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Volumn 84, Issue 3, 2010, Pages 1513-1526

Protease cleavage sites in HIV-1 gp120 recognized by antigen processing enzymes are conserved and located at receptor binding sites

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN D; CATHEPSIN L; CATHEPSIN S; CD4 ANTIGEN; IMMUNOGLOBULIN G; NEUTRALIZING ANTIBODY; RECOMBINANT GLYCOPROTEIN GP 120;

EID: 73949101842     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.01765-09     Document Type: Article
Times cited : (22)

References (105)
  • 1
    • 0029871010 scopus 로고    scopus 로고
    • Molecular analysis of presentation by HLA-A2.1 of a promiscuously binding V3 loop peptide from the HIV-envelope protein to human cytotoxic T lymphocytes
    • Alexander-Miller, M. A., K. C. Parker, T. Tsukui, C. D. Pendleton, J. E. Coligan, and J. A. Berzofsky. 1996. Molecular analysis of presentation by HLA-A2.1 of a promiscuously binding V3 loop peptide from the HIV-envelope protein to human cytotoxic T lymphocytes. Int. Immunol. 8:641-649.
    • (1996) Int. Immunol , vol.8 , pp. 641-649
    • Alexander-Miller, M.A.1    Parker, K.C.2    Tsukui, T.3    Pendleton, C.D.4    Coligan, J.E.5    Berzofsky, J.A.6
  • 3
    • 33947590277 scopus 로고    scopus 로고
    • A comparative immunogenicity study in rabbits of disulfide-stabilized, proteolytically cleaved, soluble trimeric human immunodeficiency virus type 1 gp140, trimeric cleavage-defective gp140 and monomeric gp120
    • Beddows, S., M. Franti, A. K. Dey, M. Kirschner, S. P. Iyer, D. C. Fisch, T. Ketas, E. Yuste, R. C. Desrosiers, P. J. Klasse, P. J. Maddon, W. C. Olson, and J. P. Moore. 2007. A comparative immunogenicity study in rabbits of disulfide-stabilized, proteolytically cleaved, soluble trimeric human immunodeficiency virus type 1 gp140, trimeric cleavage-defective gp140 and monomeric gp120. Virology 360:329-340.
    • (2007) Virology , vol.360 , pp. 329-340
    • Beddows, S.1    Franti, M.2    Dey, A.K.3    Kirschner, M.4    Iyer, S.P.5    Fisch, D.C.6    Ketas, T.7    Yuste, E.8    Desrosiers, R.C.9    Klasse, P.J.10    Maddon, P.J.11    Olson, W.C.12    Moore, J.P.13
  • 5
    • 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 virionassociated structure
    • Binley, J. M., R. W. Sanders, B. Clas, N. Schuelke, A. Master, Y. Guo, F. Kajumo, D. J. Anselma, P. J. Maddon, W. C. Olson, and J. P. Moore. 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 virionassociated 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
  • 6
    • 0011720253 scopus 로고
    • Role for intracellular proteases in the processing and transport of class II HLA antigens
    • Blum, J. S., and P. Cresswell. 1988. Role for intracellular proteases in the processing and transport of class II HLA antigens. Proc. Natl. Acad. Sci. USA 85:3975-3979.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3975-3979
    • Blum, J.S.1    Cresswell, P.2
  • 7
    • 0028146788 scopus 로고
    • Cryptic nature of envelope V3 region epitopes protects primary monocytotropic human immunodeficiency virus type 1 from antibody neutralization
    • Bou-Habib, D. C., G. Roderiquez, T. Oravecz, P. W. Berman, P. Lusso, and M. A. Norcross. 1994. Cryptic nature of envelope V3 region epitopes protects primary monocytotropic human immunodeficiency virus type 1 from antibody neutralization. J. Virol. 68:6006-6013.
    • (1994) J. Virol , vol.68 , pp. 6006-6013
    • Bou-Habib, D.C.1    Roderiquez, G.2    Oravecz, T.3    Berman, P.W.4    Lusso, P.5    Norcross, M.A.6
  • 16
    • 30044444910 scopus 로고    scopus 로고
    • Endosomal proteases in antigen presentation
    • Chapman, H. A. 2006. Endosomal proteases in antigen presentation. Curr. Opin. Immunol. 18:78-84.
    • (2006) Curr. Opin. Immunol , vol.18 , pp. 78-84
    • Chapman, H.A.1
  • 17
    • 0025755463 scopus 로고
    • Expression of cathepsin L in human tumors
    • Chauhan, S. S., L. J. Goldstein, and M. M. Gottesman. 1991. Expression of cathepsin L in human tumors. Cancer Res. 51:1478-1481.
    • (1991) Cancer Res , vol.51 , pp. 1478-1481
    • Chauhan, S.S.1    Goldstein, L.J.2    Gottesman, M.M.3
  • 18
    • 3142741003 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 evades T-helper responses by exploiting antibodies that suppress antigen processing
    • Chien, P. C., Jr., S. Cohen, M. Tuen, J. Arthos, P. D. Chen, S. Patel, and C. E. Hioe. 2004. Human immunodeficiency virus type 1 evades T-helper responses by exploiting antibodies that suppress antigen processing. J. Virol. 78:7645-7652.
