메뉴 건너뛰기




Volumn 78, Issue 5, 2004, Pages 2627-2631

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

Author keywords

[No Author keywords available]

Indexed keywords

CD4 ANTIGEN; GLYCOPROTEIN GP 41; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; VIRUS GLYCOPROTEIN;

EID: 1242342052     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.78.5.2627-2631.2004     Document Type: Article
Times cited : (84)

References (41)
  • 2
    • 0037159248 scopus 로고    scopus 로고
    • A monomeric 3(10)-helix is formed in water by a 13-residue peptide representing the neutralizing determinant of HIV-1 on gp41
    • Biron, Z., S. Khare, A. O. Samson, Y. Hayek, F. Naider, and J. Anglister. 2002. A monomeric 3(10)-helix is formed in water by a 13-residue peptide representing the neutralizing determinant of HIV-1 on gp41. Biochemistry 41:12687-12696.
    • (2002) Biochemistry , vol.41 , pp. 12687-12696
    • Biron, Z.1    Khare, S.2    Samson, A.O.3    Hayek, Y.4    Naider, F.5    Anglister, J.6
  • 3
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational changes of influenza hemagglutinin
    • Carr, C. M., and P. S. Kim. 1993. A spring-loaded mechanism for the conformational changes of influenza hemagglutinin. Cell 73:823-832.
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 4
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan, D. C., D. Fass, J. M. Berger, and P. S. Kim. 1997. Core structure of gp41 from the HIV envelope glycoprotein. Cell 89:263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 5
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan, D. C., and P. S. Kim. 1998. HIV entry and its inhibition. Cell 93:681-684.
    • (1998) Cell , vol.93 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 6
    • 0034892978 scopus 로고    scopus 로고
    • Peptides corresponding to the heptad repeat motifs in the transmembrane protein (gp41) of human immunodeficiency virus type 1 elicit antibodies to receptor-activated conformations of the envelope glycoprotein
    • de Rosny, E., V. Vassell, P. T. Wingfield, C. T. Wild, and C. D. Weiss. 2001. Peptides corresponding to the heptad repeat motifs in the transmembrane protein (gp41) of human immunodeficiency virus type 1 elicit antibodies to receptor-activated conformations of the envelope glycoprotein. J. Virol. 75:8859-8863.
    • (2001) J. Virol. , vol.75 , pp. 8859-8863
    • De Rosny, E.1    Vassell, V.2    Wingfield, P.T.3    Wild, C.T.4    Weiss, C.D.5
  • 7
    • 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
  • 8
    • 0028355456 scopus 로고
    • Native oligomeric human immunodeficiency virus type 1 envelope glycoprotein elicits diverse monoclonal antibody reactivities
    • Earl, P. L., C. C. Broder, D. Long, S. A. Lee, J. Peterson, S. Chakrabarti, R. W. Doms, and B. Moss. 1994. Native oligomeric human immunodeficiency virus type 1 envelope glycoprotein elicits diverse monoclonal antibody reactivities. J. Virol. 68:3015-3026.
    • (1994) J. Virol. , vol.68 , pp. 3015-3026
    • Earl, P.L.1    Broder, C.C.2    Long, D.3    Lee, S.A.4    Peterson, J.5    Chakrabarti, S.6    Doms, R.W.7    Moss, B.8
  • 9
    • 0036889127 scopus 로고    scopus 로고
    • Antigenic properties of the human immunodeficiency virus transmembrane glycoprotein during cell-cell fusion
    • Finnegan, C. M., W. Berg, G. K. Lewis, and A. L. DeVico. 2002. Antigenic properties of the human immunodeficiency virus transmembrane glycoprotein during cell-cell fusion. J. Virol. 76:12123-12134.
    • (2002) J. Virol. , vol.76 , pp. 12123-12134
    • Finnegan, C.M.1    Berg, W.2    Lewis, G.K.3    DeVico, A.L.4
  • 10
    • 0036633932 scopus 로고    scopus 로고
    • Genetic evidence that interhelical packing interactions in the gp41 core are critical for transition of the human immunodeficiency virus type 1 envelope glycoprotein to the fusion-active state
