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Volumn 83, Issue 9, 2009, Pages 4121-4126

Intersubunit interactions modulate pH-induced activation of membrane fusion by the Junín virus envelope glycoprotein GPC

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN;

EID: 66149085621     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.02410-08     Document Type: Article
Times cited : (59)

References (48)
  • 1
    • 34247118403 scopus 로고    scopus 로고
    • Bitopic membrane topology of the stable signal peptide in the tripartite Junín virus GP-C envelope glycoprotein complex
    • DOI 10.1128/JVI.02779-06
    • Agnihothram, S. S., J. York, M. Trahey, and J. H. Nunberg. 2007. Bitopic membrane topology of the stable signal peptide in the tripartite Junín virus GP-C envelope glycoprotein complex. J. Virol. 81:4331-4337. (Pubitemid 46586927)
    • (2007) Journal of Virology , vol.81 , Issue.8 , pp. 4331-4337
    • Agnihothram, S.S.1    York, J.2    Trahey, M.3    Nunberg, J.H.4
  • 2
    • 0037372280 scopus 로고    scopus 로고
    • Endoproteolytic processing of the lymphocytic choriomeningitis virus glycoprotein by the subtilase SKI-1/S1P
    • DOI 10.1128/JVI.77.5.2866-2872.2003
    • Beyer, W. R., D. Popplau, W. Garten, D. von Laer, and O. Lenz. 2003. Endoproteolytic processing of the lymphocytic choriomeningitis virus glycoprotein by the subtilase SKI-1/S1P. J. Virol. 77:2866-2872. (Pubitemid 36228070)
    • (2003) Journal of Virology , vol.77 , Issue.5 , pp. 2866-2872
    • Beyer, W.R.1    Popplau, D.2    Garten, W.3    Von Laer, D.4    Lenz, O.5
  • 4
    • 0028365697 scopus 로고
    • Mechanism of lymphocytic choriomeningitis virus entry into cells
    • Borrow, P., and M. B. A. Oldstone. 1994. Mechanism of lymphocytic choriomeningitis virus entry into cells. Virology 198:1-9.
    • (1994) Virology , vol.198 , pp. 1-9
    • Borrow, P.1    Oldstone, M.B.A.2
  • 5
    • 0034954578 scopus 로고    scopus 로고
    • Second-site suppressors of Rous sarcoma virus Ca mutations: Evidence for interdomain interactions
    • Bowzard, J. B., J. W. Wills, and R. C. Craven. 2001. Second-site suppressors of Rous sarcoma virus Ca mutations: evidence for interdomain interactions. J. Virol. 75:6850-6856.
    • (2001) J. Virol. , vol.75 , pp. 6850-6856
    • Bowzard, J.B.1    Wills, J.W.2    Craven, R.C.3
  • 6
    • 0036191901 scopus 로고    scopus 로고
    • Arenaviruses: Protein structure and function
    • Buchmeier, M. J. 2002. Arenaviruses: protein structure and function. Curr. Top. Microbiol. Immunol. 262:159-173.
    • (2002) Curr. Top. Microbiol. Immunol. , vol.262 , pp. 159-173
    • Buchmeier, M.J.1
  • 7
    • 0001142645 scopus 로고    scopus 로고
    • Arenaviruses and their replication
    • D. M. Knipe and P. M. Howley (ed.), Lippincott, Williams & Wilkins, Philadelphia, PA
    • Buchmeier, M. J., M. D. Bowen, and C. J. Peters. 2001. Arenaviruses and their replication, p. 1635-1668. In D. M. Knipe and P. M. Howley (ed.), Fields virology, vol.2. Lippincott, Williams & Wilkins, Philadelphia, PA.
    • (2001) Fields Virology , vol.2 , pp. 1635-1668
    • Buchmeier, M.J.1    Bowen, M.D.2    Peters, C.J.3
  • 9
    • 0029812792 scopus 로고    scopus 로고
    • Low-pH-induced fusion of Vero cells infected with Junin virus
    • Castilla, V., and S. E. Mersich. 1996. Low-pH-induced fusion of Vero cells infected with Junin virus. Arch. Virol. 141:1307-1317. (Pubitemid 26324856)
    • (1996) Archives of Virology , vol.141 , Issue.7 , pp. 1307-1317
    • Castilla, V.1    Mersich, S.E.2
  • 12
    • 0029042344 scopus 로고
    • Kinetics and pH dependence of acid-induced structural changes in the lymphocytic choriomeningitis virus glycoprotein complex
    • Di Simone, C., and M. J. Buchmeier. 1995. Kinetics and pH dependence of acid-induced structural changes in the lymphocytic choriomeningitis virus glycoprotein complex. Virology 209:3-9.
