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Volumn 243, Issue 2, 1998, Pages 380-387

Mutations in the Sindbis virus capsid gene can partially suppress mutations in the cytoplasmic domain of the virus E2 glycoprotein spike

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; COMPLEMENTARY DNA; PLASMID DNA; VIRUS GLYCOPROTEIN; VIRUS PROTEIN;

EID: 0032502761     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1998.9074     Document Type: Article
Times cited : (6)

References (31)
  • 1
    • 0026534432 scopus 로고
    • The fidelity ofTaq
    • Barnes W. The fidelity ofTaq. Gene. 112:1992;29-35.
    • (1992) Gene , vol.112 , pp. 29-35
    • Barnes, W.1
  • 4
    • 0026419333 scopus 로고
    • Structure of Sindbis virus core protein reveals a chymotrypsin-like serine protease and the organization of the virion
    • Choi H.-K., Tong L., Minor W., Dumas P., Boege U., Rossmann M. G., Wengler G. Structure of Sindbis virus core protein reveals a chymotrypsin-like serine protease and the organization of the virion. Nature. 354:1991;37-43.
    • (1991) Nature , vol.354 , pp. 37-43
    • Choi, H.-K.1    Tong, L.2    Minor, W.3    Dumas, P.4    Boege, U.5    Rossmann, M.G.6    Wengler, G.7
  • 5
    • 0026536605 scopus 로고
    • Inhibition of enveloped RNA virus formation by peptides corresponding to glycoprotein sequences
    • Collier N. C., Adams S. P., Weingarten H., Schlesinger M. J. Inhibition of enveloped RNA virus formation by peptides corresponding to glycoprotein sequences. Antiviral Chem. Chemother. 3:1992;31-36.
    • (1992) Antiviral Chem. Chemother. , vol.3 , pp. 31-36
    • Collier, N.C.1    Adams, S.P.2    Weingarten, H.3    Schlesinger, M.J.4
  • 6
    • 0028819071 scopus 로고
    • Virion incorporation of envelope glycoproteins with long but not short cytoplasmic tails is blocked by specific, single amino acid substitutions in the human immunodeficiency virus Type 1 matrix
    • Freed E. O., Martin M. A. Virion incorporation of envelope glycoproteins with long but not short cytoplasmic tails is blocked by specific, single amino acid substitutions in the human immunodeficiency virus Type 1 matrix. J. Virol. 69:1995;1984-1989.
    • (1995) J. Virol. , vol.69 , pp. 1984-1989
    • Freed, E.O.1    Martin, M.A.2
  • 7
    • 0025913578 scopus 로고
    • Site-directed mutations in Sindbis virus E2 glycoprotein's cytoplasmic domain and the 6K protein lead to similar defects in virus assembly and budding
    • Gaedigk-Nitschko K., Schlesinger M. J. Site-directed mutations in Sindbis virus E2 glycoprotein's cytoplasmic domain and the 6K protein lead to similar defects in virus assembly and budding. Virology. 183:1991;206-214.
    • (1991) Virology , vol.183 , pp. 206-214
    • Gaedigk-Nitschko, K.1    Schlesinger, M.J.2
  • 8
    • 2542497232 scopus 로고
    • Location of the spike glycoproteins in the Semliki Forest virus membrane
    • Garoff H., Simons K. Location of the spike glycoproteins in the Semliki Forest virus membrane. Proc. Natl. Acad. Sci. USA. 71:1974;3988-3992.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 3988-3992
    • Garoff, H.1    Simons, K.2
  • 9
    • 0027419559 scopus 로고
    • Site-directed mutations in the Sindbis virus E2 glycoprotein identify palmitoylation sites and affect virus budding
    • Ivanova L., Schlesinger M. J. Site-directed mutations in the Sindbis virus E2 glycoprotein identify palmitoylation sites and affect virus budding. J. Virol. 67:1993;2546-2551.
    • (1993) J. Virol. , vol.67 , pp. 2546-2551
    • Ivanova, L.1    Schlesinger, M.J.2
  • 10
    • 0030952367 scopus 로고    scopus 로고
    • Functional analysis of the cytoplasmic tail of Moloney murine leukemia virus envelope protein
    • Januszeski M. M., Cannon P. M., Chen D., Rozenberg Y., Anderson W. F. Functional analysis of the cytoplasmic tail of Moloney murine leukemia virus envelope protein. J. Virol. 71:1997;3613-3619.
    • (1997) J. Virol. , vol.71 , pp. 3613-3619
    • Januszeski, M.M.1    Cannon, P.M.2    Chen, D.3    Rozenberg, Y.4    Anderson, W.F.5
  • 11
    • 0025766624 scopus 로고
    • The cytoplasmic domain of alphavirus E2 glycoprotein contains a short linear recognition signal sequence required for viral budding
    • Kail M., Hollinshead M., Ansorge W., Pepperkok R., Frank R., Griffiths G., Vaux D. The cytoplasmic domain of alphavirus E2 glycoprotein contains a short linear recognition signal sequence required for viral budding. EMBO J. 10:1991;2343-2351.
