Retrovir
    • Hartley, O., P. J. Klasse, Q. J. Sattentau, and J. P. Moore. 2005. V3: HIV's switch-hitter. AIDS Res. Hum. Retrovir. 21:171-189.
    • (2005) , vol.21 , pp. 171-189
    • Hartley, O.1    Klasse, P.J.2    Sattentau, Q.J.3    Moore, J.P.4
  • 32
    • 33746763724 scopus 로고    scopus 로고
    • Aiming to induce broadly reactive neutralizing antibody responses with HIV-1 vaccine candidates
    • Haynes, B. F., and D. C. Montefiori. 2006. Aiming to induce broadly reactive neutralizing antibody responses with HIV-1 vaccine candidates. Expert Rev. Vaccines 5:347-363.
    • (2006) Expert Rev. Vaccines , vol.5 , pp. 347-363
    • Haynes, B.F.1    Montefiori, D.C.2
  • 33
  • 34
    • 20644433322 scopus 로고    scopus 로고
    • The impact of envelope glycoprotein cleavage on the antigenicity, infectivity, and neutralization sensitivity of Env-pseudotyped human immunodeficiency virus type 1 particles
    • Herrera, C., P. J. Klasse, E. Michael, S. Kake, K. Barnes, C. W. Kibler, L. Campbell-Gardener, Z. Si, J. Sodroski, J. P. Moore, and S. Beddows. 2005. The impact of envelope glycoprotein cleavage on the antigenicity, infectivity, and neutralization sensitivity of Env-pseudotyped human immunodeficiency virus type 1 particles. Virology 338:154-172.
    • (2005) Virology , vol.338 , pp. 154-172
    • Herrera, C.1    Klasse, P.J.2    Michael, E.3    Kake, S.4    Barnes, K.5    Kibler, C.W.6    Campbell-Gardener, L.7    Si, Z.8    Sodroski, J.9    Moore, J.P.10    Beddows, S.11
  • 35
    • 0037223708 scopus 로고    scopus 로고
    • Nonneutralizing antibodies to the CD4-binding site on the gp120 subunit of human immunodeficiency virus type 1 do not interfere with the activity of a neutralizing antibody against the same site
    • Herrera, C., C. Spenlehauer, M. S. Fung, D. R. Burton, S. Beddows, and J. P. Moore. 2003. Nonneutralizing antibodies to the CD4-binding site on the gp120 subunit of human immunodeficiency virus type 1 do not interfere with the activity of a neutralizing antibody against the same site. J. Virol. 77:1084-1091.
    • (2003) J. Virol , vol.77 , pp. 1084-1091
    • Herrera, C.1    Spenlehauer, C.2    Fung, M.S.3    Burton, D.R.4    Beddows, S.5    Moore, J.P.6
  • 36
    • 0025958022 scopus 로고
    • Conformational epitope on gp120 important in CD4 binding and human immunodeficiency virus type 1 neutralization identified by a human monoclonal antibody
    • Ho, D. D., J. A. McKeating, X. L. Li, T. Moudgil, E. S. Daar, N. C. Sun, and J. E. Robinson. 1991. Conformational epitope on gp120 important in CD4 binding and human immunodeficiency virus type 1 neutralization identified by a human monoclonal antibody. J. Virol. 65:489-493.
    • (1991) J. Virol , vol.65 , pp. 489-493
    • Ho, D.D.1    McKeating, J.A.2    Li, X.L.3    Moudgil, T.4    Daar, E.S.5    Sun, N.C.6    Robinson, J.E.7
  • 37
    • 84954358531 scopus 로고    scopus 로고
    • Lipid modulation of membrane-bound epitope recognition and blocking by HIV-1 neutralizing antibodies
    • Huarte, N., M. Lorizate, R. Kunert, and J. L. Nieva. 2008. Lipid modulation of membrane-bound epitope recognition and blocking by HIV-1 neutralizing antibodies. FEBS Lett. 582:3798-3804.
