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Volumn 58, Issue 6, 2006, Pages 759-767

HIV-1 neutralizing antibodies elicited by the candidate CBD1 epitope vaccine react with the conserved caveolin-1 binding motif of viral glycoprotein gp41

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CAVEOLIN 1; CBD1 ANTIBODY; EPITOPE; GLYCOPROTEIN GP 41; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; NEUTRALIZING ANTIBODY; PROLINE; TRYPTOPYLASPARAGYLASPARAGYLMETHIONYLTHREONYLTRYPTOPHYLMETHIONYLGLUTAMYLTRYTOPHAN; UNCLASSIFIED DRUG;

EID: 33744918518     PISSN: 00223573     EISSN: None     Source Type: Journal    
DOI: 10.1211/jpp.58.6.0006     Document Type: Article
Times cited : (8)

References (41)
  • 1
    • 0035873475 scopus 로고    scopus 로고
    • Secretory IgA specific for a conserved epitope on gp41 envelope glycoprotein inhibits epithelial transcytosis of HIV-1
    • Alfsen, A., Iniguez, P., Bouguyon, E., Bomsel, M. (2001) Secretory IgA specific for a conserved epitope on gp41 envelope glycoprotein inhibits epithelial transcytosis of HIV-1. J. Immunol. 166: 6257-6265
    • (2001) J. Immunol. , vol.166 , pp. 6257-6265
    • Alfsen, A.1    Iniguez, P.2    Bouguyon, E.3    Bomsel, M.4
  • 2
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- And cholesterol-rich membrane rafts
    • Brown, D. A., London, E. (2000) Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J. Biol. Chem. 275: 17221-17224
    • (2000) J. Biol. Chem. , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 3
    • 0034853037 scopus 로고    scopus 로고
    • Lipid rafts and HIV-1: From viral entry to assembly of progeny virions
    • Campbell, S. M., Crowe, S. M., Mak, J. (2001) Lipid rafts and HIV-1: from viral entry to assembly of progeny virions. J. Clin. Virol. 22: 217-227
    • (2001) J. Clin. Virol. , vol.22 , pp. 217-227
    • Campbell, S.M.1    Crowe, S.M.2    Mak, J.3
  • 5
    • 13844255333 scopus 로고    scopus 로고
    • Broadly neutralizing anti-HIV antibody 4E10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41
    • Cardoso, R. M., Zwick, M. B., Stanfield, R. L., Kunert, R., Binley, J. M., Katinger, H., Burton, D. R., Wilson, I. A. (2005) Broadly neutralizing anti-HIV antibody 4E10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41. Immunity 22: 163-173
    • (2005) Immunity , vol.22 , pp. 163-173
    • Cardoso, R.M.1    Zwick, M.B.2    Stanfield, R.L.3    Kunert, R.4    Binley, J.M.5    Katinger, H.6    Burton, D.R.7    Wilson, I.A.8
  • 6
    • 0032433685 scopus 로고    scopus 로고
    • Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target
    • Chan, D. C., Chutkowski, C. T., Kim, P. S. (1998) Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target. Proc. Natl Acad. Sci. USA 95: 15613-15617
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 15613-15617
    • Chan, D.C.1    Chutkowski, C.T.2    Kim, P.S.3
  • 8
    • 0030941001 scopus 로고    scopus 로고
    • Identification of peptide and protein ligands for the caveolin-scaffolding domain
    • Couet, J., Li, S., Okamoto, T., Ikezu, T., Lisanti, M. P. (1997) Identification of peptide and protein ligands for the caveolin-scaffolding domain. J. Biol. Chem. 272: 6525-6533
    • (1997) J. Biol. Chem. , vol.272 , pp. 6525-6533
    • Couet, J.1    Li, S.2    Okamoto, T.3    Ikezu, T.4    Lisanti, M.P.5
  • 9
    • 0035862545 scopus 로고    scopus 로고
    • N- And C-domains of HIV-1 gp41: Mutation, structure and functions
    • Dong, X. N., Yi, X., Dierich, M. P., Chen, B. K. (2001) N- and C-domains of HIV-1 gp41: mutation, structure and functions. Immunol. Lett. 75: 215-220
    • (2001) Immunol. Lett. , vol.75 , pp. 215-220
    • Dong, X.N.1    Yi, X.2    Dierich, M.P.3    Chen, B.K.4