    • (1991) EMBO J. , vol.10 , pp. 2343-2351
    • Kail, M.1    Hollinshead, M.2    Ansorge, W.3    Pepperkok, R.4    Frank, R.5    Griffiths, G.6    Vaux, D.7
  • 12
    • 0027989589 scopus 로고
    • Mutations in an exposed domain of Sindbis virus capsid protein result in the production of noninfectious virions and morphological variants
    • Lee H., Brown D. T. Mutations in an exposed domain of Sindbis virus capsid protein result in the production of noninfectious virions and morphological variants. Virology. 202:1994;390-400.
    • (1994) Virology , vol.202 , pp. 390-400
    • Lee, H.1    Brown, D.T.2
  • 13
    • 0028094470 scopus 로고
    • The configuration of Sindbis virus envelope proteins is stabilized by the nucleocapsid protein
    • Lee H., Ricker P. D., Brown D. T. The configuration of Sindbis virus envelope proteins is stabilized by the nucleocapsid protein. Virology. 204:1994;471-474.
    • (1994) Virology , vol.204 , pp. 471-474
    • Lee, H.1    Ricker, P.D.2    Brown, D.T.3
  • 14
    • 0030585119 scopus 로고    scopus 로고
    • Identification of a protein binding site on the surface of the alphavirus nucleocapsid and its implication in virus assembly
    • Lee S., Owen K. E., Choi H.-K., Lee H., Lu G., Wengler G., Brown D. T., Rossmann M. G., Kuhn R. J. Identification of a protein binding site on the surface of the alphavirus nucleocapsid and its implication in virus assembly. Structure. 4:1996;531-541.
    • (1996) Structure , vol.4 , pp. 531-541
    • Lee, S.1    Owen, K.E.2    Choi, H.-K.3    Lee, H.4    Lu, G.5    Wengler, G.6    Brown, D.T.7    Rossmann, M.G.8    Kuhn, R.J.9
  • 15
    • 9044241680 scopus 로고    scopus 로고
    • Effect of E2 envelope glycoprotein cytoplasmic domain mutations on Sindbis virus pathogenesis
    • Levine B., Jiang H. H., Kleeman L., Yang G. Effect of E2 envelope glycoprotein cytoplasmic domain mutations on Sindbis virus pathogenesis. J. Virol. 70:1996;1255-1260.
    • (1996) J. Virol. , vol.70 , pp. 1255-1260
    • Levine, B.1    Jiang, H.H.2    Kleeman, L.3    Yang, G.4
  • 16
    • 0025912001 scopus 로고
    • In vitro mutagenesis of a full length cDNA clone of Semliki Forest virus: The small 6000 molecular-weight membrane protein modulates virus release
    • Liljeström P., Lusa S., Huylebroeck D., Garoff H. In vitro mutagenesis of a full length cDNA clone of Semliki Forest virus: The small 6000 molecular-weight membrane protein modulates virus release. J. Virol. 65:1991;4107-4113.
    • (1991) J. Virol. , vol.65 , pp. 4107-4113
    • Liljeström, P.1    Lusa, S.2    Huylebroeck, D.3    Garoff, H.4
  • 17
    • 0030219994 scopus 로고    scopus 로고
    • Mutations in the endo domain of Sindbis virus glycoprotein E2 block phosphorylation, reorientation of the endo domain, and nucleocapsid binding
    • Liu L. N., Lee H., Hernandez R., Brown D. T. Mutations in the endo domain of Sindbis virus glycoprotein E2 block phosphorylation, reorientation of the endo domain, and nucleocapsid binding. Virology. 222:1996;236-246.
    • (1996) Virology , vol.222 , pp. 236-246
    • Liu, L.N.1    Lee, H.2    Hernandez, R.3    Brown, D.T.4
  • 18
    • 0027976652 scopus 로고
    • Nucleocapsid-glycoprotein interactions required for assembly of alphaviruses
    • Lopez S., Yao J.-S., Kuhn R. J., Strauss E. G., Strauss J. H. Nucleocapsid-glycoprotein interactions required for assembly of alphaviruses. J. Virol. 68:1994;1316-1323.
    • (1994) J. Virol. , vol.68 , pp. 1316-1323
    • Lopez, S.1    Yao, J.-S.2    Kuhn, R.J.3    Strauss, E.G.4    Strauss, J.H.5
  • 19
    • 0025129428 scopus 로고
    • Oligomers of the cytoplasmic domain of the p62/E2 membrane protein of Semliki Forest virus bind to the nucleocapsid in vitro
    • Metsikkö K., Garoff H. Oligomers of the cytoplasmic domain of the p62/E2 membrane protein of Semliki Forest virus bind to the nucleocapsid in vitro. J. Virol. 64:1990;4678-4683.