    • (2008) FEBS Lett , vol.582 , pp. 3798-3804
    • Huarte, N.1    Lorizate, M.2    Kunert, R.3    Nieva, J.L.4
  • 38
    • 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., M. Lorizate, R. Maeso, R. Kunert, R. Arranz, J. M. Valpuesta, and J. L. Nieva. 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    Lorizate, M.2    Maeso, R.3    Kunert, R.4    Arranz, R.5    Valpuesta, J.M.6    Nieva, J.L.7
  • 39
    • 0035919637 scopus 로고    scopus 로고
    • Analysis of dominant-negative effects of mutant Env proteins of human immunodeficiency virus type 1
    • Iwatani, Y., K. Kawano, T. Ueno, M. Tanaka, A. Ishimoto, M. Ito, and H. Sakai. 2001. Analysis of dominant-negative effects of mutant Env proteins of human immunodeficiency virus type 1. Virology 286:45-53.
    • (2001) Virology , vol.286 , pp. 45-53
    • Iwatani, Y.1    Kawano, K.2    Ueno, T.3    Tanaka, M.4    Ishimoto, A.5    Ito, M.6    Sakai, H.7
  • 41
    • 38649091973 scopus 로고    scopus 로고
    • Peptide mimic of the HIV envelope gp120-gp41 interface
    • Kim, S., H. B. Pang, and M. S. Kay. 2008. Peptide mimic of the HIV envelope gp120-gp41 interface. J. Mol. Biol. 376:786-797.
    • (2008) J. Mol. Biol , vol.376 , pp. 786-797
    • Kim, S.1    Pang, H.B.2    Kay, M.S.3
  • 42
    • 65249139402 scopus 로고    scopus 로고
    • Conformational stability and membrane interaction of the full-length ectodomain of HIV-1 gp41: Implication for mode of action
    • Lev, N., Y. Fridmann-Sirkis, L. Blank, A. Bitler, R. F. Epand, R. M. Epand, and Y. Shai. 2009. Conformational stability and membrane interaction of the full-length ectodomain of HIV-1 gp41: implication for mode of action. Biochemistry 48:3166-3175.
    • (2009) Biochemistry , vol.48 , pp. 3166-3175
    • Lev, N.1    Fridmann-Sirkis, Y.2    Blank, L.3    Bitler, A.4    Epand, R.F.5    Epand, R.M.6    Shai, Y.7
  • 46
    • 65349132918 scopus 로고    scopus 로고
    • A yeast glycoprotein shows high-affinity binding to the broadly neutralizing human immunodeficiency virus antibody 2G12 and inhibits gp120 interactions with 2G12 and DCSIGN
    • Luallen, R. J., H. Fu, C. Agrawal-Gamse, I. Mboudjeka, W. Huang, F. H. Lee, L. X. Wang, R. W. Doms, and Y. Geng. 2009. A yeast glycoprotein shows high-affinity binding to the broadly neutralizing human immunodeficiency virus antibody 2G12 and inhibits gp120 interactions with 2G12 and DCSIGN. J. Virol. 83:4861-4870.
    • (2009) J. Virol , vol.83 , pp. 4861-4870
    • Luallen, R.J.1    Fu, H.2    Agrawal-Gamse, C.3    Mboudjeka, I.4    Huang, W.5    Lee, F.H.6    Wang, L.X.7    Doms, R.W.8    Geng, Y.9
  • 47
    • 45749122331 scopus 로고    scopus 로고
    • An engineered Saccharomyces cerevisiae strain binds the broadly neutralizing human immunodeficiency virus type 1 antibody 2G12 and elicits mannose-specific gp120-binding antibodies
    • Luallen, R. J., J. Lin, H. Fu, K. K. Cai, C. Agrawal, I. Mboudjeka, F. H. Lee, D. Montefiori, D. F. Smith, R. W. Doms, and Y. Geng. 2008. An engineered Saccharomyces cerevisiae strain binds the broadly neutralizing human immunodeficiency virus type 1 antibody 2G12 and elicits mannose-specific gp120-binding antibodies. J. Virol. 82:6447-6457.
    • (2008) J. Virol , vol.82 , pp. 6447-6457
    • Luallen, R.J.1    Lin, J.2    Fu, H.3    Cai, K.K.4    Agrawal, C.5    Mboudjeka, I.6    Lee, F.H.7    Montefiori, D.8    Smith, D.F.9    Doms, R.W.10    Geng, Y.11
  • 49
    • 0023921610 scopus 로고
    • Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus
    • McCune, J. M., L. B. Rabin, M. B. Feinberg, M. Lieberman, J. C. Kosek, G. R. Reyes, and I. L. Weissman. 1988. Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus. Cell 53:55-67.