    • (2004) J. Virol , vol.78 , pp. 7645-7652
    • Chien Jr., P.C.1    Cohen, S.2    Tuen, M.3    Arthos, J.4    Chen, P.D.5    Patel, S.6    Hioe, C.E.7
  • 19
    • 33744961634 scopus 로고    scopus 로고
    • Substrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique speci-ficities
    • Choe, Y., F. Leonetti, D. C. Greenbaum, F. Lecaille, M. Bogyo, D. Bromme, J. A. Ellman, and C. S. Craik. 2006. Substrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique speci-ficities. J. Biol. Chem. 281:12824-12832.
    • (2006) J. Biol. Chem , vol.281 , pp. 12824-12832
    • Choe, Y.1    Leonetti, F.2    Greenbaum, D.C.3    Lecaille, F.4    Bogyo, M.5    Bromme, D.6    Ellman, J.A.7    Craik, C.S.8
  • 21
    • 0029955497 scopus 로고    scopus 로고
    • The V3 domain of the HIV-1 gp120 envelope glycoprotein is critical for chemokine-mediated blockade of infection
    • Cocchi, F., A. L. DeVico, A. Garzino-Demo, A. Cara, R. C. Gallo, and P. Lusso. 1996. The V3 domain of the HIV-1 gp120 envelope glycoprotein is critical for chemokine-mediated blockade of infection. Nat. Med. 2:1244-1247.
    • (1996) Nat. Med , vol.2 , pp. 1244-1247
    • Cocchi, F.1    DeVico, A.L.2    Garzino-Demo, A.3    Cara, A.4    Gallo, R.C.5    Lusso, P.6
  • 22
    • 36249005448 scopus 로고    scopus 로고
    • AIDS research. Did Merck's failed HIV vaccine cause harm?
    • Cohen, J. 2007. AIDS research. Did Merck's failed HIV vaccine cause harm? Science 318:1048-1049.
    • (2007) Science , vol.318 , pp. 1048-1049
    • Cohen, J.1
  • 23
    • 35148818748 scopus 로고    scopus 로고
    • AIDS research. Promising AIDS vaccine's failure leaves field reeling
    • Cohen, J. 2007. AIDS research. Promising AIDS vaccine's failure leaves field reeling. Science 318:28-29.
    • (2007) Science , vol.318 , pp. 28-29
    • Cohen, J.1
  • 26
    • 67249085575 scopus 로고    scopus 로고
    • Dey, B., K. Svehla, L. Xu, D. Wycuff, T. Zhou, G. Voss, A. Phogat, B. K. Chakrabarti, Y. Li, G. Shaw, P. D. Kwong, G. J. Nabel, J. R. Mascola, and R. T. Wyatt. 2009. Structure-based stabilization of HIV-1 gp120 enhances humoral immune responses to the induced co-receptor binding site. PLoS Pathog. 5:e1000445.
    • Dey, B., K. Svehla, L. Xu, D. Wycuff, T. Zhou, G. Voss, A. Phogat, B. K. Chakrabarti, Y. Li, G. Shaw, P. D. Kwong, G. J. Nabel, J. R. Mascola, and R. T. Wyatt. 2009. Structure-based stabilization of HIV-1 gp120 enhances humoral immune responses to the induced co-receptor binding site. PLoS Pathog. 5:e1000445.
  • 27
    • 32944477067 scopus 로고    scopus 로고
    • The rational design of an AIDS vaccine
    • Douek, D. C., P. D. Kwong, and G. J. Nabel. 2006. The rational design of an AIDS vaccine. Cell 124:677-681.
    • (2006) Cell , vol.124 , pp. 677-681
    • Douek, D.C.1    Kwong, P.D.2    Nabel, G.J.3
  • 32
    • 13944254982 scopus 로고    scopus 로고
    • Placebo-controlled phase 3 trial of a recombinant glycoprotein 120 vaccine to prevent HIV-1 infection
    • Flynn, N. M., D. N. Forthal, C. D. Harro, F. N. Judson, K. H. Mayer, and M. F. Para. 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    Forthal, D.N.2    Harro, C.D.3    Judson, F.N.4    Mayer, K.H.5    Para, M.F.6
  • 33
    • 73949085495 scopus 로고    scopus 로고
    • Frahm, N., B. Baker, and C. Brander. 2008. Identification and optimal definition of HIV-derived cytotoxic lymphocyte (CTL) epitopes for the study of CTL escape, functional avidity and viral evolution, p. 3-24. In B. Korber, C. Brander, B. Haynes, R. Koup, J. Moore, B. Walker, and B. A. Watkins (ed.), HIV molecular immunology 2008. Los Alamos National Laboratory, Theoretical Biology and Biophysics, Los Alamos, NM.
    • Frahm, N., B. Baker, and C. Brander. 2008. Identification and optimal definition of HIV-derived cytotoxic lymphocyte (CTL) epitopes for the study of CTL escape, functional avidity and viral evolution, p. 3-24. In B. Korber, C. Brander, B. Haynes, R. Koup, J. Moore, B. Walker, and B. A. Watkins (ed.), HIV molecular immunology 2008. Los Alamos National Laboratory, Theoretical Biology and Biophysics, Los Alamos, NM.