  • 10
    • 0034924823 scopus 로고    scopus 로고
    • Mechanism of viral membrane fusion and its inhibition
    • Eckert, D. M., Kim, P. S. (2001) Mechanism of viral membrane fusion and its inhibition. Annu. Rev. Biochem. 70: 777-810
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 11
    • 0037379284 scopus 로고    scopus 로고
    • Rapid localization of Gag/GagPol complexes to detergent-resistant membrane during the assembly of human immunodeficiency virus type 1
    • Halwani, R., Khorchid, A., Cen, S., Kleiman, L. (2003) Rapid localization of Gag/GagPol complexes to detergent-resistant membrane during the assembly of human immunodeficiency virus type 1. J. Virol. 77: 3973-3984
    • (2003) J. Virol. , vol.77 , pp. 3973-3984
    • Halwani, R.1    Khorchid, A.2    Cen, S.3    Kleiman, L.4
  • 12
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder, T., Scheiffele, P., Verkade, P., Simons, K. (1998) Lipid domain structure of the plasma membrane revealed by patching of membrane components. J. Cell Biol. 141: 929-942
    • (1998) J. Cell Biol. , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 14
    • 8544258110 scopus 로고    scopus 로고
    • The caveolin-1 binding domain of HIV-1 glycoprotein gp41 is an efficient B-cell epitope vaccine candidate against virus infection
    • Hovanessian, A. G., Briand, J. P., Said, A. S., Svab, J., Ferris, S., Dali, H., Muller, S., Desgranges, C., Krust, B. (2004) The caveolin-1 binding domain of HIV-1 glycoprotein gp41 is an efficient B-cell epitope vaccine candidate against virus infection. Immunity 21: 617-720
    • (2004) Immunity , vol.21 , pp. 617-720
    • Hovanessian, A.G.1    Briand, J.P.2    Said, A.S.3    Svab, J.4    Ferris, S.5    Dali, H.6    Muller, S.7    Desgranges, C.8    Krust, B.9
  • 15
    • 22844441184 scopus 로고    scopus 로고
    • Alanine scanning mutants of the HIV gp41 loop
    • Jacobs, A., Sen, J., Rong, L., Caffrey, M. (2005) Alanine scanning mutants of the HIV gp41 loop. J. Biol. Chem. 280: 27284-27288
    • (2005) J. Biol. Chem. , vol.280 , pp. 27284-27288
    • Jacobs, A.1    Sen, J.2    Rong, L.3    Caffrey, M.4
  • 16
    • 0035163480 scopus 로고    scopus 로고
    • Conserved, N-linked carbohydrates of human immunodeficiency virus type 1 gp41 are largely dispensable for viral replication
    • Johnson, W. E., Sauvron, J. M., Desrosiers, R. C. (2001) Conserved, N-linked carbohydrates of human immunodeficiency virus type 1 gp41 are largely dispensable for viral replication. J. Virol. 15: 11426-11436
    • (2001) J. Virol. , vol.15 , pp. 11426-11436
    • Johnson, W.E.1    Sauvron, J.M.2    Desrosiers, R.C.3
  • 17
    • 0025076762 scopus 로고
    • Budding process and maturation of human immunodeficiency virus examined by means of pre- And post-embedding immunocolloidal gold electron microscopy
    • Kadsumoto, T., Asanaka, M., Kageyama, S., Kurimura, T., Nakajima, K., N., A., Tanaka, H., Sato, R. (1990) Budding process and maturation of human immunodeficiency virus examined by means of pre- and post-embedding immunocolloidal gold electron microscopy. J. Electron Microsc. 39: 33-38
    • (1990) J. Electron Microsc. , vol.39 , pp. 33-38
    • Kadsumoto, T.1    Asanaka, M.2    Kageyama, S.3    Kurimura, T.4    Nakajima, K.5    Tanaka, H.6    Sato, R.7
  • 21
    • 20444365510 scopus 로고    scopus 로고
    • Aromatic-aromatic and proline-aromatic interactions in endomorphin-1 and endomorphin-2
    • Leitgeb, B., Toth, G. (2005) Aromatic-aromatic and proline-aromatic interactions in endomorphin-1 and endomorphin-2. Eur. J. Med. Chem. 40: 674-686
    • (2005) Eur. J. Med. Chem. , vol.40 , pp. 674-686
    • Leitgeb, B.1    Toth, G.2
  • 22
    • 0034834457 scopus 로고    scopus 로고