    • (1988) Cell , vol.53 , pp. 55-67
    • McCune, J.M.1    Rabin, L.B.2    Feinberg, M.B.3    Lieberman, M.4    Kosek, J.C.5    Reyes, G.R.6    Weissman, I.L.7
  • 50
    • 26844448487 scopus 로고    scopus 로고
    • Miller, M. D., R. Geleziunas, E. Bianchi, S. Lennard, R. Hrin, H. Zhang, M. Lu, Z. An, P. Ingallinella, M. Finotto, M. Mattu, A. C. Finnefrock, D. Bramhill, J. Cook, D. M. Eckert, R. Hampton, M. Patel, S. Jarantow, J. Joyce, G. Ciliberto, R. Cortese, P. Lu, W. Strohl, W. Schleif, M. McElhaugh, S. Lane, C. Lloyd, D. Lowe, J. Osbourn, T. Vaughan, E. Emini, G. Barbato, P. S. Kim, D. J. Hazuda, J. W. Shiver, and A. Pessi. 2005. A human monoclonal antibody neutralizes diverse HIV-1 isolates by binding a critical gp41 epitope. Proc. Natl. Acad. Sci. U. S. A. 102:14759-14764.
    • Miller, M. D., R. Geleziunas, E. Bianchi, S. Lennard, R. Hrin, H. Zhang, M. Lu, Z. An, P. Ingallinella, M. Finotto, M. Mattu, A. C. Finnefrock, D. Bramhill, J. Cook, D. M. Eckert, R. Hampton, M. Patel, S. Jarantow, J. Joyce, G. Ciliberto, R. Cortese, P. Lu, W. Strohl, W. Schleif, M. McElhaugh, S. Lane, C. Lloyd, D. Lowe, J. Osbourn, T. Vaughan, E. Emini, G. Barbato, P. S. Kim, D. J. Hazuda, J. W. Shiver, and A. Pessi. 2005. A human monoclonal antibody neutralizes diverse HIV-1 isolates by binding a critical gp41 epitope. Proc. Natl. Acad. Sci. U. S. A. 102:14759-14764.
  • 54
    • 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, J. D., F. M. Brunel, R. Jensen, E. T. Crooks, R. M. Cardoso, M. Wang, A. Hessell, I. A. Wilson, J. M. Binley, P. E. Dawson, D. R. Burton, and M. B. Zwick. 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    Brunel, F.M.2    Jensen, R.3    Crooks, E.T.4    Cardoso, R.M.5    Wang, M.6    Hessell, A.7    Wilson, I.A.8    Binley, J.M.9    Dawson, P.E.10    Burton, D.R.11    Zwick, M.B.12
  • 56
    • 0031710046 scopus 로고    scopus 로고
    • Mapping of epitopes exposed on intact human immunodeficiency virus type 1 (HIV-1) virions: A new strategy for studying the immunologic relatedness of HIV-1
    • Nyambi, P. N., M. K. Gorny, L. Bastiani, G. van der Groen, C. Williams, and S. Zolla-Pazner. 1998. Mapping of epitopes exposed on intact human immunodeficiency virus type 1 (HIV-1) virions: a new strategy for studying the immunologic relatedness of HIV-1. J. Virol. 72:9384-9391.
    • (1998) J. Virol , vol.72 , pp. 9384-9391
    • Nyambi, P.N.1    Gorny, M.K.2    Bastiani, L.3    van der Groen, G.4    Williams, C.5    Zolla-Pazner, S.6
  • 57
    • 0033942757 scopus 로고    scopus 로고
    • Conserved and exposed epitopes on intact, native, primary human immunodeficiency virus type 1 virions of group M
    • Nyambi, P. N., H. A. Mbah, S. Burda, C. Williams, M. K. Gorny, A. Nadas, and S. Zolla-Pazner. 2000. Conserved and exposed epitopes on intact, native, primary human immunodeficiency virus type 1 virions of group M. J. Virol. 74:7096-7107.
