메뉴 건너뛰기




Volumn 290, Issue 32, 2015, Pages 19780-19795

A new approach to produce HIV-1 envelope trimers: Both cleavage and proper glycosylation are essential to generate authentic trimers

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; DISEASES; GLYCOSYLATION; VACCINES; VIRUSES;

EID: 84939128392     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.656611     Document Type: Article
Times cited : (21)

References (81)
  • 1
    • 84866495323 scopus 로고    scopus 로고
    • Human antibodies that neutralize HIV-1: Identification, structures, and B cell ontogenies
    • Kwong, P. D., and Mascola, J. R. (2012) Human antibodies that neutralize HIV-1: identification, structures, and B cell ontogenies. Immunity 37, 412-425
    • (2012) Immunity , vol.37 , pp. 412-425
    • Kwong, P.D.1    Mascola, J.R.2
  • 2
    • 0035425509 scopus 로고    scopus 로고
    • Vaccines for the prevention of HIV-1 disease
    • Mascola, J. R., and Nabel, G. J. (2001) Vaccines for the prevention of HIV-1 disease. Curr. Opin. Immunol. 13, 489-495
    • (2001) Curr. Opin. Immunol. , vol.13 , pp. 489-495
    • Mascola, J.R.1    Nabel, G.J.2
  • 3
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: Fusogens, antigens, and immunogens
    • Wyatt, R., and Sodroski, J. (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
  • 4
    • 84921606536 scopus 로고    scopus 로고
    • Insights into the trimeric HIV-1 envelope glycoprotein structure
    • Ward, A. B., and Wilson, I. A. (2015) Insights into the trimeric HIV-1 envelope glycoprotein structure. Trends Biochem. Sci. 40, 101-107
    • (2015) Trends Biochem. Sci. , vol.40 , pp. 101-107
    • Ward, A.B.1    Wilson, I.A.2
  • 7
    • 79251526530 scopus 로고    scopus 로고
    • HIV-1 envelope, integrins and co-receptor use in mucosal transmission of HIV
    • Cicala, C., Arthos, J., and Fauci, A. S. (2011) HIV-1 envelope, integrins and co-receptor use in mucosal transmission of HIV. J. Transl. Med. 9, S2
    • (2011) J. Transl. Med. , vol.9 , pp. S2
    • Cicala, C.1    Arthos, J.2    Fauci, A.S.3
  • 8
    • 0021751840 scopus 로고
    • The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus
    • Dalgleish, A. G., Beverley, P. C., Clapham, P. R., Crawford, D. H., Greaves, M. F., and Weiss, R. A. (1984) The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus. Nature 312, 763-767
    • (1984) Nature , vol.312 , pp. 763-767
    • Dalgleish, A.G.1    Beverley, P.C.2    Clapham, P.R.3    Crawford, D.H.4    Greaves, M.F.5    Weiss, R.A.6
  • 9
    • 0022978934 scopus 로고
    • Binding of the human retrovirus HTLV-III/LAV/ARV/HIV to the CD4 (T4) molecule: Conformation dependence, epitope mapping, antibody inhibition, and potential for idiotypic mimicry
    • McDougal, J. S., Nicholson, J. K., Cross, G. D., Cort, S. P., Kennedy, M. S., and Mawle, A. C. (1986) Binding of the human retrovirus HTLV-III/LAV/ARV/HIV to the CD4 (T4) molecule: conformation dependence, epitope mapping, antibody inhibition, and potential for idiotypic mimicry. J. Immunol. 137, 2937-2944
    • (1986) J. Immunol. , vol.137 , pp. 2937-2944
    • McDougal, J.S.1    Nicholson, J.K.2    Cross, G.D.3    Cort, S.P.4    Kennedy, M.S.5    Mawle, A.C.6
  • 11
    • 0030018156 scopus 로고    scopus 로고
    • CC CKR5: A RANTES, MIP-1α, MIP-1β receptor as a fusion cofactor for macrophage-tropic HIV-1