  • 34
  • 35
    • 0033233121 scopus 로고    scopus 로고
    • HLA-A*1101-restricted cytotoxic T lymphocyte recognition for a novel epitope derived from the HIV-1 Env protein
    • Fukada, K., H. Tomiyama, Y. Chujoh, K. Miwa, Y. Kaneko, S. Oka, and M. Takiguchi. 1999. HLA-A*1101-restricted cytotoxic T lymphocyte recognition for a novel epitope derived from the HIV-1 Env protein. AIDS 13: 2597-2599.
    • (1999) AIDS , vol.13 , pp. 2597-2599
    • Fukada, K.1    Tomiyama, H.2    Chujoh, Y.3    Miwa, K.4    Kaneko, Y.5    Oka, S.6    Takiguchi, M.7
  • 36
    • 0026595148 scopus 로고
    • Identification and characterization of a neutralization site within the second variable region of human immunode-ficiency virus type 1 gp120
    • Fung, M. S., C. R. Sun, W. L. Gordon, R. S. Liou, T. W. Chang, W. N. Sun, E. S. Daar, and D. D. Ho. 1992. Identification and characterization of a neutralization site within the second variable region of human immunode-ficiency virus type 1 gp120. J. Virol. 66:848-856.
    • (1992) J. Virol , vol.66 , pp. 848-856
    • Fung, M.S.1    Sun, C.R.2    Gordon, W.L.3    Liou, R.S.4    Chang, T.W.5    Sun, W.N.6    Daar, E.S.7    Ho, D.D.8
  • 37
    • 0026032735 scopus 로고
    • Enzyme-linked immunoassay for human immunodeficiency virus type 1 envelope glycoprotein 120
    • Gilbert, M., J. Kirihara, and J. Mills. 1991. Enzyme-linked immunoassay for human immunodeficiency virus type 1 envelope glycoprotein 120. J. Clin. Microbiol. 29:142-147.
    • (1991) J. Clin. Microbiol , vol.29 , pp. 142-147
    • Gilbert, M.1    Kirihara, J.2    Mills, J.3
  • 38
    • 12444296516 scopus 로고    scopus 로고
    • Long-term safety analysis of preventive HIV-1 vaccines evaluated in AIDS vaccine evaluation group NIAID-sponsored phase I and II clinical trials
    • Gilbert, P. B., Y. L. Chiu, M. Allen, D. N. Lawrence, C. Chapdu, H. Israel, D. Holman, M. C. Keefer, M. Wolff, and S. E. Frey. 2003. Long-term safety analysis of preventive HIV-1 vaccines evaluated in AIDS vaccine evaluation group NIAID-sponsored phase I and II clinical trials. Vaccine 21:2933-2947.
    • (2003) Vaccine , vol.21 , pp. 2933-2947
    • Gilbert, P.B.1    Chiu, Y.L.2    Allen, M.3    Lawrence, D.N.4    Chapdu, C.5    Israel, H.6    Holman, D.7    Keefer, M.C.8    Wolff, M.9    Frey, S.E.10
  • 40
    • 7544236606 scopus 로고    scopus 로고
    • Factors limiting the immunogenicity of HIV-1 gp120 envelope glycoproteins
    • Grundner, C., M. Pancera, J. M. Kang, M. Koch, J. Sodroski, and R. Wyatt. 2004. Factors limiting the immunogenicity of HIV-1 gp120 envelope glycoproteins. Virology 330:233-248.
    • (2004) Virology , vol.330 , pp. 233-248
    • Grundner, C.1    Pancera, M.2    Kang, J.M.3    Koch, M.4    Sodroski, J.5    Wyatt, R.6
  • 41
    • 0023885197 scopus 로고    scopus 로고
    • Gurgo, C., H. G. Guo, G. Franchini, A. Aldovini, E. Collalti, K. Farrell, F. Wong-Staal, R. C. Gallo, and M. S. Reitz, Jr. 1988. Envelope sequences of two new United States HIV-1 isolates. Virology 164:531-536.
    • Gurgo, C., H. G. Guo, G. Franchini, A. Aldovini, E. Collalti, K. Farrell, F. Wong-Staal, R. C. Gallo, and M. S. Reitz, Jr. 1988. Envelope sequences of two new United States HIV-1 isolates. Virology 164:531-536.
  • 42
    • 0029880783 scopus 로고    scopus 로고
    • Cytotoxic T lymphocytes in asymptomatic long-term nonprogressing HIV-1 infection. Breadth and specificity of the response and relation to in vivo viral quasispecies in a person with prolonged infection and low viral load
    • Harrer, T., E. Harrer, S. A. Kalams, P. Barbosa, A. Trocha, R. P. Johnson, T. Elbeik, M. B. Feinberg, S. P. Buchbinder, and B. D. Walker. 1996. Cytotoxic T lymphocytes in asymptomatic long-term nonprogressing HIV-1 infection. Breadth and specificity of the response and relation to in vivo viral quasispecies in a person with prolonged infection and low viral load. J. Immunol. 156:2616-2623.