    • (2000) J. Virol , vol.74 , pp. 7096-7107
    • Nyambi, P.N.1    Mbah, H.A.2    Burda, S.3    Williams, C.4    Gorny, M.K.5    Nadas, A.6    Zolla-Pazner, S.7
  • 58
    • 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., M. Tang, A. Sambor, H. Katinger, J. R. Mascola, R. Wyatt, and P. D. Kwong. 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    Tang, M.2    Sambor, A.3    Katinger, H.4    Mascola, J.R.5    Wyatt, R.6    Kwong, P.D.7
  • 59
    • 77649132440 scopus 로고    scopus 로고
    • Relationship between antibody 2F5 neutralization of HIV-1 and hydrophobicity of its heavy chain third complementarity-determining region
    • Ofek, G., K. McKee, Y. Yang, Z.-Y. Yang, J. Skinner, F. J. Guenaga, R. Wyatt, M. B. Zwick, G. J. Nabel, J. R. Mascola, and P. D. Kwong. 2009. Relationship between antibody 2F5 neutralization of HIV-1 and hydrophobicity of its heavy chain third complementarity-determining region. J. Virol. 84:2955-2962.
    • (2009) J. Virol , vol.84 , pp. 2955-2962
    • Ofek, G.1    McKee, K.2    Yang, Y.3    Yang, Z.-Y.4    Skinner, J.5    Guenaga, F.J.6    Wyatt, R.7    Zwick, M.B.8    Nabel, G.J.9    Mascola, J.R.10    Kwong, P.D.11
  • 60
    • 0025203223 scopus 로고
    • The human immunodeficiency virus type 1 envelope glycoprotein precursor acquires aberrant intermolecular disulfide bonds that may prevent normal proteolytic processing
    • Owens, R. J., and R. W. Compans. 1990. The human immunodeficiency virus type 1 envelope glycoprotein precursor acquires aberrant intermolecular disulfide bonds that may prevent normal proteolytic processing. Virology 179:827-833.
    • (1990) Virology , vol.179 , pp. 827-833
    • Owens, R.J.1    Compans, R.W.2
  • 61
    • 12344264596 scopus 로고    scopus 로고
    • Selective recognition of oligomeric HIV-1 primary isolate envelope glycoproteins by potently neutralizing ligands requires efficient precursor cleavage
    • Pancera, M., and R. Wyatt. 2005. Selective recognition of oligomeric HIV-1 primary isolate envelope glycoproteins by potently neutralizing ligands requires efficient precursor cleavage. Virology 332:145-156.
    • (2005) Virology , vol.332 , pp. 145-156
    • Pancera, M.1    Wyatt, R.2
  • 62
    • 0029861453 scopus 로고    scopus 로고
    • In vitro antigen challenge of human antibody libraries for vaccine evaluation: The human immunodeficiency virus type 1 envelope
    • Parren, P. W., P. Fisicaro, A. F. Labrijn, J. M. Binley, W. P. Yang, H. J. Ditzel, C. F. Barbas III, and D. R. Burton. 1996. In vitro antigen challenge of human antibody libraries for vaccine evaluation: the human immunodeficiency virus type 1 envelope. J. Virol. 70:9046-9050.
    • (1996) J. Virol , vol.70 , pp. 9046-9050
    • Parren, P.W.1    Fisicaro, P.2    Labrijn, A.F.3    Binley, J.M.4    Yang, W.P.5    Ditzel, H.J.6    Barbas III, C.F.7    Burton, D.R.8
  • 63
    • 0026318224 scopus 로고
    • Changes in growth properties on passage in tissue culture of viruses derived from infectious molecular clones of HIV-1LAI, HIV-1MAL, and HIV-1ELI
    • Peden, K., M. Emerman, and L. Montagnier. 1991. Changes in growth properties on passage in tissue culture of viruses derived from infectious molecular clones of HIV-1LAI, HIV-1MAL, and HIV-1ELI. Virology 185: 661-672.
    • (1991) Virology , vol.185 , pp. 661-672
    • Peden, K.1    Emerman, M.2    Montagnier, L.3
  • 64
    • 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., J. S. Gach, F. M. Brunel, R. M. Cardoso, R. L. Stanfield, P. E. Dawson, D. R. Burton, M. B. Zwick, and I. A. Wilson. 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    Gach, J.S.2    Brunel, F.M.3    Cardoso, R.M.4    Stanfield, R.L.5    Dawson, P.E.6    Burton, D.R.7    Zwick, M.B.8    Wilson, I.A.9
  • 65
    • 0037442143 scopus 로고    scopus 로고
    • In vivo efficacy of anti-glycoprotein 41, but not antiglycoprotein 120, immunotoxins in a mouse model of HIV infection
    • Pincus, S. H., H. Fang, R. A. Wilkinson, T. K. Marcotte, J. E. Robinson, and W. C. Olson. 2003. In vivo efficacy of anti-glycoprotein 41, but not antiglycoprotein 120, immunotoxins in a mouse model of HIV infection. J. Immunol. 170:2236-2241.
