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Volumn 334, Issue 2, 2005, Pages 306-318

Spike protein assembly into the coronavirion: Exploring the limits of its sequence requirements

Author keywords

Coronavirus; Cytoplasmic domain; S protein

Indexed keywords

CORONAVIRUS SPIKE VIRUS; MEMBRANE PROTEIN; UNCLASSIFIED DRUG; VIRUS GLYCOPROTEIN; VIRUS PROTEIN;

EID: 15144362170     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virol.2005.02.001     Document Type: Article
Times cited : (42)

References (68)
  • 1
    • 0034715352 scopus 로고    scopus 로고
    • Assembly of Sendai virus: M protein interacts with F and HN proteins and with the cytoplasmic tail and transmembrane domain of F protein
    • A. Ali, and D.P. Nayak Assembly of Sendai virus: M protein interacts with F and HN proteins and with the cytoplasmic tail and transmembrane domain of F protein Virology 276 2 2000 289 303
    • (2000) Virology , vol.276 , Issue.2 , pp. 289-303
    • Ali, A.1    Nayak, D.P.2
  • 2
    • 0029592197 scopus 로고
    • Mutational analysis of the murine coronavirus spike protein: Effect on cell-to-cell fusion
    • E.C. Bos, L. Heijnen, W. Luytjes, and W.J. Spaan Mutational analysis of the murine coronavirus spike protein: effect on cell-to-cell fusion Virology 214 2 1995 453 463
    • (1995) Virology , vol.214 , Issue.2 , pp. 453-463
    • Bos, E.C.1    Heijnen, L.2    Luytjes, W.3    Spaan, W.J.4
  • 3
    • 0031907095 scopus 로고    scopus 로고
    • Measles viruses with altered envelope protein cytoplasmic tails gain cell fusion competence
    • T. Cathomen, H.Y. Naim, and R. Cattaneo Measles viruses with altered envelope protein cytoplasmic tails gain cell fusion competence J. Virol. 72 2 1998 1224 1234
    • (1998) J. Virol. , vol.72 , Issue.2 , pp. 1224-1234
    • Cathomen, T.1    Naim, H.Y.2    Cattaneo, R.3
  • 4
    • 0002437897 scopus 로고
    • The coronavirus surface glycoprotein
    • S.G. Siddell Plenum Press New York
    • D. Cavanagh The coronavirus surface glycoprotein S.G. Siddell The coronaviridae 1995 Plenum Press New York
    • (1995) The Coronaviridae
    • Cavanagh, D.1
  • 5
    • 0034732109 scopus 로고    scopus 로고
    • Coronavirus-induced membrane fusion requires the cysteine-rich domain in the spike protein
    • K.W. Chang, Y. Sheng, and J.L. Gombold Coronavirus-induced membrane fusion requires the cysteine-rich domain in the spike protein Virology 269 1 2000 212 224
    • (2000) Virology , vol.269 , Issue.1 , pp. 212-224
    • Chang, K.W.1    Sheng, Y.2    Gombold, J.L.3
  • 6
    • 0033998035 scopus 로고    scopus 로고
    • Infectious bronchitis virus e protein is targeted to the Golgi complex and directs release of virus-like particles
    • E. Corse, and C.E. Machamer Infectious bronchitis virus E protein is targeted to the Golgi complex and directs release of virus-like particles J. Virol. 74 9 2000 4319 4326
    • (2000) J. Virol. , vol.74 , Issue.9 , pp. 4319-4326
    • Corse, E.1    MacHamer, C.E.2
  • 7
    • 0032874344 scopus 로고    scopus 로고
    • Mapping of the coronavirus membrane protein domains involved in interaction with the spike protein
    • C.A. de Haan, M. Smeets, F. Vernooij, H. Vennema, and P.J. Rottier Mapping of the coronavirus membrane protein domains involved in interaction with the spike protein J. Virol. 73 9 1999 7441 7452
    • (1999) J. Virol. , vol.73 , Issue.9 , pp. 7441-7452
    • De Haan, C.A.1    Smeets, M.2    Vernooij, F.3    Vennema, H.4    Rottier, P.J.5
  • 8
    • 0034067478 scopus 로고    scopus 로고
    • Assembly of the coronavirus envelope: Homotypic interactions between the M proteins
    • C.A. de Haan, H. Vennema, and P.J. Rottier Assembly of the coronavirus envelope: homotypic interactions between the M proteins J. Virol. 74 11 2000 4967 4978
    • (2000) J. Virol. , vol.74 , Issue.11 , pp. 4967-4978
    • De Haan, C.A.1    Vennema, H.2    Rottier, P.J.3
  • 9
    • 0036343241 scopus 로고    scopus 로고
    • The group-specific murine coronavirus genes are not essential, but their deletion, by reverse genetics, is attenuating in the natural host
    • C.A. de Haan, P.S. Masters, X. Shen, S. Weiss, and P.J. Rottier The group-specific murine coronavirus genes are not essential, but their deletion, by reverse genetics, is attenuating in the natural host Virology 296 1 2002 177 189