    • (1995) Virology , vol.209 , pp. 3-9
    • Di Simone, C.1    Buchmeier, M.J.2
  • 13
    • 0028241840 scopus 로고
    • Acidic pH triggers LCMV membrane fusion activity and conformational change in the glycoprotein spike
    • Di Simone, C., M. A. Zandonatti, and M. J. Buchmeier. 1994. Acidic pH triggers LCMV membrane fusion activity and conformational change in the glycoprotein spike. Virology 198:455-465.
    • (1994) Virology , vol.198 , pp. 455-465
    • Di Simone, C.1    Zandonatti, M.A.2    Buchmeier, M.J.3
  • 14
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • DOI 10.1146/annurev.biochem.70.1.777
    • Eckert, D. M., and P. S. Kim. 2001. Mechanisms of viral membrane fusion and its inhibition. Annu. Rev. Biochem. 70:777-810. (Pubitemid 32662225)
    • (2001) Annual Review of Biochemistry , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 15
    • 0346242739 scopus 로고    scopus 로고
    • Identification of Lassa virus glycoprotein signal peptide as a trans-acting maturation factor
    • DOI 10.1038/sj.embor.7400002
    • Eichler, R., O. Lenz, T. Strecker, M. Eickmann, H. D. Klenk, and W. Garten. 2003. Identification of Lassa virus glycoprotein signal peptide as a transacting maturation factor. EMBO Rep. 4:1084-1088. (Pubitemid 37527428)
    • (2003) EMBO Reports , vol.4 , Issue.11 , pp. 1084-1088
    • Eichler, R.1    Lenz, O.2    Strecker, T.3    Eickmann, M.4    Klenk, H.-D.5    Garten, W.6
  • 16
    • 0031041242 scopus 로고    scopus 로고
    • Mutational analysis of the oligomer assembly domain in the transmembrane subunit of the Rous sarcoma virus glycoprotein
    • Einfeld, D. A., and E. Hunter. 1997. Mutational analysis of the oligomer assembly domain in the transmembrane subunit of the Rous sarcoma virus glycoprotein. J. Virol. 71:2383-2389. (Pubitemid 27078621)
    • (1997) Journal of Virology , vol.71 , Issue.3 , pp. 2383-2389
    • Einfeld, D.A.1    Hunter, E.2
  • 17
    • 33744935523 scopus 로고    scopus 로고
    • Identification of an N-terminal trimeric coiled-coil core within arenavirus glycoprotein 2 permits assignment to class I viral fusion proteins
    • DOI 10.1128/JVI.00008-06
    • Eschli, B., K. Quirin, A. Wepf, J. Weber, R. Zinkernagel, and H. Hengartner. 2006. Identification of an N-terminal trimeric coiled-coil core within arenavirus glycoprotein 2 permits assignment to class I viral fusion proteins. J. Virol. 80:5897-5907. (Pubitemid 43849167)
    • (2006) Journal of Virology , vol.80 , Issue.12 , pp. 5897-5907
    • Eschli, B.1    Quirin, K.2    Wepf, A.3    Weber, J.4    Zinkernagel, R.5    Hengartner, H.6
  • 18
    • 37849036757 scopus 로고    scopus 로고
    • New world clade B arenaviruses can use transferrin receptor 1 (TfR1)-dependent and -independent entry pathways, and glycoproteins from human pathogenic strains are associated with the use of TfR1
    • Flanagan, M. L., J. Oldenburg, T. Reignier, N. Holt, G. A. Hamilton, V. K. Martin, and P. M. Cannon. 2008. New world clade B arenaviruses can use transferrin receptor 1 (TfR1)-dependent and -independent entry pathways, and glycoproteins from human pathogenic strains are associated with the use of TfR1. J. Virol. 82:938-948.