    • (1996) J. Immunol , vol.156 , pp. 2616-2623
    • Harrer, T.1    Harrer, E.2    Kalams, S.A.3    Barbosa, P.4    Trocha, A.5    Johnson, R.P.6    Elbeik, T.7    Feinberg, M.B.8    Buchbinder, S.P.9    Walker, B.D.10
  • 43
    • 33750324765 scopus 로고    scopus 로고
    • Aiming to induce broadly reactive neutralizing antibody responses with HIV-1 vaccine candidates
    • Haynes, B., and D. Montefiori. 2006. Aiming to induce broadly reactive neutralizing antibody responses with HIV-1 vaccine candidates. Expert Rev. Vaccines 5:579-595.
    • (2006) Expert Rev. Vaccines , vol.5 , pp. 579-595
    • Haynes, B.1    Montefiori, D.2
  • 44
    • 0037087364 scopus 로고    scopus 로고
    • A role for cathepsin L and cathepsin S in peptide generation for MHC class II presentation
    • Hsieh, C. S., P. deRoos, K. Honey, C. Beers, and A. Y. Rudensky. 2002. A role for cathepsin L and cathepsin S in peptide generation for MHC class II presentation. J. Immunol. 168:2618-2625.
    • (2002) J. Immunol , vol.168 , pp. 2618-2625
    • Hsieh, C.S.1    deRoos, P.2    Honey, K.3    Beers, C.4    Rudensky, A.Y.5
  • 45
    • 26244445000 scopus 로고    scopus 로고
    • The lysosomal cysteine proteases in MHC class II antigen presentation
    • Hsing, L. C., and A. Y. Rudensky. 2005. The lysosomal cysteine proteases in MHC class II antigen presentation. Immunol. Rev. 207:229-241.
    • (2005) Immunol. Rev , vol.207 , pp. 229-241
    • Hsing, L.C.1    Rudensky, A.Y.2
  • 46
    • 38949170716 scopus 로고    scopus 로고
    • Prospects of HIV Env modification as an approach to HIV vaccine design
    • Hu, S. L., and L. Stamatatos. 2007. Prospects of HIV Env modification as an approach to HIV vaccine design. Curr. HIV Res. 5:507-513.
    • (2007) Curr. HIV Res , vol.5 , pp. 507-513
    • Hu, S.L.1    Stamatatos, L.2
  • 50
    • 34249068954 scopus 로고    scopus 로고
    • An HIV vaccine-evolving concepts
    • Johnston, M. I., and A. S. Fauci. 2007. An HIV vaccine-evolving concepts. N. Engl. J. Med. 356:2073-2081.
    • (2007) N. Engl. J. Med , vol.356 , pp. 2073-2081
    • Johnston, M.I.1    Fauci, A.S.2
  • 52
    • 13744252890 scopus 로고    scopus 로고
    • MAFFT version 5: Improvement in accuracy of multiple sequence alignment
    • Katoh, K., K. Kuma, H. Toh, and T. Miyata. 2005. MAFFT version 5: improvement in accuracy of multiple sequence alignment. Nucleic Acids Res. 33:511-518.
    • (2005) Nucleic Acids Res , vol.33 , pp. 511-518
    • Katoh, K.1    Kuma, K.2    Toh, H.3    Miyata, T.4
  • 53
    • 44649102135 scopus 로고    scopus 로고
    • Keele, B. F., E. E. Giorgi, J. F. Salazar-Gonzalez, J. M. Decker, K. T. Pham, M. G. Salazar, C. Sun, T. Grayson, S. Wang, H. Li, X. Wei, C. Jiang, J. L. Kirchherr, F. Gao, J. A. Anderson, L. H. Ping, R. Swanstrom, G. D. Tomaras, W. A. Blattner, P. A. Goepfert, J. M. Kilby, M. S. Saag, E. L. Delwart, M. P. Busch, M. S. Cohen, D. C. Montefiori, B. F. Haynes, B. Gaschen, G. S. Athreya, H. Y. Lee, N. Wood, C. Seoighe, A. S. Perelson, T. Bhattacharya, B. T. Korber, B. H. Hahn, and G. M. Shaw. 2008. Identifi-cation and characterization of transmitted and early founder virus envelopes in primary HIV-1 infection. Proc. Natl. Acad. Sci. USA 105:7552-7557.
    • Keele, B. F., E. E. Giorgi, J. F. Salazar-Gonzalez, J. M. Decker, K. T. Pham, M. G. Salazar, C. Sun, T. Grayson, S. Wang, H. Li, X. Wei, C. Jiang, J. L. Kirchherr, F. Gao, J. A. Anderson, L. H. Ping, R. Swanstrom, G. D. Tomaras, W. A. Blattner, P. A. Goepfert, J. M. Kilby, M. S. Saag, E. L. Delwart, M. P. Busch, M. S. Cohen, D. C. Montefiori, B. F. Haynes, B. Gaschen, G. S. Athreya, H. Y. Lee, N. Wood, C. Seoighe, A. S. Perelson, T. Bhattacharya, B. T. Korber, B. H. Hahn, and G. M. Shaw. 2008. Identifi-cation and characterization of transmitted and early founder virus envelopes in primary HIV-1 infection. Proc. Natl. Acad. Sci. USA 105:7552-7557.