    • (2002) Virology , vol.296 , Issue.1 , pp. 177-189
    • De Haan, C.A.1    Masters, P.S.2    Shen, X.3    Weiss, S.4    Rottier, P.J.5
  • 10
    • 0142124183 scopus 로고    scopus 로고
    • Coronaviruses as vectors: Position dependence of foreign gene expression
    • C.A. de Haan, L. van Genne, J.N. Stoop, H. Volders, and P.J. Rottier Coronaviruses as vectors: position dependence of foreign gene expression J. Virol. 77 21 2003 11312 11323
    • (2003) J. Virol. , vol.77 , Issue.21 , pp. 11312-11323
    • De Haan, C.A.1    Van Genne, L.2    Stoop, J.N.3    Volders, H.4    Rottier, P.J.5
  • 11
    • 0025103827 scopus 로고
    • Assembly of coronavirus spike protein into trimers and its role in epitope expression
    • B. Delmas, and H. Laude Assembly of coronavirus spike protein into trimers and its role in epitope expression J. Virol. 64 11 1990 5367 5375
    • (1990) J. Virol. , vol.64 , Issue.11 , pp. 5367-5375
    • Delmas, B.1    Laude, H.2
  • 12
    • 0019934717 scopus 로고
    • The helical hydrophobic moment: A measure of the amphiphilicity of a helix
    • D. Eisenberg, R.M. Weiss, and T.C. Terwilliger The helical hydrophobic moment: a measure of the amphiphilicity of a helix Nature 299 5881 1982 371 374
    • (1982) Nature , vol.299 , Issue.5881 , pp. 371-374
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger, T.C.3
  • 13
    • 0025155473 scopus 로고
    • Cytoplasmic expression system based on constitutive synthesis of bacteriophage T7 RNA polymerase in mammalian cells
    • O. Elroy-Stein, and B. Moss Cytoplasmic expression system based on constitutive synthesis of bacteriophage T7 RNA polymerase in mammalian cells Proc. Natl. Acad. Sci. U.S.A. 87 17 1990 6743 6747
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , Issue.17 , pp. 6743-6747
    • Elroy-Stein, O.1    Moss, B.2
  • 14
    • 0034630855 scopus 로고    scopus 로고
    • Structure-function analysis of the Sendai virus F and HN cytoplasmic domain: Different role for the two proteins in the production of virus particle
    • N. Fouillot-Coriou, and L. Roux Structure-function analysis of the Sendai virus F and HN cytoplasmic domain: different role for the two proteins in the production of virus particle Virology 270 2 2000 464 475
    • (2000) Virology , vol.270 , Issue.2 , pp. 464-475
    • Fouillot-Coriou, N.1    Roux, L.2
  • 15
    • 0021795178 scopus 로고
    • A single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein
    • C.J. Gallione, and J.K. Rose A single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein J. Virol. 54 2 1985 374 382
    • (1985) J. Virol. , vol.54 , Issue.2 , pp. 374-382
    • Gallione, C.J.1    Rose, J.K.2
  • 16
    • 0021459206 scopus 로고
    • Intracellular appearance of a glycoprotein in VSV-infected BHK cells lacking the membrane-anchoring oligopeptide of the viral G-protein
    • C. Garreis-Wabnitz, and J. Kruppa Intracellular appearance of a glycoprotein in VSV-infected BHK cells lacking the membrane-anchoring oligopeptide of the viral G-protein EMBO J. 3 7 1984 1469 1476
    • (1984) EMBO J. , vol.3 , Issue.7 , pp. 1469-1476
    • Garreis-Wabnitz, C.1    Kruppa, J.2
  • 17
    • 0033960161 scopus 로고    scopus 로고
    • Assembly of spikes into coronavirus particles is mediated by the carboxy-terminal domain of the spike protein
    • G.J. Godeke, C.A. de Haan, J.W. Rossen, H. Vennema, and P.J. Rottier Assembly of spikes into coronavirus particles is mediated by the carboxy-terminal domain of the spike protein J. Virol. 74 3 2000 1566 1571
    • (2000) J. Virol. , vol.74 , Issue.3 , pp. 1566-1571
    • Godeke, G.J.1    De Haan, C.A.2    Rossen, J.W.3    Vennema, H.4    Rottier, P.J.5
  • 18
    • 0033960161 scopus 로고    scopus 로고
    • Assembly of spikes into coronavirus particles is mediated by the carboxy-terminal domain of the spike protein
    • G.J. Godeke, C.A. de Haan, J.W. Rossen, H. Vennema, and P.J. Rottier Assembly of spikes into coronavirus particles is mediated by the carboxy-terminal domain of the spike protein J. Virol. 74 3 2000 1566 1571
    • (2000) J. Virol. , vol.74 , Issue.3 , pp. 1566-1571
    • Godeke, G.J.1    De Haan, C.A.2    Rossen, J.W.3    Vennema, H.4    Rottier, P.J.5