    • (2008) J. Virol. , vol.82 , pp. 938-948
    • Flanagan, M.L.1    Oldenburg, J.2    Reignier, T.3    Holt, N.4    Hamilton, G.A.5    Martin, V.K.6    Cannon, P.M.7
  • 19
    • 0000233999 scopus 로고
    • Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase
    • Fuerst, T. R., E. G. Niles, F. W. Studier, and B. Moss. 1986. Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase. Proc. Natl. Acad. Sci. USA 83:8122-8126.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8122-8126
    • Fuerst, T.R.1    Niles, E.G.2    Studier, F.W.3    Moss, B.4
  • 20
    • 3142545672 scopus 로고    scopus 로고
    • The viral transmembrane superfamily: Possible divergence of arenavirus and filovirus glycoproteins from a common RNA virus ancestor
    • Gallaher, W. R., C. DiSimone, and M. J. Buchmeier. 2001. The viral transmembrane superfamily: possible divergence of arenavirus and filovirus glycoproteins from a common RNA virus ancestor. BMC Microbiol. 1:1.
    • (2001) BMC Microbiol. , vol.1 , pp. 1
    • Gallaher, W.R.1    Disimone, C.2    Buchmeier, M.J.3
  • 21
    • 0025807536 scopus 로고
    • Molecular organization of Junin virus S RNA: Complete nucleotide sequence, relationship with other members of the Arenaviridae and unusual secondary structures
    • Ghiringhelli, P. D., R. V. Rivera-Pomar, M. E. Lozano, O. Grau, and V. Romanowski. 1991. Molecular organization of Junin virus S RNA: complete nucleotide sequence, relationship with other members of the Arenaviridae and unusual secondary structures. J. Gen. Virol. 72:2129-2141.
    • (1991) J. Gen. Virol. , vol.72 , pp. 2129-2141
    • Ghiringhelli, P.D.1    Rivera-Pomar, R.V.2    Lozano, M.E.3    Grau, O.4    Romanowski, V.5
  • 23
    • 0030753409 scopus 로고    scopus 로고
    • Structure-based identification of an inducer of the low-pH conformational change in the influenza virus hemagglutinin: Irreversible inhibition of infectivity
    • Hoffman, L. R., I. D. Kuntz, and J. M. White. 1997. Structure-based identification of an inducer of the low-pH conformational change in the influenza virus hemagglutinin: irreversible inhibition of infectivity. J. Virol. 71:8808-8820.
    • (1997) J. Virol. , vol.71 , pp. 8808-8820
    • Hoffman, L.R.1    Kuntz, I.D.2    White, J.M.3
  • 24
    • 0018827621 scopus 로고
    • Identification of a virus-specified protein in the nucleus of vaccinia virus-infected cells
    • Hruby, D. E., D. L. Lynn, and J. R. Kates. 1980. Identification of a virus-specified protein in the nucleus of vaccinia virus-infected cells. J. Gen. Virol. 47:293-299. (Pubitemid 10092463)
    • (1980) Journal of General Virology , vol.47 , Issue.2 , pp. 293-299
    • Hruby, D.E.1    Lynn, D.L.2    Kates, J.R.3
  • 25
    • 34548813656 scopus 로고    scopus 로고
    • Structure of acid-sensing ion channel 1 at 1.9 a resolution and low pH
    • Jasti, J., H. Furukawa, E. B. Gonzales, and E. Gouaux. 2007. Structure of acid-sensing ion channel 1 at 1.9 A resolution and low pH. Nature 449:316-323.
    • (2007) Nature , vol.449 , pp. 316-323
    • Jasti, J.1    Furukawa, H.2    Gonzales, E.B.3    Gouaux, E.4
  • 26
    • 0141680276 scopus 로고    scopus 로고
    • Mechanisms for lymphocytic choriomeningitis virus glycoprotein cleavage, transport, and incorporation into virions
    • Kunz, S., K. H. Edelmann, J.-C. de la Torre, R. Gorney, and M. B. A. Oldstone. 2003. Mechanisms for lymphocytic choriomeningitis virus glycoprotein cleavage, transport, and incorporation into virions. Virology 314:168-178.
    • (2003) Virology , vol.314 , pp. 168-178
    • Kunz, S.1    Edelmann, K.H.2    De La Torre, J.-C.3    Gorney, R.4    Oldstone, M.B.A.5
  • 29
    • 0034466514 scopus 로고    scopus 로고
    • Identification of a novel consensus sequence at the cleavage site of the Lassa virus glycoprotein
    • Lenz, O., J. ter Meulen, H. Feldmann, H.-D. Klenk, and W. Garten. 2000. Identification of a novel consensus sequence at the cleavage site of the Lassa virus glycoprotein. J. Virol. 74:11418-11421.