    • (1990) J. Virol. , vol.64 , pp. 4678-4683
    • Metsikkö, K.1    Garoff, H.2
  • 20
    • 0030916277 scopus 로고    scopus 로고
    • Alpha virus budding is dependent on the interaction between the nucleocapsid and hydrophobic amino acids on the cytoplasmic domain of the E2 envelope glycoprotein
    • Owen K. E., Kuhn R. J. Alpha virus budding is dependent on the interaction between the nucleocapsid and hydrophobic amino acids on the cytoplasmic domain of the E2 envelope glycoprotein. Virology. 230:1997;187-196.
    • (1997) Virology , vol.230 , pp. 187-196
    • Owen, K.E.1    Kuhn, R.J.2
  • 22
    • 0023510284 scopus 로고
    • Production of infectious RNA transcripts from Sindbis virus cDNA clones: Mapping of lethal mutations, rescue of a temperature sensitive marker, and in vitro mutagenesis to generate defined mutants
    • Rice C. M., Levis R., Strauss J. H., Huang H. V. Production of infectious RNA transcripts from Sindbis virus cDNA clones: Mapping of lethal mutations, rescue of a temperature sensitive marker, and in vitro mutagenesis to generate defined mutants. J. Virol. 61:1987;3809-3819.
    • (1987) J. Virol. , vol.61 , pp. 3809-3819
    • Rice, C.M.1    Levis, R.2    Strauss, J.H.3    Huang, H.V.4
  • 24
    • 0000243165 scopus 로고    scopus 로고
    • Togaviridae: The viruses and their replication
    • New York: Lippincott-Raven. p. 523-540
    • Schlesinger S., Schlesinger M. J. Togaviridae: the viruses and their replication. Fundamental Virology. 1996;Lippincott-Raven, New York. p. 523-540.
    • (1996) Fundamental Virology
    • Schlesinger, S.1    Schlesinger, M.J.2
  • 25
    • 0030585135 scopus 로고    scopus 로고
    • Aromatic interactions define the binding of the alphavirus spike to its nucleocapsid
    • Sköging U., Vihinen M., Nilsson L., Liljeström P. Aromatic interactions define the binding of the alphavirus spike to its nucleocapsid. Structure. 4:1996;519-529.
    • (1996) Structure , vol.4 , pp. 519-529
    • Sköging, U.1    Vihinen, M.2    Nilsson, L.3    Liljeström, P.4
  • 26
    • 0031060529 scopus 로고    scopus 로고
    • Efficient multiplication of a Semliki Forest virus chimera containing Sindbis virus spikes
    • Smyth J., Soumalainen M., Garoff H. Efficient multiplication of a Semliki Forest virus chimera containing Sindbis virus spikes. J. Virol. 71:1997;818-823.
    • (1997) J. Virol. , vol.71 , pp. 818-823
    • Smyth, J.1    Soumalainen, M.2    Garoff, H.3
  • 27
    • 0028088152 scopus 로고
    • The alphaviruses: Gene expression, replication, and evolution
    • Strauss J. H., Strauss E. G. The alphaviruses: Gene expression, replication, and evolution. Microbiol. Rev. 58:1994;491-562.
    • (1994) Microbiol. Rev. , vol.58 , pp. 491-562
    • Strauss, J.H.1    Strauss, E.G.2
  • 29
    • 0026691322 scopus 로고
    • Spike protein-nucleocapsid interactions drive the budding of alphaviruses
    • Suomalainen M., Liljeström P., Garoff H. Spike protein-nucleocapsid interactions drive the budding of alphaviruses. J. Virol. 66:1992;4737-4747.
    • (1992) J. Virol. , vol.66 , pp. 4737-4747
    • Suomalainen, M.1    Liljeström, P.2    Garoff, H.3
  • 30
    • 0026490847 scopus 로고
    • Role of cell surface spikes in alphavirus budding
    • Zhao H., Garoff H. Role of cell surface spikes in alphavirus budding. J. Virol. 66:1992;7089-7095.
    • (1992) J. Virol. , vol.66 , pp. 7089-7095
    • Zhao, H.1    Garoff, H.2
  • 31
    • 0027965259 scopus 로고
    • A tyrosine-based motif in the cytoplasmic domain of the alphavirus envelope protein is essential for budding
    • Zhao H., Lindqvist B., Garoff H., von Bonnsdorf C., Liljeström P. A tyrosine-based motif in the cytoplasmic domain of the alphavirus envelope protein is essential for budding. EMBO J. 13:1994;4204-4211.
    • (1994) EMBO J. , vol.13 , pp. 4204-4211
    • Zhao, H.1    Lindqvist, B.2    Garoff, H.3    Von Bonnsdorf, C.4    Liljeström, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.