    • Follis, K. E., S. J. Larson, M. Lu, and J. H. Nunberg. 2002. Genetic evidence that interhelical packing interactions in the gp41 core are critical for transition of the human immunodeficiency virus type 1 envelope glycoprotein to the fusion-active state. J. Virol. 76:7356-7362.
    • (2002) J. Virol. , vol.76 , pp. 7356-7362
    • Follis, K.E.1    Larson, S.J.2    Lu, M.3    Nunberg, J.H.4
  • 11
    • 0031959601 scopus 로고    scopus 로고
    • Capture of an early fusion-active conformation of HIV-1 gp41
    • Furuta, R. A., C. T. Wild, Y. Weng, and C. D. Weiss. 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
  • 12
    • 0034046091 scopus 로고    scopus 로고
    • Recognition by human monoclonal antibodies of free and complexed peptides representing the prefusogenic and fusogenic forms of human immunodeficiency virus type 1 gp41
    • Gorny, M. K., and S. Zolla-Pazner. 2000. Recognition by human monoclonal antibodies of free and complexed peptides representing the prefusogenic and fusogenic forms of human immunodeficiency virus type 1 gp41. J. Virol. 74:6186-6192.
    • (2000) J. Virol. , vol.74 , pp. 6186-6192
    • Gorny, M.K.1    Zolla-Pazner, S.2
  • 13
    • 0037301373 scopus 로고    scopus 로고
    • Peptides trap the human immunodeficiency virus type 1 envelope glycoprotein fusion intermediate at two sites
    • He, Y., R. Vassell, M. Zaitseva, N. Nguyen, Z. Yang, Y. Weng, and C. D. Weiss. 2003. Peptides trap the human immunodeficiency virus type 1 envelope glycoprotein fusion intermediate at two sites. J. Virol. 77:1666-1671.
    • (2003) J. Virol. , vol.77 , pp. 1666-1671
    • He, Y.1    Vassell, R.2    Zaitseva, M.3    Nguyen, N.4    Yang, Z.5    Weng, Y.6    Weiss, C.D.7
  • 14
    • 0037081391 scopus 로고    scopus 로고
    • Construction of recombinant targeting immunogens incorporating an HIV-1 neutralizing epitope into sites of differing conformational constraint
    • Ho, J., K. S. MacDonald, and B. H. Barber. 2002. Construction of recombinant targeting immunogens incorporating an HIV-1 neutralizing epitope into sites of differing conformational constraint. Vaccine 20:1169-1180.
    • (2002) Vaccine , vol.20 , pp. 1169-1180
    • Ho, J.1    MacDonald, K.S.2    Barber, B.H.3
  • 15
    • 0031743949 scopus 로고    scopus 로고
    • A conformation-specific monoclonal antibody reacting with fusion-active gp41 from the human immunodeficiency virus type 1 envelope glycoprotein
    • Jiang, S., K. Lin, and M. Lu. 1998. A conformation-specific monoclonal antibody reacting with fusion-active gp41 from the human immunodeficiency virus type 1 envelope glycoprotein. J. Virol. 72:10213-10217.
    • (1998) J. Virol. , vol.72 , pp. 10213-10217
    • Jiang, S.1    Lin, K.2    Lu, M.3
  • 17
    • 0037195784 scopus 로고    scopus 로고
    • Enhancement of alpha-helicity in the HIV-1 inhibitory peptide DP178 leads to an increased affinity for human monoclonal antibody 2F5 but does not elicit neutralizing responses in vitro. Implications for vaccine design
    • Joyce, J. G., W. M. Hurni, M. J. Bogusky, V. M. Garsky, X. Liang, M. P. Citron, R. C. Danzeisen, M. D. Miller, J. W. Shiver, and P. M. Keller. 2002. Enhancement of alpha-helicity in the HIV-1 inhibitory peptide DP178 leads to an increased affinity for human monoclonal antibody 2F5 but does not elicit neutralizing responses in vitro. Implications for vaccine design. J. Biol. Chem. 277:45811-45820.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45811-45820
    • Joyce, J.G.1    Hurni, W.M.2    Bogusky, M.J.3    Garsky, V.M.4    Liang, X.5    Citron, M.P.6    Danzeisen, R.C.7    Miller, M.D.8    Shiver, J.W.9    Keller, P.M.10
  • 18
    • 0038467539 scopus 로고    scopus 로고
    • Direct evidence that C-peptide inhibitors of human immunodeficiency virus type 1 entry bind to the gp41 N-helical domain in receptor-activated viral envelope
    • Kilgore, N. R., K. Salzwedel, M. Reddick, G. P. Allaway, and C. T. Wild. 2003. Direct evidence that C-peptide inhibitors of human immunodeficiency virus type 1 entry bind to the gp41 N-helical domain in receptor-activated viral envelope. J. Virol. 77:7669-7672.