    • Alkhatib, G., Combadiere, C., Broder, C. C., Feng, Y., Kennedy, P. E., Murphy, P. M., and Berger, E. A. (1996) CC CKR5: a RANTES, MIP-1α, MIP-1β receptor as a fusion cofactor for macrophage-tropic HIV-1. Science 272, 1955-1958
    • (1996) Science , vol.272 , pp. 1955-1958
    • Alkhatib, G.1    Combadiere, C.2    Broder, C.C.3    Feng, Y.4    Kennedy, P.E.5    Murphy, P.M.6    Berger, E.A.7
  • 12
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry cofactor: Functional cDNA cloning of a seven-transmembrane, G proteincoupled receptor
    • Feng, Y., Broder, C. C., Kennedy, P. E., and Berger, E. A. (1996) HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G proteincoupled receptor. Science 272, 872-877
    • (1996) Science , vol.272 , pp. 872-877
    • Feng, Y.1    Broder, C.C.2    Kennedy, P.E.3    Berger, E.A.4
  • 13
    • 33747132429 scopus 로고    scopus 로고
    • Biology of CCR5 and its role in HIV infection and treatment
    • Lederman, M. M., Penn-Nicholson, A., Cho, M., and Mosier, D. (2006) Biology of CCR5 and its role in HIV infection and treatment. JAMA 296, 815-826
    • (2006) JAMA , vol.296 , pp. 815-826
    • Lederman, M.M.1    Penn-Nicholson, A.2    Cho, M.3    Mosier, D.4
  • 14
    • 0031959601 scopus 로고    scopus 로고
    • Capture of an early fusion-active conformation of HIV-1 gp41
    • Furuta, R. A., Wild, C. T., Weng, Y., and Weiss, C. D. (1998) Capture of an early fusion-active conformation of HIV-1 gp41. Nat. Struct. Biol. 5, 276-279
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 276-279
    • Furuta, R.A.1    Wild, C.T.2    Weng, Y.3    Weiss, C.D.4
  • 16
    • 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., Moore, J. P., Thali, M., Sodroski, J., Barbas, C. F., 3rd, and Burton, D. R. (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, C.F.5    Burton, D.R.6
  • 18
    • 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, M. B., Jensen, R., Church, S., Wang, M., Stiegler, G., Kunert, R., Katinger, H., and Burton, D. R. (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    Jensen, R.2    Church, S.3    Wang, M.4    Stiegler, G.5    Kunert, R.6    Katinger, H.7    Burton, D.R.8
  • 20
    • 84870689010 scopus 로고    scopus 로고
    • Role of human immunodeficiency virus type 1 envelope structure in the induction of broadly neutralizing antibodies
    • Benjelloun, F., Lawrence, P., Verrier, B., Genin, C., and Paul, S. (2012) Role of human immunodeficiency virus type 1 envelope structure in the induction of broadly neutralizing antibodies. J. Virol. 86, 13152-13163
    • (2012) J. Virol. , vol.86 , pp. 13152-13163
    • Benjelloun, F.1    Lawrence, P.2    Verrier, B.3    Genin, C.4    Paul, S.5
  • 21
    • 84905672117 scopus 로고    scopus 로고
    • Immunologic basis for long HCDR3s in broadly neutralizing antibodies against HIV-1
    • Yu, L., and Guan, Y. (2014) Immunologic basis for long HCDR3s in broadly neutralizing antibodies against HIV-1. Front. Immunol. 5, 250
    • (2014) Front. Immunol. , vol.5 , pp. 250
    • Yu, L.1    Guan, Y.2
  • 22
    • 84880714310 scopus 로고    scopus 로고
    • A brief history of the global effort to develop a preventive HIV vaccine
    • Esparza, J. (2013) A brief history of the global effort to develop a preventive HIV vaccine. Vaccine 31, 3502-3518
    • (2013) Vaccine , vol.31 , pp. 3502-3518
    • Esparza, J.1
  • 31
    • 84903173697 scopus 로고    scopus 로고