  • 54
    • 54449094603 scopus 로고    scopus 로고
    • Human cytomegalovirus infection interferes with major histocompatibility complex type II maturation and endocytic proteases in dendritic cells at multiple levels
    • Kessler, T., M. Reich, G. Jahn, E. Tolosa, A. Beck, H. Kalbacher, H. Overkleeft, S. Schempp, and C. Driessen. 2008. Human cytomegalovirus infection interferes with major histocompatibility complex type II maturation and endocytic proteases in dendritic cells at multiple levels. J. Gen. Virol. 89:2427-2436.
    • (2008) J. Gen. Virol , vol.89 , pp. 2427-2436
    • Kessler, T.1    Reich, M.2    Jahn, G.3    Tolosa, E.4    Beck, A.5    Kalbacher, H.6    Overkleeft, H.7    Schempp, S.8    Driessen, C.9
  • 55
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong, P. D., R. Wyatt, J. Robinson, R. W. Sweet, J. Sodroski, and W. A. Hendrickson. 1998. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393:648-659.
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 56
    • 0023651341 scopus 로고
    • Delineation of a region of the human immunodeficiency virus type 1 gp120 glycoprotein critical for interaction with the CD4 receptor
    • Lasky, L. A., G. Nakamura, D. H. Smith, C. Fennie, C. Shimasaki, E. Patzer, P. Berman, T. Gregory, and D. J. Capon. 1987. Delineation of a region of the human immunodeficiency virus type 1 gp120 glycoprotein critical for interaction with the CD4 receptor. Cell 50:975-985.
    • (1987) Cell , vol.50 , pp. 975-985
    • Lasky, L.A.1    Nakamura, G.2    Smith, D.H.3    Fennie, C.4    Shimasaki, C.5    Patzer, E.6    Berman, P.7    Gregory, T.8    Capon, D.J.9
  • 57
    • 0030837038 scopus 로고    scopus 로고
    • Selective induction of the secretion of cathepsins B and L by cytokines in synovial fibroblast-like cells
    • Lemaire, R., G. Huet, F. Zerimech, G. Grard, C. Fontaine, B. Duquesnoy, and R. M. Flipo. 1997. Selective induction of the secretion of cathepsins B and L by cytokines in synovial fibroblast-like cells. Br. J. Rheumatol. 36: 735-743.
    • (1997) Br. J. Rheumatol , vol.36 , pp. 735-743
    • Lemaire, R.1    Huet, G.2    Zerimech, F.3    Grard, G.4    Fontaine, C.5    Duquesnoy, B.6    Flipo, R.M.7
  • 58
    • 0025292252 scopus 로고
    • Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells
    • Leonard, C. K., M. W. Spellman, L. Riddle, R. J. Harris, J. N. Thomas, and T. J. Gregory. 1990. Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells. J. Biol. Chem. 265:10373-10382.
    • (1990) J. Biol. Chem , vol.265 , pp. 10373-10382
    • Leonard, C.K.1    Spellman, M.W.2    Riddle, L.3    Harris, R.J.4    Thomas, J.N.5    Gregory, T.J.6
  • 60
    • 31144451337 scopus 로고    scopus 로고
    • Characterization of antibody responses elicited by human immunodefi-ciency virus type 1 primary isolate trimeric and monomeric envelope glycoproteins in selected adjuvants
    • Li, Y., K. Svehla, N. L. Mathy, G. Voss, J. R. Mascola, and R. Wyatt. 2006. Characterization of antibody responses elicited by human immunodefi-ciency virus type 1 primary isolate trimeric and monomeric envelope glycoproteins in selected adjuvants. J. Virol. 80:1414-1426.
    • (2006) J. Virol , vol.80 , pp. 1414-1426
    • Li, Y.1    Svehla, K.2    Mathy, N.L.3    Voss, G.4    Mascola, J.R.5    Wyatt, R.6
  • 62
    • 0027199489 scopus 로고
    • Characterization of neutralizing monoclonal antibodies to linear and conformation-dependent epitopes within the first and second variable domains of human immunodeficiency virus type 1 gp120
    • McKeating, J. A., C. Shotton, J. Cordell, S. Graham, P. Balfe, N. Sullivan, M. Charles, M. Page, A. Bolmstedt, S. Olofsson, et al. 1993. Characterization of neutralizing monoclonal antibodies to linear and conformation-dependent epitopes within the first and second variable domains of human immunodeficiency virus type 1 gp120. J. Virol. 67:4932-4944.
    • (1993) J. Virol , vol.67 , pp. 4932-4944
    • McKeating, J.A.1    Shotton, C.2    Cordell, J.3    Graham, S.4    Balfe, P.5    Sullivan, N.6    Charles, M.7    Page, M.8    Bolmstedt, A.9    Olofsson, S.10
  • 64
    • 65249139458 scopus 로고    scopus 로고
    • HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes
    • Miyauchi, K., Y. Kim, O. Latinovic, V. Morozov, and G. B. Melikyan. 2009. HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes. Cell 137:433-444.
