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Volumn 73, Issue 5, 1999, Pages 4433-4438

Subdomain folding and biological activity of the core structure from human immunodeficiency virus type 1 gp41: Implications for viral membrane fusion

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; CELL FUSION; HUMAN IMMUNODEFICIENCY VIRUS 1; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; VIRUS CELL INTERACTION; VIRUS CORE; VIRUS ENVELOPE;

EID: 0032899254     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.73.5.4433-4438.1999     Document Type: Article
Times cited : (66)

References (42)
  • 1
    • 0028023726 scopus 로고
    • Structure of influenza hemagglutinin at the pH of membrane fusion
    • Bullough, P. A., F. M. Hughson, J. J. Skehel, and D. C. Wiley. 1994. Structure of influenza hemagglutinin at the pH of membrane fusion. Nature 371:37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 3
    • 0027499917 scopus 로고
    • Effects of amino acid changes in the extracellular domain of the human immunodeficiency virus type 1 gp41 envelope glycoprotein
    • Cao, J., L. Bergeron, E. Helseth, M. Thali, H. Repke, and J. Sodroski. 1993. Effects of amino acid changes in the extracellular domain of the human immunodeficiency virus type 1 gp41 envelope glycoprotein. J. Virol. 67:2747-2755.
    • (1993) J. Virol. , vol.67 , pp. 2747-2755
    • Cao, J.1    Bergeron, L.2    Helseth, E.3    Thali, M.4    Repke, H.5    Sodroski, J.6
  • 4
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr, C. M., and P. S. Kim. 1993. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73:823-832.
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 5
    • 0031460632 scopus 로고    scopus 로고
    • Influenza hemagglutinin is spring-loaded by a metastable native conformation
    • Carr, C. M., C. Chaudhry, and P. S. Kim. 1997. Influenza hemagglutinin is spring-loaded by a metastable native conformation. Proc. Natl. Acad. Sci. USA 94:14306-14313.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14306-14313
    • Carr, C.M.1    Chaudhry, C.2    Kim, P.S.3
  • 6
    • 0025678671 scopus 로고
    • Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins
    • Chambers, P., C. R. Pringle, and A. J. Easton. 1990. Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins. J. Gen. Virol. 71:3075-3080.
    • (1990) J. Gen. Virol. , vol.71 , pp. 3075-3080
    • Chambers, P.1    Pringle, C.R.2    Easton, A.J.3
  • 7
    • 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
  • 8
    • 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
  • 9
    • 0029072191 scopus 로고
    • A molecular clasp in the human immunodeficiency virus (HIV) type 1 TM protein determines the anti-HIV activity of gp41 derivatives: Implication for viral fusion
    • Chen, C.-H., T. J. Matthews, C. B. McDanal, D. P. Bolognesi, and M. L. Greenberg. 1995. A molecular clasp in the human immunodeficiency virus (HIV) type 1 TM protein determines the anti-HIV activity of gp41 derivatives: implication for viral fusion. J. Virol. 69:3771-3777.
    • (1995) J. Virol. , vol.69 , pp. 3771-3777
    • Chen, C.-H.1    Matthews, T.J.2    McDanal, C.B.3    Bolognesi, D.P.4    Greenberg, M.L.5
  • 10
    • 0029558245 scopus 로고
    • A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation
    • Chen, J., S. A. Wharton, W. Weissenhorn, L. J. Calder, F. M. Hughson, J. J. Skehel, and D. C. Wiley. 1994. A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation. Proc. Natl. Acad. Sci. USA 92:12205-12209.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 12205-12209
    • Chen, J.1    Wharton, S.A.2    Weissenhorn, W.3    Calder, L.J.4    Hughson, F.M.5    Skehel, J.J.6    Wiley, D.C.7
  • 11
    • 0027266886 scopus 로고
    • Mutational analysis of the leucine zipper-like motif of the human immunodeficiency virus type 1 envelope transmembrane glycoprotein
    • Chen, S. S.-L., C.-N. Lee, W.-R. Lee, K. McIntosh, and T.-H. Lee. 1993. Mutational analysis of the leucine zipper-like motif of the human immunodeficiency virus type 1 envelope transmembrane glycoprotein. J. Virol. 67: 3615-3619.
    • (1993) J. Virol. , vol.67 , pp. 3615-3619