    • (2003) J. Virol. , vol.77 , pp. 7669-7672
    • Kilgore, N.R.1    Salzwedel, K.2    Reddick, M.3    Allaway, G.P.4    Wild, C.T.5
  • 20
    • 0034606680 scopus 로고    scopus 로고
    • Stable recombinant expression of the anti HIV-1 monoclonal antibody 2F5 after IgG3/IgG1 subclass switch in CHO cells
    • Kunert, R., W. Steinfellner, M. Purtscher, A. Assadian, and H. Katinger. 2000. Stable recombinant expression of the anti HIV-1 monoclonal antibody 2F5 after IgG3/IgG1 subclass switch in CHO cells. Biotechnol. Bioeng. 67:97-103.
    • (2000) Biotechnol. Bioeng. , vol.67 , pp. 97-103
    • Kunert, R.1    Steinfellner, W.2    Purtscher, M.3    Assadian, A.4    Katinger, H.5
  • 21
    • 0031441562 scopus 로고    scopus 로고
    • A trimeric structural subdomain of the HIV-1 transmembrane glycoprotein
    • Lu, M., and P. S. Kim. 1997. A trimeric structural subdomain of the HIV-1 transmembrane glycoprotein. J. Biomol. Struct. Dyn. 15:465-471.
    • (1997) J. Biomol. Struct. Dyn. , vol.15 , pp. 465-471
    • Lu, M.1    Kim, P.S.2
  • 22
    • 0037340005 scopus 로고    scopus 로고
    • HIV-1 envelope proteins complete their folding into six-helix bundles immediately after fusion pore formation
    • Markosyan, R. M., F. S. Cohen, and G. B. Melikyan. 2003. HIV-1 envelope proteins complete their folding into six-helix bundles immediately after fusion pore formation. Mol. Biol. Cell 14:926-938.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 926-938
    • Markosyan, R.M.1    Cohen, F.S.2    Melikyan, G.B.3
  • 25
    • 0029040825 scopus 로고
    • Multifaceted consequences of anti-gp41 monoclonal antibody 2F5 binding to HIV type 1 virions
    • Neurath, A. R., N. Strick, K. Lin, and S. Jiang. 1995. Multifaceted consequences of anti-gp41 monoclonal antibody 2F5 binding to HIV type 1 virions. AIDS Res. Hum. Retrovir. 11:687-696.
    • (1995) AIDS Res. Hum. Retrovir. , vol.11 , pp. 687-696
    • Neurath, A.R.1    Strick, N.2    Lin, K.3    Jiang, S.4
  • 26
    • 1242281320 scopus 로고    scopus 로고
    • October 2000. World Intellectual Property Organization patent WO-00/61618
    • Pai, E. F., M. H. Klein, P. Chong, and A. Pedyczak. October 2000. World Intellectual Property Organization patent WO-00/61618.
    • Pai, E.F.1    Klein, M.H.2    Chong, P.3    Pedyczak, A.4
  • 27
    • 0034755554 scopus 로고    scopus 로고
    • Fine definition of the epitope on the gp41 glycoprotein of human immunodeficiency virus type 1 for the neutralizing monoclonal antibody 2F5
    • Parker, C. E., L. J. Deterding, C. Hager-Braun, J. M. Binley, N. Schulke, H. Katinger, J. P. Moore, and K. B. Tomer. 2001. Fine definition of the epitope on the gp41 glycoprotein of human immunodeficiency virus type 1 for the neutralizing monoclonal antibody 2F5. J. Virol. 75:10906-10911.
    • (2001) J. Virol. , vol.75 , pp. 10906-10911
    • Parker, C.E.1    Deterding, L.J.2    Hager-Braun, C.3    Binley, J.M.4    Schulke, N.5    Katinger, H.6    Moore, J.P.7    Tomer, K.B.8
  • 29
    • 0031883832 scopus 로고    scopus 로고
    • Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides
    • Rimsky, L. T., D. C. Shugars, and T. J. Matthews. 1998. Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides. J. Virol. 72:986-993.
    • (1998) J. Virol. , vol.72 , pp. 986-993
    • Rimsky, L.T.1    Shugars, D.C.2    Matthews, T.J.3
  • 30
    • 0035793406 scopus 로고    scopus 로고
    • Protein design of an HIV-1 entry inhibitor
    • Root, M. J., M. S. Kay, and P. S. Kim. 2001. Protein design of an HIV-1 entry inhibitor. Science 291:884-888.
    • (2001) Science , vol.291 , pp. 884-888
    • Root, M.J.1    Kay, M.S.2    Kim, P.S.3
  • 31
    • 0028801450 scopus 로고
    • Epitope exposure on functional, oligomeric HIV-1 gp41 molecules
    • Sattentau, Q. J., S. Zolla-Pazner, and P. Poignard. 1995. Epitope exposure on functional, oligomeric HIV-1 gp41 molecules. Virology 206:713-717.