    • (2003) J. Immunol , vol.170 , pp. 2236-2241
    • Pincus, S.H.1    Fang, H.2    Wilkinson, R.A.3    Marcotte, T.K.4    Robinson, J.E.5    Olson, W.C.6
  • 66
    • 0037213278 scopus 로고    scopus 로고
    • Heterogeneity of envelope molecules expressed on primary human immunodeficiency virus type 1 particles as probed by the binding of neutralizing and nonneutralizing antibodies
    • Poignard, P., M. Moulard, E. Golez, V. Vivona, M. Franti, S. Venturini, M. Wang, P. W. Parren, and D. R. Burton. 2003. Heterogeneity of envelope molecules expressed on primary human immunodeficiency virus type 1 particles as probed by the binding of neutralizing and nonneutralizing antibodies. J. Virol. 77:353-365.
    • (2003) J. Virol , vol.77 , pp. 353-365
    • Poignard, P.1    Moulard, M.2    Golez, E.3    Vivona, V.4    Franti, M.5    Venturini, S.6    Wang, M.7    Parren, P.W.8    Burton, D.R.9
  • 67
    • 0027458347 scopus 로고
    • Neutralization of HIV-1 by F105, a human monoclonal antibody to the CD4 binding site of gp120
    • Posner, M. R., L. A. Cavacini, C. L. Emes, J. Power, and R. Byrn. 1993. Neutralization of HIV-1 by F105, a human monoclonal antibody to the CD4 binding site of gp120. J. Acquir. Immune Defic. Syndr. 6:7-14.
    • (1993) J. Acquir. Immune Defic. Syndr , vol.6 , pp. 7-14
    • Posner, M.R.1    Cavacini, L.A.2    Emes, C.L.3    Power, J.4    Byrn, R.5
  • 68
    • 69249216589 scopus 로고    scopus 로고
    • The infectious molecular clone and pseudotyped virus models of human immunodeficiency virus type 1 exhibit significant differences in virion composition with only moderate differences in infectivity and inhibition sensitivity
    • Provine, N. M., W. B. Puryear, X. Wu, J. Overbaugh, and N. L. Haigwood. 2009. The infectious molecular clone and pseudotyped virus models of human immunodeficiency virus type 1 exhibit significant differences in virion composition with only moderate differences in infectivity and inhibition sensitivity. J. Virol. 83:9002-9007.
    • (2009) J. Virol , vol.83 , pp. 9002-9007
    • Provine, N.M.1    Puryear, W.B.2    Wu, X.3    Overbaugh, J.4    Haigwood, N.L.5
  • 69
    • 33750295885 scopus 로고    scopus 로고
    • Transfection of mammalian cells using linear polyethylenimine is a simple and effective means of producing recombinant adeno-associated virus vectors
    • Reed, S. E., E. M. Staley, J. P. Mayginnes, D. J. Pintel, and G. E. Tullis. 2006. Transfection of mammalian cells using linear polyethylenimine is a simple and effective means of producing recombinant adeno-associated virus vectors. J. Virol. Methods 138:85-98.
    • (2006) J. Virol. Methods , vol.138 , pp. 85-98
    • Reed, S.E.1    Staley, E.M.2    Mayginnes, J.P.3    Pintel, D.J.4    Tullis, G.E.5
  • 70
  • 71
    • 0028291731 scopus 로고
    • Recognition properties of a panel of human recombinant Fab fragments to the CD4 binding site of gp120 that show differing abilities to neutralize human immunodeficiency virus type 1
    • Roben, P., J. P. Moore, M. Thali, J. Sodroski, C. F. Barbas III, and D. R. Burton. 1994. Recognition properties of a panel of human recombinant Fab fragments to the CD4 binding site of gp120 that show differing abilities to neutralize human immunodeficiency virus type 1. J. Virol. 68:4821-4828.