    • (2000) J. Virol. , vol.74 , pp. 11418-11421
    • Lenz, O.1    Ter Meulen, J.2    Feldmann, H.3    Klenk, H.-D.4    Garten, W.5
  • 31
    • 0028129959 scopus 로고
    • Fusogenic mechanisms of enveloped-virus glycoproteins analyzed by a novel recombinant vaccinia virus-based assay quantitating cell fusion-dependent reporter gene activation
    • Nussbaum, O., C. C. Broder, and E. A. Berger. 1994. Fusogenic mechanisms of enveloped-virus glycoproteins analyzed by a novel recombinant vaccinia virus-based assay quantitating cell fusion-dependent reporter gene activation. J. Virol. 68:5411-5422. (Pubitemid 24258553)
    • (1994) Journal of Virology , vol.68 , Issue.9 , pp. 5411-5422
    • Nussbaum, O.1    Broder, C.C.2    Berger, E.A.3
  • 32
    • 0028875256 scopus 로고
    • Structural requirements in the membrane-spanning domain of the paramyxovirus HN protein for the formation of a stable tetramer
    • Parks, G. D., and S. Pohlmann. 1995. Structural requirements in the membrane-spanning domain of the paramyxovirus HN protein for the formation of a stable tetramer. Virology 213:263-270.
    • (1995) Virology , vol.213 , pp. 263-270
    • Parks, G.D.1    Pohlmann, S.2
  • 38
    • 0036232837 scopus 로고    scopus 로고
    • New World arenavirus clade C, but not clade a and B viruses, utilizes α-dystroglycan as its major receptor
    • Spiropoulou, C. F., S. Kunz, P. E. Rollin, K. P. Campbell, and M. B. A. Oldstone. 2002. New World arenavirus clade C, but not clade A and B viruses, utilizes α-dystroglycan as its major receptor. J. Virol. 76:5140-5146.
    • (2002) J. Virol. , vol.76 , pp. 5140-5146
    • Spiropoulou, C.F.1    Kunz, S.2    Rollin, P.E.3    Campbell, K.P.4    Oldstone, M.B.A.5
  • 39
    • 0029828938 scopus 로고    scopus 로고
    • Studies using double mutants of the conformational transitions in influenza hemagglutinin required for its membrane fusion activity
    • Steinhauer, D. A., J. Martin, Y. P. Lin, S. A. Wharton, M. B. Oldstone, J. J. Skehel, and D. C. Wiley. 1996. Studies using double mutants of the conformational transitions in influenza hemagglutinin required for its membrane fusion activity. Proc. Natl. Acad. Sci. USA 93:12873-12878.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12873-12878
    • Steinhauer, D.A.1    Martin, J.2    Lin, Y.P.3    Wharton, S.A.4    Oldstone, M.B.5    Skehel, J.J.6    Wiley, D.C.7
  • 40
    • 0026343370 scopus 로고
    • Amantadine selection of a mutant influenza virus containing an acid-stable hemagglutinin glycoprotein: Evidence for virus-specific regulation of the pH of glycoprotein transport vesicles
    • Steinhauer, D. A., S. A. Wharton, J. J. Skehel, D. C. Wiley, and A. J. Hay. 1991. Amantadine selection of a mutant influenza virus containing an acid-stable hemagglutinin glycoprotein: evidence for virus-specific regulation of the pH of glycoprotein transport vesicles. Proc. Natl. Acad. Sci. USA 88:11525-11529.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11525-11529
    • Steinhauer, D.A.1    Wharton, S.A.2    Skehel, J.J.3    Wiley, D.C.4    Hay, A.J.5
  • 41
    • 36749003222 scopus 로고    scopus 로고
    • Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion
    • Thoennes, S., Z. N. Li, B. J. Lee, W. A. Langley, J. J. Skehel, R. J. Russell, and D. A. Steinhauer. 2008. Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion. Virology 370:403-414.