    • (2009) Cell , vol.137 , pp. 433-444
    • Miyauchi, K.1    Kim, Y.2    Latinovic, O.3    Morozov, V.4    Melikyan, G.B.5
  • 67
    • 0027170414 scopus 로고
    • Strain specificity and binding affinity requirements of neutralizing monoclonal antibodies to the C4 domain of gp120 from human immunodeficiency virus type 1
    • Nakamura, G. R., R. Byrn, D. M. Wilkes, J. A. Fox, M. R. Hobbs, R. Hastings, H. C. Wessling, M. A. Norcross, B. M. Fendly, and P. W. Berman. 1993. Strain specificity and binding affinity requirements of neutralizing monoclonal antibodies to the C4 domain of gp120 from human immunodeficiency virus type 1. J. Virol. 67:6179-6191.
    • (1993) J. Virol , vol.67 , pp. 6179-6191
    • Nakamura, G.R.1    Byrn, R.2    Wilkes, D.M.3    Fox, J.A.4    Hobbs, M.R.5    Hastings, R.6    Wessling, H.C.7    Norcross, M.A.8    Fendly, B.M.9    Berman, P.W.10
  • 69
    • 37549070672 scopus 로고    scopus 로고
    • Cysteine cathepsin proteases as pharmacological targets in cancer
    • Palermo, C., and J. A. Joyce. 2008. Cysteine cathepsin proteases as pharmacological targets in cancer. Trends Pharmacol. Sci. 29:22-28.
    • (2008) Trends Pharmacol. Sci , vol.29 , pp. 22-28
    • Palermo, C.1    Joyce, J.A.2
  • 70
    • 33646146379 scopus 로고    scopus 로고
    • GP120: Target for neutralizing HIV-1 antibodies
    • Pantophlet, R., and D. R. Burton. 2006. GP120: target for neutralizing HIV-1 antibodies. Annu. Rev. Immunol. 24:739-769.
    • (2006) Annu. Rev. Immunol , vol.24 , pp. 739-769
    • Pantophlet, R.1    Burton, D.R.2
  • 71
    • 0034692465 scopus 로고    scopus 로고
    • A comparison of full-length glycoprotein 120 from incident HIV type 1 subtype E and B infections in Bangkok injecting drug users with prototype E and B strains that are components of a candidate vaccine
    • Phan, K. O., M. E. Callahan, S. Vanichseni, D. J. Hu, S. Raktham, N. Young, K. Choopanya, T. D. Mastro, and S. Subbarao. 2000. A comparison of full-length glycoprotein 120 from incident HIV type 1 subtype E and B infections in Bangkok injecting drug users with prototype E and B strains that are components of a candidate vaccine. AIDS Res. Hum. Retrovir. 16:1445-1450.
    • (2000) AIDS Res. Hum. Retrovir , vol.16 , pp. 1445-1450
    • Phan, K.O.1    Callahan, M.E.2    Vanichseni, S.3    Hu, D.J.4    Raktham, S.5    Young, N.6    Choopanya, K.7    Mastro, T.D.8    Subbarao, S.9
  • 72
    • 2342644898 scopus 로고    scopus 로고
    • The V1/V2 domain of gp120 is a global regulator of the sensitivity of primary human immunodeficiency virus type 1 isolates to neutralization by antibodies commonly induced upon infection
    • Pinter, A., W. J. Honnen, Y. He, M. K. Gorny, S. Zolla-Pazner, and S. C. Kayman. 2004. The V1/V2 domain of gp120 is a global regulator of the sensitivity of primary human immunodeficiency virus type 1 isolates to neutralization by antibodies commonly induced upon infection. J. Virol. 78:5205-5215.
    • (2004) J. Virol , vol.78 , pp. 5205-5215
    • Pinter, A.1    Honnen, W.J.2    He, Y.3    Gorny, M.K.4    Zolla-Pazner, S.5    Kayman, S.C.6
  • 73
    • 0032941595 scopus 로고    scopus 로고
    • HIV-1-specific CD4+ T cells are detectable in most individuals with active HIV-1 infection, but decline with prolonged viral suppression
    • Pitcher, C. J., C. Quittner, D. M. Peterson, M. Connors, R. A. Koup, V. C. Maino, and L. J. Picker. 1999. HIV-1-specific CD4+ T cells are detectable in most individuals with active HIV-1 infection, but decline with prolonged viral suppression. Nat. Med. 5:518-525.