    • Lipid rafts and HIV pathogenesis: Host membrane cholesterol is required for infection by HIV type 1
    • Liao, Z., Cimakasky, L. M., Hampton, R., Nguyen, D. H., Hildreth, J. E. K. (2001) Lipid rafts and HIV pathogenesis: host membrane cholesterol is required for infection by HIV type 1. AIDS Res. Hum. Retroviruses 17: 1009-1019
    • (2001) AIDS Res. Hum. Retroviruses , vol.17 , pp. 1009-1019
    • Liao, Z.1    Cimakasky, L.M.2    Hampton, R.3    Nguyen, D.H.4    Hildreth, J.E.K.5
  • 23
    • 0036830114 scopus 로고    scopus 로고
    • Multiple functions of caveolin-1
    • Liu, P., Rudick, M., Anderson, R. G. W. (2002) Multiple functions of caveolin-1. J. Biol. Chem. 277: 41295-41298
    • (2002) J. Biol. Chem. , vol.277 , pp. 41295-41298
    • Liu, P.1    Rudick, M.2    Anderson, R.G.W.3
  • 25
    • 0038638590 scopus 로고    scopus 로고
    • HIV vaccines 1983-2003
    • McMichael, A. J., Hanke, T. (2003) HIV vaccines 1983-2003. Nat. Med. 9: 874-880
    • (2003) Nat. Med. , vol.9 , pp. 874-880
    • McMichael, A.J.1    Hanke, T.2
  • 26
    • 0034978733 scopus 로고    scopus 로고
    • Genetic subtypes, humoral immunity, and human immunodeficiency virus type 1 vaccine development
    • Moore, J. P., Parren, P. W. H. I., Burton, D. R. (2001) Genetic subtypes, humoral immunity, and human immunodeficiency virus type 1 vaccine development. J. Virol. 75: 5721-5729
    • (2001) J. Virol. , vol.75 , pp. 5721-5729
    • Moore, J.P.1    Parren, P.W.H.I.2    Burton, D.R.3
  • 27
    • 0027632992 scopus 로고
    • Development of a fully automated multichannel peptide synthesizer with integrated TFA cleavage capability
    • Neimark, J., Briand, J. P. (1993) Development of a fully automated multichannel peptide synthesizer with integrated TFA cleavage capability. Peptide Res. 6: 219-228
    • (1993) Peptide Res. , vol.6 , pp. 219-228
    • Neimark, J.1    Briand, J.P.2
  • 28
    • 0034015604 scopus 로고    scopus 로고
    • Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid enriched membrane lipid rafts
    • Nguyen, D. H., Hildreth, J. E. K. (2000) Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid enriched membrane lipid rafts. J. Virol. 74: 3264-3272
    • (2000) J. Virol. , vol.74 , pp. 3264-3272
    • Nguyen, D.H.1    Hildreth, J.E.K.2
  • 29
    • 0036354940 scopus 로고    scopus 로고
    • Anchorage of HIV on permissive cells leads to co-aggregation of viral particles with surface nucleolin at membrane raft microdomains
    • Nisole, S., Krust, B., Hovanessian, A. G. (2002) Anchorage of HIV on permissive cells leads to co-aggregation of viral particles with surface nucleolin at membrane raft microdomains. Exp. Cell Res. 276: 155-173
    • (2002) Exp. Cell Res. , vol.276 , pp. 155-173
    • Nisole, S.1    Krust, B.2    Hovanessian, A.G.3
  • 30
    • 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., Tang, M., Sambor, A., Katinger, H., Mascola, J. R., Wyatt, R., Kwong, P. D. (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
  • 31
    • 0032489443 scopus 로고    scopus 로고
    • Caveolins, a family of scaffolding proteins for organizing 'pre-assembled signaling complexes' at the plasma membrane
    • Okamoto, T., Schlegel, A., Scherer, P. E., Lisanti, M. P. (1998) Caveolins, a family of scaffolding proteins for organizing 'pre-assembled signaling complexes' at the plasma membrane. J. Biol. Chem. 273: 5419-5422
    • (1998) J. Biol. Chem. , vol.273 , pp. 5419-5422
    • Okamoto, T.1    Schlegel, A.2    Scherer, P.E.3    Lisanti, M.P.4
  • 32
    • 0035923525 scopus 로고    scopus 로고
    • Plasma membrane rafts play a critical role in HIV-1 assembly and release