    • (1995) Virology , vol.206 , pp. 713-717
    • Sattentau, Q.J.1    Zolla-Pazner, S.2    Poignard, P.3
  • 32
    • 0035859948 scopus 로고    scopus 로고
    • The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles
    • Schibli, D. J., R. C. Montelaro, and H. J. Vogel. 2001. The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles. Biochemistry 40:9570-9578.
    • (2001) Biochemistry , vol.40 , pp. 9570-9578
    • Schibli, D.J.1    Montelaro, R.C.2    Vogel, H.J.3
  • 33
    • 0035701421 scopus 로고    scopus 로고
    • A potent cross-clade neutralizing human monoclonal antibody against a novel epitope on gp41 of human immunodeficiency virus type 1
    • Stiegler, G., R. Kunert, M. Purtscher, S. Wolbank, R. Voglauer, F. Steindl, and H. Katinger. 2001. A potent cross-clade neutralizing human monoclonal antibody against a novel epitope on gp41 of human immunodeficiency virus type 1. AIDS Res. Hum. Retrovir. 17:1757-1765.
    • (2001) AIDS Res. Hum. Retrovir. , vol.17 , pp. 1757-1765
    • Stiegler, G.1    Kunert, R.2    Purtscher, M.3    Wolbank, S.4    Voglauer, R.5    Steindl, F.6    Katinger, H.7
  • 34
    • 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., W. R. Gallaher, A. Agirre, F. M. Goni, and J. L. Nieva. 2000. Membrane interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein: putative role during viral fusion. J. Virol. 74:8038-8047.
    • (2000) J. Virol. , vol.74 , pp. 8038-8047
    • Suarez, T.1    Gallaher, W.R.2    Agirre, A.3    Goni, F.M.4    Nieva, J.L.5
  • 35
    • 0030780614 scopus 로고    scopus 로고
    • Atomic structure of a thermostable subdomain of HIV-1 gp41
    • Tan, K., J. Liu, J. Wang, S. Shen, and M. Lu. 1997. Atomic structure of a thermostable subdomain of HIV-1 gp41. Proc. Natl. Acad. Sci. USA 94:12303-12308.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12303-12308
    • Tan, K.1    Liu, J.2    Wang, J.3    Shen, S.4    Lu, M.5
  • 36
    • 0027483786 scopus 로고
    • Characterization of stable Chinese hamster ovary cells expressing wild-type, secreted, and glycosylphosphatidylinositol-anchored human immunodeficiency virus type 1 envelope glycoprotein
    • Weiss, C. D., and J. M. White. 1993. Characterization of stable Chinese hamster ovary cells expressing wild-type, secreted, and glycosylphosphatidylinositol-anchored human immunodeficiency virus type 1 envelope glycoprotein. J. Virol. 67:7060-7066.
    • (1993) J. Virol. , vol.67 , pp. 7060-7066
    • Weiss, C.D.1    White, J.M.2
  • 38
    • 0031798443 scopus 로고    scopus 로고
    • Mutational analysis of residues in the coiled coil domain of the human immunodeficiency virus type-1 (HIV-1) gp41
    • Weng, Y., and C. D. Weiss. 1998. Mutational analysis of residues in the coiled coil domain of the human immunodeficiency virus type-1 (HIV-1) gp41. J. Virol. 72:9676-9682.
    • (1998) J. Virol. , vol.72 , pp. 9676-9682
    • Weng, Y.1    Weiss, C.D.2
  • 39
    • 0027692502 scopus 로고
    • A synthetic peptide from HIV-1 gp41 is a potent inhibitor of virus-mediated cell-cell fusion
    • Wild, C., T. Greenwell, and T. Matthews. 1993. A synthetic peptide from HIV-1 gp41 is a potent inhibitor of virus-mediated cell-cell fusion. AIDS Res. Hum. Retrovir. 9:1051-1053.
    • (1993) AIDS Res. Hum. Retrovir. , vol.9 , pp. 1051-1053
    • Wild, C.1    Greenwell, T.2    Matthews, T.3
  • 40
    • 0026465468 scopus 로고
    • A synthetic peptide inhibitor of human immunodeficiency virus replication: Correlation between solution structure and viral inhibition
    • Wild, C., T. Oas, C. McDanal, D. Bolognesi, and T. Matthews. 1992. A synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibition. Proc. Natl. Acad. Sci. USA 89:10537-10541.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10537-10541
    • Wild, C.1    Oas, T.2    McDanal, C.3    Bolognesi, D.4    Matthews, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.