    • (1999) Nat. Med , vol.5 , pp. 518-525
    • Pitcher, C.J.1    Quittner, C.2    Peterson, D.M.3    Connors, M.4    Koup, R.A.5    Maino, V.C.6    Picker, L.J.7
  • 74
    • 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
    • Pitisuttithum, P., P. Gilbert, M. Gurwith, W. Heyward, M. Martin, F. van Griensven, D. Hu, J. W. Tappero, and K. Choopanya. 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    Gilbert, P.2    Gurwith, M.3    Heyward, W.4    Martin, M.5    van Griensven, F.6    Hu, D.7    Tappero, J.W.8    Choopanya, K.9
  • 77
    • 0029007093 scopus 로고
    • Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages
    • Reddy, V. Y., Q. Y. Zhang, and S. J. Weiss. 1995. Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages. Proc. Natl. Acad. Sci. USA 92: 3849-3853.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3849-3853
    • Reddy, V.Y.1    Zhang, Q.Y.2    Weiss, S.J.3
  • 78
    • 0034690683 scopus 로고    scopus 로고
    • Fine definition of a conserved CCR5-binding region on the human immunodeficiency virus type 1 glycoprotein 120
    • Rizzuto, C., and J. Sodroski. 2000. Fine definition of a conserved CCR5-binding region on the human immunodeficiency virus type 1 glycoprotein 120. AIDS Res. Hum. Retrovir. 16:741-749.
    • (2000) AIDS Res. Hum. Retrovir , vol.16 , pp. 741-749
    • Rizzuto, C.1    Sodroski, J.2
  • 84
    • 21644446614 scopus 로고    scopus 로고
    • The V1, V2, and V3 regions of the human immunodeficiency virus type 1 envelope differentially affect the viral phenotype in an isolate-dependent manner
    • Saunders, C. J., R. A. McCaffrey, I. Zharkikh, Z. Kraft, S. E. Malenbaum, B. Burke, C. Cheng-Mayer, and L. Stamatatos. 2005. The V1, V2, and V3 regions of the human immunodeficiency virus type 1 envelope differentially affect the viral phenotype in an isolate-dependent manner. J. Virol. 79: 9069-9080.
    • (2005) J. Virol , vol.79 , pp. 9069-9080
    • Saunders, C.J.1    McCaffrey, R.A.2    Zharkikh, I.3    Kraft, Z.4    Malenbaum, S.E.5    Burke, B.6    Cheng-Mayer, C.7    Stamatatos, L.8
  • 85
    • 0027400775 scopus 로고
    • Exploration of subsite binding specificity of human cathepsin D through kinetics and rule-based molecular modeling
    • Scarborough, P. E., K. Guruprasad, C. Topham, G. R. Richo, G. E. Conner, T. L. Blundell, and B. M. Dunn. 1993. Exploration of subsite binding specificity of human cathepsin D through kinetics and rule-based molecular modeling. Protein Sci. 2:264-276.
    • (1993) Protein Sci , vol.2 , pp. 264-276
    • Scarborough, P.E.1    Guruprasad, K.2    Topham, C.3    Richo, G.R.4    Conner, G.E.5    Blundell, T.L.6    Dunn, B.M.7
  • 86
    • 0014211618 scopus 로고    scopus 로고
    • Schechter, I., and A. Berger. 1967. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27:157-162.
    • Schechter, I., and A. Berger. 1967. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27:157-162.
  • 88
    • 4143146210 scopus 로고    scopus 로고
    • Important role of cathepsin S in generating peptides for TAP-independent MHC class I crosspresentation in vivo
    • Shen, L., L. J. Sigal, M. Boes, and K. L. Rock. 2004. Important role of cathepsin S in generating peptides for TAP-independent MHC class I crosspresentation in vivo. Immunity 21:155-165.
    • (2004) Immunity , vol.21 , pp. 155-165
    • Shen, L.1    Sigal, L.J.2    Boes, M.3    Rock, K.L.4
  • 90
    • 0031666180 scopus 로고    scopus 로고
    • An envelope modification that renders a primary, neutralization-resistant clade B human immunodefi-ciency virus type 1 isolate highly susceptible to neutralization by sera from other clades
    • Stamatatos, L., and C. Cheng-Mayer. 1998. An envelope modification that renders a primary, neutralization-resistant clade B human immunodefi-ciency virus type 1 isolate highly susceptible to neutralization by sera from other clades. J. Virol. 72:7840-7845.
    • (1998) J. Virol , vol.72 , pp. 7840-7845
    • Stamatatos, L.1    Cheng-Mayer, C.2
  • 91
    • 0026044947 scopus 로고
    • Neutralization of divergent HIV-1 isolates by conformation-dependent human antibodies to Gp120
    • Steimer, K. S., C. J. Scandella, P. V. Skiles, and N. L. Haigwood. 1991. Neutralization of divergent HIV-1 isolates by conformation-dependent human antibodies to Gp120. Science 254:105-108.
    • (1991) Science , vol.254 , pp. 105-108
    • Steimer, K.S.1    Scandella, C.J.2    Skiles, P.V.3    Haigwood, N.L.4
  • 94
    • 17644370329 scopus 로고    scopus 로고
    • Cell biology of antigen processing in vitro and in vivo
    • Trombetta, E. S., and I. Mellman. 2005. Cell biology of antigen processing in vitro and in vivo. Annu. Rev. Immunol. 23:975-1028.