    • (1994) J. Virol , vol.68 , pp. 4821-4828
    • Roben, P.1    Moore, J.P.2    Thali, M.3    Sodroski, J.4    Barbas III, C.F.5    Burton, D.R.6
  • 72
    • 0037077229 scopus 로고    scopus 로고
    • Sphingomyelin and cholesterol promote HIV-1 gp41 pre-transmembrane sequence surface aggregation and membrane restructuring
    • Saez-Cirion, A., S. Nir, M. Lorizate, A. Agirre, A. Cruz, J. Perez-Gil, and J. L. Nieva. 2002. Sphingomyelin and cholesterol promote HIV-1 gp41 pre-transmembrane sequence surface aggregation and membrane restructuring. J. Biol. Chem. 277:21776-21785.
    • (2002) J. Biol. Chem , vol.277 , pp. 21776-21785
    • Saez-Cirion, A.1    Nir, S.2    Lorizate, M.3    Agirre, A.4    Cruz, A.5    Perez-Gil, J.6    Nieva, J.L.7
  • 73
    • 33646394886 scopus 로고    scopus 로고
    • Specific phospholipid recognition by human immunodeficiency virus type-1 neutralizing anti-gp41 2F5 antibody
    • Sanchez-Martinez, S., M. Lorizate, K. Hermann, R. Kunert, G. Basanez, and J. L. Nieva. 2006. Specific phospholipid recognition by human immunodeficiency virus type-1 neutralizing anti-gp41 2F5 antibody. FEBS Lett. 580:2395-2399.
    • (2006) FEBS Lett , vol.580 , pp. 2395-2399
    • Sanchez-Martinez, S.1    Lorizate, M.2    Hermann, K.3    Kunert, R.4    Basanez, G.5    Nieva, J.L.6
  • 74
    • 33845978962 scopus 로고    scopus 로고
    • Membrane association and epitope recognition by HIV-1 neutralizing anti-gp41 2F5 and 4E10 antibodies
    • Sanchez-Martinez, S., M. Lorizate, H. Katinger, R. Kunert, and J. L. Nieva. 2006. Membrane association and epitope recognition by HIV-1 neutralizing anti-gp41 2F5 and 4E10 antibodies. AIDS Res. Hum. Retrovir. 22:998-1006.
    • (2006) AIDS Res. Hum. Retrovir , vol.22 , pp. 998-1006
    • Sanchez-Martinez, S.1    Lorizate, M.2    Katinger, H.3    Kunert, R.4    Nieva, J.L.5
  • 75
    • 18244422922 scopus 로고    scopus 로고
    • The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of α1→2 mannose residues on the outer face of gp120
    • Scanlan, C. N., R. Pantophlet, M. R. Wormald, E. Ollmann Saphire, R. Stanfield, I. A. Wilson, H. Katinger, R. A. Dwek, P. M. Rudd, and D. R. Burton. 2002. The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of α1→2 mannose residues on the outer face of gp120. J. Virol. 76:7306-7321.
    • (2002) J. Virol , vol.76 , pp. 7306-7321
    • Scanlan, C.N.1    Pantophlet, R.2    Wormald, M.R.3    Ollmann Saphire, E.4    Stanfield, R.5    Wilson, I.A.6    Katinger, H.7    Dwek, R.A.8    Rudd, P.M.9    Burton, D.R.10
  • 77
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schagger, H., and G. von Jagow. 1991. Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 199:223-231.
    • (1991) Anal. Biochem , vol.199 , pp. 223-231
    • Schagger, H.1    von Jagow, G.2
  • 78
    • 37349058177 scopus 로고    scopus 로고
    • Difficulties in eliciting broadly neutralizing anti-HIV antibodies are not explained by cardiolipin autoreactivity
    • Scherer, E. M., M. B. Zwick, L. Teyton, and D. R. Burton. 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
  • 80
    • 0035859948 scopus 로고    scopus 로고
    • The membraneproximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles
    • Schibli, D. J., R. C. Montelaro, and H. J. Vogel. 2001. The membraneproximal 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
  • 81
    • 43949136434 scopus 로고    scopus 로고
    • Role of the membrane-spanning domain of human immunodeficiency virus type 1 envelope glycoprotein in cell-cell fusion and virus infection
    • Shang, L., L. Yue, and E. Hunter. 2008. Role of the membrane-spanning domain of human immunodeficiency virus type 1 envelope glycoprotein in cell-cell fusion and virus infection. J. Virol. 82:5417-5428.