    • Chen, S.S.-L.1    Lee, C.-N.2    Lee, W.-R.3    McIntosh, K.4    Lee, T.-H.5
  • 12
    • 0025010813 scopus 로고
    • Retroviral envelope glycoproteins contain a leucine zipper like repeat
    • Delwart, E. J., G. Mosialos, and T. Gilmore. 1990. Retroviral envelope glycoproteins contain a leucine zipper like repeat. AIDS Res. Hum. Retroviruses 6:703-706.
    • (1990) AIDS Res. Hum. Retroviruses , vol.6 , pp. 703-706
    • Delwart, E.J.1    Mosialos, G.2    Gilmore, T.3
  • 13
    • 0031470456 scopus 로고    scopus 로고
    • How do viruses enter cells? The HIV coreceptors teach us a lesson of complexity
    • Dimitrov, D. S. 1997. How do viruses enter cells? The HIV coreceptors teach us a lesson of complexity. Cell 91:721-730.
    • (1997) Cell , vol.91 , pp. 721-730
    • Dimitrov, D.S.1
  • 14
    • 0026652457 scopus 로고
    • Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity
    • Dubay, J. W., S. J. Roberts, B. Brody, and E. Hunter. 1992. Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity. J. Virol. 66:4748-4756.
    • (1992) J. Virol. , vol.66 , pp. 4748-4756
    • Dubay, J.W.1    Roberts, S.J.2    Brody, B.3    Hunter, E.4
  • 15
    • 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
  • 18
    • 0029156388 scopus 로고
    • Molecular mechanisms of protein-mediated membrane fusion
    • Hughson, F. M. 1995. Molecular mechanisms of protein-mediated membrane fusion. Curr. Opin. Struct. Biol. 5:507-513.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 507-513
    • Hughson, F.M.1
  • 20
    • 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
  • 22
    • 0019756004 scopus 로고
    • Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques
    • Johnson, M. L., J. J. Correia, D. A. Yphantis, and H. R. Halvorson. 1981. Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques. Biophys. J. 36:575-588.
    • (1981) Biophys. J. , vol.36 , pp. 575-588
    • Johnson, M.L.1    Correia, J.J.2    Yphantis, D.A.3    Halvorson, H.R.4
  • 23
    • 0031473771 scopus 로고    scopus 로고
    • Inhibition of HIV type 1 infectivity by constrained α-helical peptides: Implications for the viral fusion mechanism
    • Judice, J. K., J. Y. K. Tom, W. Huang, T. Wrin, J. Vennari, C. J. Petropoulos, and R. S. McDowell. 1997. Inhibition of HIV type 1 infectivity by constrained α-helical peptides: implications for the viral fusion mechanism. Proc. Natl. Acad. Sci. USA 94:13426-13430.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13426-13430
    • Judice, J.K.1    Tom, J.Y.K.2    Huang, W.3    Wrin, T.4    Vennari, J.5    Petropoulos, C.J.6    McDowell, R.S.7
  • 24
    • 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
  • 25
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • S. E. Harding, A. J. Rowe, and J. C. Horton (ed.), Royal Society of Chemistry, Cambridge, England
    • Laue, T. M., B. D. Shah, T. M. Ridgeway, and S. L. Pelletier. 1992. Computer-aided interpretation of analytical sedimentation data for proteins, p. 90-125. In S. E. Harding, A. J. Rowe, and J. C. Horton (ed.), Analytical ultracentrifugation in biochemistry and polymer science. Royal Society of Chemistry, Cambridge, England.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 26
    • 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
  • 27
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu, M., S. C. Blacklow, and P. S. Kim. 1995. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nat. Struct. Biol. 2:1075-1082.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 28
    • 0000557449 scopus 로고    scopus 로고
    • Human immunodeficiency viruses and their replication
    • B. N. Fields, D. M. Knipe, P. M. Howley, R. M. Chanock, J. L. Melnick, T. P. Monath, B. Roizman, and S. E. Straus (ed.), Lippincott-Raven Publishers, Philadelphia, Pa.
    • Luciw, P. A. 1996. Human immunodeficiency viruses and their replication, p. 1881-1952. In B. N. Fields, D. M. Knipe, P. M. Howley, R. M. Chanock, J. L. Melnick, T. P. Monath, B. Roizman, and S. E. Straus (ed.), Fields virology. Lippincott-Raven Publishers, Philadelphia, Pa.
    • (1996) Fields Virology , pp. 1881-1952
    • Luciw, P.A.1
  • 29
    • 0000476294 scopus 로고