    • (2005) Annu. Rev. Immunol , vol.23 , pp. 975-1028
    • Trombetta, E.S.1    Mellman, I.2
  • 96
    • 0024412693 scopus 로고
    • The selectivity of cathepsin D suggests an involvement of the enzyme in the generation of T-cell epitopes
    • van Noort, J. M., and A. C. van der Drift. 1989. The selectivity of cathepsin D suggests an involvement of the enzyme in the generation of T-cell epitopes. J. Biol. Chem. 264:14159-14164.
    • (1989) J. Biol. Chem , vol.264 , pp. 14159-14164
    • van Noort, J.M.1    van der Drift, A.C.2
  • 97
    • 0033695299 scopus 로고    scopus 로고
    • Proteolysis in MHC class II antigen presentation: Who's in charge?
    • Villadangos, J. A., and H. L. Ploegh. 2000. Proteolysis in MHC class II antigen presentation: who's in charge? Immunity 12:233-239.
    • (2000) Immunity , vol.12 , pp. 233-239
    • Villadangos, J.A.1    Ploegh, H.L.2
  • 99
    • 0029615496 scopus 로고
    • How MHC class II molecules acquire peptide cargo: Biosynthesis and trafficking through the endocytic pathway
    • Wolf, P. R., and H. L. Ploegh. 1995. How MHC class II molecules acquire peptide cargo: biosynthesis and trafficking through the endocytic pathway. Annu. Rev. Cell Dev. Biol. 11:267-306.
    • (1995) Annu. Rev. Cell Dev. Biol , vol.11 , pp. 267-306
    • Wolf, P.R.1    Ploegh, H.L.2
  • 100
    • 0028965263 scopus 로고
    • Characterization of neutralization epitopes in the V2 region of human immunodefi-ciency virus type 1 gp120: Role of glycosylation in the correct folding of the V1/V2 domain
    • Wu, Z., S. C. Kayman, W. Honnen, K. Revesz, H. Chen, S. Vijh-Warrier, S. A. Tilley, J. McKeating, C. Shotton, and A. Pinter. 1995. Characterization of neutralization epitopes in the V2 region of human immunodefi-ciency virus type 1 gp120: role of glycosylation in the correct folding of the V1/V2 domain. J. Virol. 69:2271-2278.
    • (1995) J. Virol , vol.69 , pp. 2271-2278
    • Wu, Z.1    Kayman, S.C.2    Honnen, W.3    Revesz, K.4    Chen, H.5    Vijh-Warrier, S.6    Tilley, S.A.7    McKeating, J.8    Shotton, C.9    Pinter, A.10
  • 101
    • 0032484486 scopus 로고    scopus 로고
    • CCR5 coreceptor usage of non-syncytium- inducing primary HIV-1 is independent of phylogenetically distinct global HIV-1 isolates: Delineation of consensus motif in the V3 domain that predicts CCR5 usage
    • Xiao, L., S. M. Owen, I. Goldman, A. A. Lal, J. J. deJong, J. Goudsmit, and R. B. Lal. 1998. CCR5 coreceptor usage of non-syncytium- inducing primary HIV-1 is independent of phylogenetically distinct global HIV-1 isolates: delineation of consensus motif in the V3 domain that predicts CCR5 usage. Virology 240:83-92.
    • (1998) Virology , vol.240 , pp. 83-92
    • Xiao, L.1    Owen, S.M.2    Goldman, I.3    Lal, A.A.4    deJong, J.J.5    Goudsmit, J.6    Lal, R.B.7
  • 102
    • 18944365919 scopus 로고    scopus 로고
    • The role of cathepsins in osteoporosis and arthritis: Rationale for the design of new therapeutics
    • Yasuda, Y., J. Kaleta, and D. Bromme. 2005. The role of cathepsins in osteoporosis and arthritis: rationale for the design of new therapeutics. Adv. Drug Deliv. Rev. 57:973-993.
    • (2005) Adv. Drug Deliv. Rev , vol.57 , pp. 973-993
    • Yasuda, Y.1    Kaleta, J.2    Bromme, D.3
  • 103
    • 0033280323 scopus 로고    scopus 로고
    • Mechanisms of viral interference with MHC class I antigen processing and presentation
    • Yewdell, J. W., and J. R. Bennink. 1999. Mechanisms of viral interference with MHC class I antigen processing and presentation. Annu. Rev. Cell Dev. Biol. 15:579-606.
    • (1999) Annu. Rev. Cell Dev. Biol , vol.15 , pp. 579-606
    • Yewdell, J.W.1    Bennink, J.R.2
  • 104
    • 34247264248 scopus 로고    scopus 로고
    • HIV-1 envelope T cell epitope "hotspots" among mice and humans and among CD4+ and CD8+ T cell subpopulations
    • Zhan, X., J. L. Hurwitz, S. A. Brown, and K. S. Slobod. 2007. HIV-1 envelope T cell epitope "hotspots" among mice and humans and among CD4+ and CD8+ T cell subpopulations. AIDS Res. Hum. Retrovir. 23: 471-476.
    • (2007) AIDS Res. Hum. Retrovir , vol.23 , pp. 471-476
    • Zhan, X.1    Hurwitz, J.L.2    Brown, S.A.3    Slobod, K.S.4


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