    • Ono, A., Freed, E. O. (2001) Plasma membrane rafts play a critical role in HIV-1 assembly and release. Proc. Natl Acad. Sci. USA 98. 13925-13930
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 13925-13930
    • Ono, A.1    Freed, E.O.2
  • 33
    • 0035222608 scopus 로고    scopus 로고
    • The antiviral activity of antibodies in vitro and in vivo
    • Parren, P. W., Burton, D. R. (2001) The antiviral activity of antibodies in vitro and in vivo. Adv. Immunol. 77: 195-262
    • (2001) Adv. Immunol. , vol.77 , pp. 195-262
    • Parren, P.W.1    Burton, D.R.2
  • 34
    • 18644375565 scopus 로고    scopus 로고
    • Structural and immunological characterisation of heteroclitic peptide analogues corresponding to the 600-612 region of the HIV envelope gp41 glycoprotein
    • Phan Chan Du, A., Limal, D., Semetey, V., Dali, H., Jolivet, M., Desgranges, C., Cung, M. T., Briand, J. P., Petit, M. C., Muller, S. (2002) Structural and immunological characterisation of heteroclitic peptide analogues corresponding to the 600-612 region of the HIV envelope gp41 glycoprotein. J. Mol. Biol. 323: 503-521
    • (2002) J. Mol. Biol. , vol.323 , pp. 503-521
    • Phan Chan Du, A.1    Limal, D.2    Semetey, V.3    Dali, H.4    Jolivet, M.5    Desgranges, C.6    Cung, M.T.7    Briand, J.P.8    Petit, M.C.9    Muller, S.10
  • 36
    • 0037077229 scopus 로고    scopus 로고
    • Sphingomyelin and cholesterol promote HIV-1 gp41 pretransmembrane sequence surface aggregation at membrane restructuring
    • Saez-Cirion, A., Nir, S., Lorizate, M., Agirre, A., Cruz, A., Ferez, J., Nieva, J. L. (2002) Sphingomyelin and cholesterol promote HIV-1 gp41 pretransmembrane sequence surface aggregation at 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    Ferez, J.6    Nieva, J.L.7
  • 37
    • 0032980413 scopus 로고    scopus 로고
    • A conserved tryptophane-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for Env-mediated fusion and virus infectivity
    • Salzwedel, K., West, J. T., Hunter, E. (1999) A conserved tryptophane-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for Env-mediated fusion and virus infectivity. J. Virol. 73: 2469-2480
    • (1999) J. Virol. , vol.73 , pp. 2469-2480
    • Salzwedel, K.1    West, J.T.2    Hunter, E.3
  • 39
    • 0033869815 scopus 로고    scopus 로고
    • Membrane-interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein: Putative role during viral fusion
    • Suarez, T., Gallaher, W. R., Agirre, A., Goni, F. M., Nieva, J. L. (2000) Membrane-interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein: putative role during viral fusion. J. Biol. Chem. 74: 8038-8047
    • (2000) J. Biol. Chem. , vol.74 , pp. 8038-8047
    • Suarez, T.1    Gallaher, W.R.2    Agirre, A.3    Goni, F.M.4    Nieva, J.L.5
  • 40
    • 0037164705 scopus 로고    scopus 로고
    • Identification of a conserved domain of the HIV-1 transmembrane protein gp41 which interacts with cholesteryl groups
    • Vincent, N., Genin, C., Malvoisin, E. (2002) Identification of a conserved domain of the HIV-1 transmembrane protein gp41 which interacts with cholesteryl groups. Biochim. Biophys. Acta 1567: 157-164
    • (2002) Biochim. Biophys. Acta , vol.1567 , pp. 157-164
    • Vincent, N.1    Genin, C.2    Malvoisin, E.3
  • 41
    • 0034023726 scopus 로고    scopus 로고
    • Structure-function studies of the self-assembly domain of the human immunodeficiency virus type 1 transmembrane protein gp41
    • Weng, Y., Yang, Z., Weiss, C. (2000) Structure-function studies of the self-assembly domain of the human immunodeficiency virus type 1 transmembrane protein gp41. J. Virol. 74: 5368-5372
    • (2000) J. Virol. , vol.74 , pp. 5368-5372
    • Weng, Y.1    Yang, Z.2    Weiss, C.3


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