    • The HIV-cell fusion reaction
    • J. Bentz (ed.), CRC Press, Inc., Boca Raton, Fla.
    • Moore, J. P., B. A. Jameson, R. A. Weiss, and Q. J. Sattentau. 1993. The HIV-cell fusion reaction, p. 233-289. In J. Bentz (ed.), Viral fusion mechanisms. CRC Press, Inc., Boca Raton, Fla.
    • (1993) Viral Fusion Mechanisms , pp. 233-289
    • Moore, J.P.1    Jameson, B.A.2    Weiss, R.A.3    Sattentau, Q.J.4
  • 30
    • 0038065763 scopus 로고
    • Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41
    • Munoz-Barroso, I., S. Durell, K. Sakaguchi, E. Appella, and R. Blumenthal. 1988. Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41. J. Cell Biol. 140:315-323.
    • (1988) J. Cell Biol. , vol.140 , pp. 315-323
    • Munoz-Barroso, I.1    Durell, S.2    Sakaguchi, K.3    Appella, E.4    Blumenthal, R.5
  • 31
    • 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
  • 33
    • 0002506954 scopus 로고
    • Influenza virus fusion: From models toward a mechanism
    • J. Bentz, (ed.), CRC Press, Boca Raton, Fla.
    • Stegmann, T., and A. Helenius. 1993. Influenza virus fusion: from models toward a mechanism, p. 89-111. In J. Bentz, (ed.), Viral fusion mechanisms. CRC Press, Boca Raton, Fla.
    • (1993) Viral Fusion Mechanisms , pp. 89-111
    • Stegmann, T.1    Helenius, A.2
  • 34
    • 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
    • 0026492542 scopus 로고
    • Membrane fusion
    • White, J. M. 1992. Membrane fusion. Science 258:917-924.
    • (1992) Science , vol.258 , pp. 917-924
    • White, J.M.1
  • 37
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive α-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • Wild, C. T., D. C. Shugars, T. K. Greenwell, C. B. McDanal, and T. J. Matthews. 1994. Peptides corresponding to a predictive α-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc. Natl. Acad. Sci. USA 91:9770-9774.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9770-9774
    • Wild, C.T.1    Shugars, D.C.2    Greenwell, T.K.3    McDanal, C.B.4    Matthews, T.J.5
  • 38
    • 0028575843 scopus 로고
    • Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex
    • Wild, C. T., J. W. Dubay, T. K. Greenwell, T. Baird, Jr., T. G. Oas, C. B. McDanal, E. Hunter, and T. J. Matthews. 1994. Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex. Proc. Natl. Acad. Sci. USA 91:12676-12680.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12676-12680
    • Wild, C.T.1    Dubay, J.W.2    Greenwell, T.K.3    Baird T., Jr.4    Oas, T.G.5    McDanal, C.B.6    Hunter, E.7    Matthews, T.J.8
  • 39
    • 0028953212 scopus 로고
    • The inhibitory activity of an HIV-1 type peptide correlates with its ability to interact with a leucine zipper structure
    • Wild, C. T., T. Greenwell, D. Shugars, L. Rimsky-Clarke, and T. Matthews. 1995. The inhibitory activity of an HIV-1 type peptide correlates with its ability to interact with a leucine zipper structure. AIDS Res. Hum. Retroviruses 11:323-325.
    • (1995) AIDS Res. Hum. Retroviruses , vol.11 , pp. 323-325
    • Wild, C.T.1    Greenwell, T.2    Shugars, D.3    Rimsky-Clarke, L.4    Matthews, T.5
  • 40
    • 0026465468 scopus 로고
    • A synthetic peptide inhibitor of human immunodeficiency virus replication: Correlation between solution structure and viral inhibition
    • Wild, C. T., T. Oas, C. B. McDanal, D. Bolognesi, and T. J. 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.T.1    Oas, T.2    McDanal, C.B.3    Bolognesi, D.4    Matthews, T.J.5
  • 41
    • 0023082135 scopus 로고
    • The structure and function of the hemagglutinin membrane glycoprotein of influenza virus
    • Wiley, D. C., and J. J. Skehel. 1987. The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu. Rev. Biochem. 56:365-394.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 365-394
    • Wiley, D.C.1    Skehel, J.J.2
  • 42
    • 0030230746 scopus 로고    scopus 로고
    • HIV-1: Cofactors provide the entry keys
    • Wilkinson, D. 1996. HIV-1: cofactors provide the entry keys. Curr. Biol. 6: 1051-1053.
    • (1996) Curr. Biol. , vol.6 , pp. 1051-1053
    • Wilkinson, D.1


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