    • Differential binding of neutralizing and non-neutralizing antibodies to native-like soluble HIV-1 Env trimers, uncleaved Env proteins, and monomeric subunits
    • Yasmeen, A., Ringe, R., Derking, R., Cupo, A., Julien, J. P., Burton, D. R., Ward, A. B., Wilson, I. A., Sanders, R. W., Moore, J. P., and Klasse, P. J. (2014) Differential binding of neutralizing and non-neutralizing antibodies to native-like soluble HIV-1 Env trimers, uncleaved Env proteins, and monomeric subunits. Retrovirology 11, 41
    • (2014) Retrovirology , vol.11 , pp. 41
    • Yasmeen, A.1    Ringe, R.2    Derking, R.3    Cupo, A.4    Julien, J.P.5    Burton, D.R.6    Ward, A.B.7    Wilson, I.A.8    Sanders, R.W.9    Moore, J.P.10    Klasse, P.J.11
  • 34
    • 84876065936 scopus 로고    scopus 로고
    • In vitro and in vivo delivery of genes and proteins using the bacteriophage T4 DNA packaging machine
    • Tao, P., Mahalingam, M., Marasa, B. S., Zhang, Z., Chopra, A. K., and Rao, V. B. (2013) In vitro and in vivo delivery of genes and proteins using the bacteriophage T4 DNA packaging machine. Proc. Natl. Acad. Sci. U.S.A. 110, 5846-5851
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 5846-5851
    • Tao, P.1    Mahalingam, M.2    Marasa, B.S.3    Zhang, Z.4    Chopra, A.K.5    Rao, V.B.6
  • 35
    • 33746190697 scopus 로고    scopus 로고
    • Assembly of human immunodeficiency virus (HIV) antigens on bacteriophage T4: A novel in vitro approach to construct multicomponent HIV vaccines
    • Sathaliyawala, T., Rao, M., Maclean, D. M., Birx, D. L., Alving, C. R., and Rao, V. B. (2006) Assembly of human immunodeficiency virus (HIV) antigens on bacteriophage T4: a novel in vitro approach to construct multicomponent HIV vaccines. J. Virol. 80, 7688-7698
    • (2006) J. Virol. , vol.80 , pp. 7688-7698
    • Sathaliyawala, T.1    Rao, M.2    Maclean, D.M.3    Birx, D.L.4    Alving, C.R.5    Rao, V.B.6
  • 38
  • 40
    • 0032849335 scopus 로고    scopus 로고
    • Determinants of neutralization resistance in the envelope glycoproteins of a simian-human immunodeficiency virus passaged in vivo
    • Etemad-Moghadam, B., Sun, Y., Nicholson, E. K., Karlsson, G. B., Schenten, D., and Sodroski, J. (1999) Determinants of neutralization resistance in the envelope glycoproteins of a simian-human immunodeficiency virus passaged in vivo. J. Virol. 73, 8873-8879
    • (1999) J. Virol. , vol.73 , pp. 8873-8879
    • Etemad-Moghadam, B.1    Sun, Y.2    Nicholson, E.K.3    Karlsson, G.B.4    Schenten, D.5    Sodroski, J.6
  • 43
    • 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., Emes, C. L., Wisnewski, A. V., Power, J., Lewis, G., Montefiori, D., and Posner, M. R. (1998) Functional and molecular characterization of human monoclonal antibody reactive with the immunodominant region of HIV type 1 glycoprotein 41. AIDS Res. Hum. Retroviruses 14, 1271-1280
    • (1998) AIDS Res. Hum. Retroviruses , 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
  • 44
    • 0023631843 scopus 로고
    • The construction and use of a human-mouse myeloma analogue suitable for the routine production of hybridomas secreting human monoclonal antibodies
    • Posner, M. R., Elboim, H., and Santos, D. (1987) The construction and use of a human-mouse myeloma analogue suitable for the routine production of hybridomas secreting human monoclonal antibodies. Hybridoma 6, 611-625