    • (2008) J. Virol , vol.82 , pp. 5417-5428
    • Shang, L.1    Yue, L.2    Hunter, E.3
  • 83
    • 37849000389 scopus 로고    scopus 로고
    • HIV-1 broadly neutralizing antibody extracts its epitope from a kinked gp41 ectodomain region on the viral membrane
    • Sun, Z. Y., K. J. Oh, M. Kim, J. Yu, V. Brusic, L. Song, Z. Qiao, J. H. Wang, G. Wagner, and E. L. Reinherz. 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    Oh, K.J.2    Kim, M.3    Yu, J.4    Brusic, V.5    Song, L.6    Qiao, Z.7    Wang, J.H.8    Wagner, G.9    Reinherz, E.L.10
  • 84
    • 0027256814 scopus 로고
    • Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding
    • Thali, M., J. P. Moore, C. Furman, M. Charles, D. D. Ho, J. Robinson, and J. Sodroski. 1993. Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding. J. Virol. 67:3978-3988.
    • (1993) J. Virol , vol.67 , pp. 3978-3988
    • Thali, M.1    Moore, J.P.2    Furman, C.3    Charles, M.4    Ho, D.D.5    Robinson, J.6    Sodroski, J.7
  • 85
    • 57349127300 scopus 로고    scopus 로고
    • Tomaras, G. D., N. L. Yates, P. Liu, L. Qin, G. G. Fouda, L. L. Chavez, A. C. Decamp, R. J. Parks, V. C. Ashley, J. T. Lucas, M. Cohen, J. Eron, C. B. Hicks, H. X. Liao, S. G. Self, G. Landucci, D. N. Forthal, K. J. Weinhold, B. F. Keele, B. H. Hahn, M. L. Greenberg, L. Morris, S. S. Karim, W. A. Blattner, D. C. Montefiori, G. M. Shaw, A. S. Perelson, and B. F. Haynes. 2008. Initial B-cell responses to transmitted human immunodeficiency virus type 1: virion-binding immunoglobulinM(IgM) and IgG antibodies followed by plasma anti-gp41 antibodies with ineffective control of initial viremia. J. Virol. 82:12449-12463.
    • Tomaras, G. D., N. L. Yates, P. Liu, L. Qin, G. G. Fouda, L. L. Chavez, A. C. Decamp, R. J. Parks, V. C. Ashley, J. T. Lucas, M. Cohen, J. Eron, C. B. Hicks, H. X. Liao, S. G. Self, G. Landucci, D. N. Forthal, K. J. Weinhold, B. F. Keele, B. H. Hahn, M. L. Greenberg, L. Morris, S. S. Karim, W. A. Blattner, D. C. Montefiori, G. M. Shaw, A. S. Perelson, and B. F. Haynes. 2008. Initial B-cell responses to transmitted human immunodeficiency virus type 1: virion-binding immunoglobulinM(IgM) and IgG antibodies followed by plasma anti-gp41 antibodies with ineffective control of initial viremia. J. Virol. 82:12449-12463.
  • 87
    • 85043488048 scopus 로고    scopus 로고
    • Interactions of HIV-1 antibodies 2F5 and 4E10 with a gp41 epitope prebound to host and viral membrane model systems
    • Veiga, A. S., L. K. Pattenden, J. M. Fletcher, M. A. Castanho, and M. I. Aguilar. 2009. Interactions of HIV-1 antibodies 2F5 and 4E10 with a gp41 epitope prebound to host and viral membrane model systems. Chembiochem 10:1032-1044.
    • (2009) Chembiochem , vol.10 , pp. 1032-1044
    • Veiga, A.S.1    Pattenden, L.K.2    Fletcher, J.M.3    Castanho, M.A.4    Aguilar, M.I.5
  • 88
    • 39649094102 scopus 로고    scopus 로고
    • Photoinduced reactivity of the HIV-1 envelope glycoprotein with a membrane-embedded probe reveals insertion of portions of the HIV-1 Gp41 cytoplasmic tail into the viral membrane
    • Viard, M., S. D. Ablan, M. Zhou, T. D. Veenstra, E. O. Freed, Y. Raviv, and R. Blumenthal. 2008. Photoinduced reactivity of the HIV-1 envelope glycoprotein with a membrane-embedded probe reveals insertion of portions of the HIV-1 Gp41 cytoplasmic tail into the viral membrane. Biochemistry 47:1977-1983.