    • (2008) Virology , vol.370 , pp. 403-414
    • Thoennes, S.1    Li, Z.N.2    Lee, B.J.3    Langley, W.A.4    Skehel, J.J.5    Russell, R.J.6    Steinhauer, D.A.7
  • 42
    • 45849108331 scopus 로고    scopus 로고
    • Structures and mechanisms of viral membrane fusion proteins: Multiple variations on a common theme
    • White, J. M., S. E. Delos, M. Brecher, and K. Schornberg. 2008. Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme. Crit. Rev. Biochem. Mol. Biol. 43:189-219.
    • (2008) Crit. Rev. Biochem. Mol. Biol. , vol.43 , pp. 189-219
    • White, J.M.1    Delos, S.E.2    Brecher, M.3    Schornberg, K.4
  • 43
    • 27744594720 scopus 로고    scopus 로고
    • Genetic analysis of heptad-repeat regions in the G2 fusion subunit of the Junin arenavirus envelope glycoprotein
    • York, J., S. S. Agnihothram, V. Romanowski, and J. H. Nunberg. 2005. Genetic analysis of heptad-repeat regions in the G2 fusion subunit of the Junin arenavirus envelope glycoprotein. Virology 343:267-279.
    • (2005) Virology , vol.343 , pp. 267-279
    • York, J.1    Agnihothram, S.S.2    Romanowski, V.3    Nunberg, J.H.4
  • 44
    • 55249103905 scopus 로고    scopus 로고
    • PH-induced activation of arenavirus membrane fusion is antagonized by small-molecule inhibitors
    • DOI 10.1128/JVI.01140-08
    • York, J., D. Dai, S. A. Amberg, and J. H. Nunberg. 2008. pH-induced activation of arenavirus membrane fusion is antagonized by small-molecule inhibitors. J. Virol. 82:10932-10939. (Pubitemid 352691170)
    • (2008) Journal of Virology , vol.82 , Issue.21 , pp. 10932-10939
    • York, J.1    Dai, D.2    Amberg, S.M.3    Nunberg, J.H.4
  • 45
    • 33846869707 scopus 로고    scopus 로고
    • Distinct requirements for signal peptidase processing and function of the stable signal peptide (SSP) subunit in the Junin virus envelope glycoprotein
    • York, J., and J. H. Nunberg. 2007. Distinct requirements for signal peptidase processing and function of the stable signal peptide (SSP) subunit in the Junin virus envelope glycoprotein. Virology 359:72-81.
    • (2007) Virology , vol.359 , pp. 72-81
    • York, J.1    Nunberg, J.H.2
  • 46
    • 37049027727 scopus 로고    scopus 로고
    • A novel zinc-binding domain is essential for formation of the functional Junín virus envelope glycoprotein complex
    • DOI 10.1128/JVI.01785-07
    • York, J., and J. H. Nunberg. 2007. A novel zinc-binding domain is essential for formation of the functional Junín virus envelope glycoprotein complex. J. Virol. 81:13385-13391. (Pubitemid 350247835)
    • (2007) Journal of Virology , vol.81 , Issue.24 , pp. 13385-13391
    • York, J.1    Nunberg, J.H.2
  • 47
    • 33746377920 scopus 로고    scopus 로고
    • Role of the stable signal peptide of Junín arenavirus envelope glycoprotein in pH-dependent membrane fusion
    • DOI 10.1128/JVI.00642-06
    • York, J., and J. H. Nunberg. 2006. Role of the stable signal peptide of the Junín arenavirus envelope glycoprotein in pH-dependent membrane fusion. J. Virol. 80:7775-7780. (Pubitemid 44109665)
    • (2006) Journal of Virology , vol.80 , Issue.15 , pp. 7775-7780
    • York, J.1    Nunberg, J.H.2
  • 48
    • 4544266361 scopus 로고    scopus 로고
    • The signal peptide of the Junín arenavirus envelope glycoprotein is myristoylated and forms an essential subunit of the mature G1-G2 complex
    • DOI 10.1128/JVI.78.19.10783-10792.2004
    • York, J., V. Romanowski, M. Lu, and J. H. Nunberg. 2004. The signal peptide of the Junín arenavirus envelope glycoprotein is myristoylated and forms an essential subunit of the mature G1-G2 complex. J. Virol. 78:10783-10792. (Pubitemid 39258403)
    • (2004) Journal of Virology , vol.78 , Issue.19 , pp. 10783-10792
    • York, J.1    Romanowski, V.2    Lu, M.3    Nunberg, J.H.4


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