    • (1987) Hybridoma , vol.6 , pp. 611-625
    • Posner, M.R.1    Elboim, H.2    Santos, D.3
  • 45
    • 0026001658 scopus 로고
    • An IgG human monoclonal antibody that reacts with HIV-1/GP120, inhibits virus binding to cells, and neutralizes infection
    • Posner, M. R., Hideshima, T., Cannon, T., Mukherjee, M., Mayer, K. H., and Byrn, R. A. (1991) An IgG human monoclonal antibody that reacts with HIV-1/GP120, inhibits virus binding to cells, and neutralizes infection. J. Immunol. 146, 4325-4332
    • (1991) J. Immunol. , vol.146 , pp. 4325-4332
    • Posner, M.R.1    Hideshima, T.2    Cannon, T.3    Mukherjee, M.4    Mayer, K.H.5    Byrn, R.A.6
  • 46
    • 0027458347 scopus 로고
    • Neutralization of HIV-1 by F105, a human monoclonal antibody to the CD4 binding site of gp120
    • Posner, M. R., Cavacini, L. A., Emes, C. L., Power, J., and Byrn, R. (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
  • 47
    • 0027508536 scopus 로고
    • Loss of serum antibodies to a conformational epitope of HIV-1/gp120 identified by a human monoclonal antibody is associated with disease progression
    • Cavacini, L. A., Emes, C. L., Power, J., Underdahl, J., Goldstein, R., Mayer, K., and Posner, M. R. (1993) Loss of serum antibodies to a conformational epitope of HIV-1/gp120 identified by a human monoclonal antibody is associated with disease progression. J. Acquir. Immune Defic. Syndr. 6, 1093-1102
    • (1993) J. Acquir. Immune Defic. Syndr. , vol.6 , pp. 1093-1102
    • Cavacini, L.A.1    Emes, C.L.2    Power, J.3    Underdahl, J.4    Goldstein, R.5    Mayer, K.6    Posner, M.R.7
  • 49
    • 0036231093 scopus 로고    scopus 로고
    • Highly stable trimers formed by human immunodeficiency virus type 1 envelope glycoproteins fused with the trimeric motif of T4 bacteriophage fibritin
    • Yang, X., Lee, J., Mahony, E. M., Kwong, P. D., Wyatt, R., and Sodroski, J. (2002) Highly stable trimers formed by human immunodeficiency virus type 1 envelope glycoproteins fused with the trimeric motif of T4 bacteriophage fibritin. J. Virol. 76, 4634-4642
    • (2002) J. Virol. , vol.76 , pp. 4634-4642
    • Yang, X.1    Lee, J.2    Mahony, E.M.3    Kwong, P.D.4    Wyatt, R.5    Sodroski, J.6
  • 50
    • 0033985999 scopus 로고    scopus 로고
    • A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure
    • Binley, J. M., Sanders, R. W., Clas, B., Schuelke, N., Master, A., Guo, Y., Kajumo, F., Anselma, D. J., Maddon, P. J., Olson, W. C., and Moore, J. P. (2000) A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure. J. Virol. 74, 627-643
    • (2000) J. Virol. , vol.74 , pp. 627-643
    • Binley, J.M.1    Sanders, R.W.2    Clas, B.3    Schuelke, N.4    Master, A.5    Guo, Y.6    Kajumo, F.7    Anselma, D.J.8    Maddon, P.J.9    Olson, W.C.10    Moore, J.P.11
  • 52
    • 33847293391 scopus 로고    scopus 로고
    • Specific amino acids in the N-terminus of the gp41 ectodomain contribute to the stabilization of a soluble, cleaved gp140 envelope glycoprotein from human immunodeficiency virus type 1
    • Dey, A. K., David, K. B., Klasse, P. J., and Moore, J. P. (2007) Specific amino acids in the N-terminus of the gp41 ectodomain contribute to the stabilization of a soluble, cleaved gp140 envelope glycoprotein from human immunodeficiency virus type 1. Virology 360, 199-208
    • (2007) Virology , vol.360 , pp. 199-208