    • (2008) Biochemistry , vol.47 , pp. 1977-1983
    • Viard, M.1    Ablan, S.D.2    Zhou, M.3    Veenstra, T.D.4    Freed, E.O.5    Raviv, Y.6    Blumenthal, R.7
  • 89
    • 44049108744 scopus 로고    scopus 로고
    • Toward an AIDS vaccine
    • Walker, B. D., and D. R. Burton. 2008. Toward an AIDS vaccine. Science 320:760-764.
    • (2008) Science , vol.320 , pp. 760-764
    • Walker, B.D.1    Burton, D.R.2
  • 92
    • 0029119783 scopus 로고
    • Involvement of the V1/V2 variable loop structure in the exposure of human immunodeficiency virus type 1 gp120 epitopes induced by receptor binding
    • Wyatt, R., J. Moore, M. Accola, E. Desjardin, J. Robinson, and J. Sodroski. 1995. Involvement of the V1/V2 variable loop structure in the exposure of human immunodeficiency virus type 1 gp120 epitopes induced by receptor binding. J. Virol. 69:5723-5733.
    • (1995) J. Virol , vol.69 , pp. 5723-5733
    • Wyatt, R.1    Moore, J.2    Accola, M.3    Desjardin, E.4    Robinson, J.5    Sodroski, J.6
  • 93
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: Fusogens, antigens, and immunogens
    • Wyatt, R., and J. Sodroski. 1998. The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens. Science 280:1884-1888.
    • (1998) Science , vol.280 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2
  • 94
    • 73849143129 scopus 로고    scopus 로고
    • Interactions between lipids and human anti-HIV antibody 4E10 can be reduced without ablating neutralizing activity
    • Xu, H., L. Song, M. Kim, M. A. Holmes, Z. Kraft, G. Sellhorn, E. L. Reinherz, L. Stamatatos, and R. K. Strong. 2009. Interactions between lipids and human anti-HIV antibody 4E10 can be reduced without ablating neutralizing activity. J. Virol. 84:1076-1088.
    • (2009) J. Virol , vol.84 , pp. 1076-1088
    • Xu, H.1    Song, L.2    Kim, M.3    Holmes, M.A.4    Kraft, Z.5    Sellhorn, G.6    Reinherz, E.L.7    Stamatatos, L.8    Strong, R.K.9
  • 95
    • 33751578678 scopus 로고    scopus 로고
    • Antibodies against the activated coagulation factor X (FXa) in the antiphospholipid syndrome that interfere with the FXa inactivation by antithrombin
    • Yang, Y. H., K. K. Hwang, J. Fitz Gerald, J. M. Grossman, M. Taylor, B. H. Hahn, and P. P. Chen. 2006. Antibodies against the activated coagulation factor X (FXa) in the antiphospholipid syndrome that interfere with the FXa inactivation by antithrombin. J. Immunol. 177:8219-8225.
    • (2006) J. Immunol , vol.177 , pp. 8219-8225
    • Yang, Y.H.1    Hwang, K.K.2    Fitz Gerald, J.3    Grossman, J.M.4    Taylor, M.5    Hahn, B.H.6    Chen, P.P.7
  • 96
    • 12344251568 scopus 로고    scopus 로고
    • Inter-subunit disulfide bonds in soluble HIV-1 envelope glycoprotein trimers
    • Yuan, W., S. Craig, X. Yang, and J. Sodroski. 2005. Inter-subunit disulfide bonds in soluble HIV-1 envelope glycoprotein trimers. Virology 332:369-383.
    • (2005) Virology , vol.332 , pp. 369-383
    • Yuan, W.1    Craig, S.2    Yang, X.3    Sodroski, J.4
  • 99
    • 33646744353 scopus 로고    scopus 로고
    • Improving on nature: Focusing the immune response on the V3 loop
    • Zolla-Pazner, S. 2005. Improving on nature: focusing the immune response on the V3 loop. Hum. Antibodies 14:69-72.
    • (2005) Hum. Antibodies , vol.14 , pp. 69-72
    • Zolla-Pazner, S.1
  • 100
    • 38949204965 scopus 로고    scopus 로고
    • HIV-1 neutralization: Mechanisms and relevance to vaccine design
    • Zwick, M. B., and D. R. Burton. 2007. HIV-1 neutralization: mechanisms and relevance to vaccine design. Curr. HIV Res. 5:608-624.
    • (2007) Curr. HIV Res , vol.5 , pp. 608-624
    • Zwick, M.B.1    Burton, D.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.