    • Dey, A.K.1    David, K.B.2    Klasse, P.J.3    Moore, J.P.4
  • 56
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • Higuchi, R., Krummel, B., and Saiki, R. K. (1988) A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. Nucleic Acids Res. 16, 7351-7367
    • (1988) Nucleic Acids Res. , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 57
    • 0028784138 scopus 로고
    • Single-step assembly of a gene and entire plasmid from large numbers of oligodeoxyribonucleotides
    • Stemmer, W. P., Crameri, A., Ha, K. D., Brennan, T. M., and Heyneker, H. L. (1995) Single-step assembly of a gene and entire plasmid from large numbers of oligodeoxyribonucleotides. Gene 164, 49-53
    • (1995) Gene , vol.164 , pp. 49-53
    • Stemmer, W.P.1    Crameri, A.2    Ha, K.D.3    Brennan, T.M.4    Heyneker, H.L.5
  • 58
    • 0037109080 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: A tetracycline-inducible system in stable mammalian cell lines for high-level expression of opsin mutants
    • Reeves, P. J., Kim, J. M., and Khorana, H. G. (2002) Structure and function in rhodopsin: a tetracycline-inducible system in stable mammalian cell lines for high-level expression of opsin mutants. Proc. Natl. Acad. Sci. U.S.A. 99, 13413-13418
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 13413-13418
    • Reeves, P.J.1    Kim, J.M.2    Khorana, H.G.3
  • 61
    • 84928523302 scopus 로고    scopus 로고
    • Single-chain soluble BG505.SOSIP gp140 trimers as structural and antigenic mimics of mature closed HIV-1 Env
    • Georgiev, I. S., Joyce, M. G., Yang, Y., Sastry, M., Zhang, B., Baxa, U., Chen, R. E., Druz, A., Lees, C. R., Narpala, S., Schön, A., Van Galen, J., Chuang, G. Y., Gorman, J., Harned, A., Pancera, M., Stewart-Jones, G. B., Cheng, C., Freire, E., McDermott, A. B., Mascola, J. R., and Kwong, P. D. (2015) Single-chain soluble BG505.SOSIP gp140 trimers as structural and antigenic mimics of mature closed HIV-1 Env. J. Virol. 89, 5318-5329
    • (2015) J. Virol. , vol.89 , pp. 5318-5329
    • Georgiev, I.S.1    Joyce, M.G.2    Yang, Y.3    Sastry, M.4    Zhang, B.5    Baxa, U.6    Chen, R.E.7    Druz, A.8    Lees, C.R.9    Narpala, S.10
  • 66
    • 0036637385 scopus 로고    scopus 로고
    • The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120
    • Sanders, R. W., Venturi, M., Schiffner, L., Kalyanaraman, R., Katinger, H., Lloyd, K. O., Kwong, P. D., and Moore, J. P. (2002) The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120. J. Virol. 76, 7293-7305
    • (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
  • 67
    • 84921564277 scopus 로고    scopus 로고
    • Structure of 2G12 Fab2 in complex with soluble and fully glycosylated HIV-1 Env by negative-stain single-particle electron microscopy
    • Murin, C. D., Julien, J. P., Sok, D., Stanfield, R. L., Khayat, R., Cupo, A., Moore, J. P., Burton, D. R., Wilson, I. A., and Ward, A. B. (2014) Structure of 2G12 Fab2 in complex with soluble and fully glycosylated HIV-1 Env by negative-stain single-particle electron microscopy. J. Virol. 88, 10177-10188
    • (2014) J. Virol. , vol.88 , pp. 10177-10188
    • Murin, C.D.1    Julien, J.P.2    Sok, D.3    Stanfield, R.L.4    Khayat, R.5    Cupo, A.6    Moore, J.P.7    Burton, D.R.8    Wilson, I.A.9    Ward, A.B.10
  • 68
    • 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 Wyatt, R. (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
  • 69
    • 84900467984 scopus 로고    scopus 로고
    • Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers
    • Blattner, C., Lee, J. H., Sliepen, K., Derking, R., Falkowska, E., de la Peña, A. T., Cupo, A., Julien, J. P., van Gils, M., Lee, P. S., Peng, W., Paulson, J. C., Poignard, P., Burton, D. R., Moore, J. P., Sanders, R. W., Wilson, I. A., and Ward, A. B. (2014) Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers. Immunity 40, 669-680
    • (2014) Immunity , vol.40 , pp. 669-680
    • Blattner, C.1    Lee, J.H.2    Sliepen, K.3    Derking, R.4    Falkowska, E.5
  • 73
    • 0026801056 scopus 로고
    • Discontinuous, conserved neutralization epitopes overlapping the CD4-binding region of human immunodeficiency virus type 1 gp120 envelope glycoprotein
    • Thali, M., Furman, C., Ho, D. D., Robinson, J., Tilley, S., Pinter, A., and Sodroski, J. (1992) Discontinuous, conserved neutralization epitopes overlapping the CD4-binding region of human immunodeficiency virus type 1 gp120 envelope glycoprotein. J. Virol. 66, 5635-5641
    • (1992) J. Virol. , vol.66 , pp. 5635-5641
    • Thali, M.1    Furman, C.2    Ho, D.D.3    Robinson, J.4    Tilley, S.5    Pinter, A.6    Sodroski, J.7
  • 75
    • 0037032903 scopus 로고    scopus 로고
    • Interactions of human antibodies, epitope exposure, antibody binding and neutralization of primary isolate HIV-1 virions
    • Cavacini, L. A., Duval, M., Robinson, J., and Posner, M. R. (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
  • 76
    • 84923850343 scopus 로고    scopus 로고
    • Well-ordered trimeric HIV-1 subtype B and C soluble spike mimetics generated by negative selection display native-like properties
    • Guenaga, J., de Val, N., Tran, K., Feng, Y., Satchwell, K., Ward, A. B., and Wyatt, R. T. (2015) Well-ordered trimeric HIV-1 subtype B and C soluble spike mimetics generated by negative selection display native-like properties. PLoS Pathog. 11, e1004570
    • (2015) PLoS Pathog. , vol.11 , pp. e1004570
    • Guenaga, J.1    De Val, N.2    Tran, K.3    Feng, Y.4    Satchwell, K.5    Ward, A.B.6    Wyatt, R.T.7
  • 77
    • 80051737642 scopus 로고    scopus 로고
    • HIV-1 envelope glycoprotein biosynthesis, trafficking, and incorporation
    • Checkley, M. A., Luttge, B. G., and Freed, E. O. (2011) HIV-1 envelope glycoprotein biosynthesis, trafficking, and incorporation. J. Mol. Biol. 410, 582-608
    • (2011) J. Mol. Biol. , vol.410 , pp. 582-608
    • Checkley, M.A.1    Luttge, B.G.2    Freed, E.O.3
  • 78
    • 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., Oh, K. J., Kim, M., Yu, J., Brusic, V., Song, L., Qiao, Z., Wang, J. H., Wagner, G., and Reinherz, E. L. (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
  • 79
    • 84890196626 scopus 로고    scopus 로고
    • Prefusion structure of trimeric HIV-1 envelope glycoprotein determined by cryo-electron microscopy
    • Bartesaghi, A., Merk, A., Borgnia, M. J., Milne, J. L., and Subramaniam, S. (2013) Prefusion structure of trimeric HIV-1 envelope glycoprotein determined by cryo-electron microscopy. Nat. Struct. Mol. Biol. 20, 1352-1357
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 1352-1357
    • Bartesaghi, A.1    Merk, A.2    Borgnia, M.J.3    Milne, J.L.4    Subramaniam, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.