  • 19
    • 0022635965 scopus 로고
    • The soluble glycoprotein of vesicular stomatitis virus is formed during or shortly after the translation process
    • L. Graeve, C. Garreis-Wabnitz, M. Zauke, M. Breindl, and J. Kruppa The soluble glycoprotein of vesicular stomatitis virus is formed during or shortly after the translation process J. Virol. 57 3 1986 968 975
    • (1986) J. Virol. , vol.57 , Issue.3 , pp. 968-975
    • Graeve, L.1    Garreis-Wabnitz, C.2    Zauke, M.3    Breindl, M.4    Kruppa, J.5
  • 20
    • 0037384422 scopus 로고    scopus 로고
    • Switching species tropism: An effective way to manipulate the feline coronavirus genome
    • B.J. Haijema, H. Volders, and P.J. Rottier Switching species tropism: an effective way to manipulate the feline coronavirus genome J. Virol. 77 8 2003 4528 4538
    • (2003) J. Virol. , vol.77 , Issue.8 , pp. 4528-4538
    • Haijema, B.J.1    Volders, H.2    Rottier, P.J.3
  • 21
    • 0033927571 scopus 로고    scopus 로고
    • Characterization of an essential RNA secondary structure in the 3′ untranslated region of the murine coronavirus genome
    • B. Hsue, T. Hartshorne, and P.S. Masters Characterization of an essential RNA secondary structure in the 3′ untranslated region of the murine coronavirus genome J. Virol. 74 15 2000 6911 6921
    • (2000) J. Virol. , vol.74 , Issue.15 , pp. 6911-6921
    • Hsue, B.1    Hartshorne, T.2    Masters, P.S.3
  • 22
    • 0028102718 scopus 로고
    • The influenza virus hemagglutinin cytoplasmic tail is not essential for virus assembly or infectivity
    • H. Jin, G.P. Leser, and R.A. Lamb The influenza virus hemagglutinin cytoplasmic tail is not essential for virus assembly or infectivity EMBO J. 13 22 1994 5504 5515
    • (1994) EMBO J. , vol.13 , Issue.22 , pp. 5504-5515
    • Jin, H.1    Leser, G.P.2    Lamb, R.A.3
  • 23
    • 0030991137 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape
    • H. Jin, G.P. Leser, J. Zhang, and R.A. Lamb Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape EMBO J. 16 6 1997 1236 1247
    • (1997) EMBO J. , vol.16 , Issue.6 , pp. 1236-1247
    • Jin, H.1    Leser, G.P.2    Zhang, J.3    Lamb, R.A.4
  • 24
    • 0028133370 scopus 로고
    • Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding
    • J. Klumperman, J.K. Locker, A. Meijer, M.C. Horzinek, H.J. Geuze, and P.J. Rottier Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding J. Virol. 68 10 1994 6523 6534
    • (1994) J. Virol. , vol.68 , Issue.10 , pp. 6523-6534
    • Klumperman, J.1    Locker, J.K.2    Meijer, A.3    Horzinek, M.C.4    Geuze, H.J.5    Rottier, P.J.6
  • 25
    • 0028069572 scopus 로고
    • Characterization of the budding compartment of mouse hepatitis virus: Evidence that transport from the RER to the Golgi complex requires only one vesicular transport step
    • J. Krijnse-Locker, M. Ericsson, P.J. Rottier, and G. Griffiths Characterization of the budding compartment of mouse hepatitis virus: evidence that transport from the RER to the Golgi complex requires only one vesicular transport step J. Cell Biol. 124 1-2 1994 55 70
    • (1994) J. Cell Biol. , vol.124 , Issue.1-2 , pp. 55-70
    • Krijnse-Locker, J.1    Ericsson, M.2    Rottier, P.J.3    Griffiths, G.4
  • 26
    • 0033982337 scopus 로고    scopus 로고
    • Retargeting of coronavirus by substitution of the spike glycoprotein ectodomain: Crossing the host cell species barrier
    • L. Kuo, G.J. Godeke, M.J. Raamsman, P.S. Masters, and P.J. Rottier Retargeting of coronavirus by substitution of the spike glycoprotein ectodomain: crossing the host cell species barrier J. Virol. 74 3 2000 1393 1406
    • (2000) J. Virol. , vol.74 , Issue.3 , pp. 1393-1406
    • Kuo, L.1    Godeke, G.J.2    Raamsman, M.J.3    Masters, P.S.4    Rottier, P.J.5
  • 27
    • 0036232932 scopus 로고    scopus 로고
    • Genetic evidence for a structural interaction between the carboxy termini of the membrane and nucleocapsid proteins of mouse hepatitis virus
    • L. Kuo, and P.S. Masters Genetic evidence for a structural interaction between the carboxy termini of the membrane and nucleocapsid proteins of mouse hepatitis virus J. Virol. 76 10 2002 4987 4999
    • (2002) J. Virol. , vol.76 , Issue.10 , pp. 4987-4999
    • Kuo, L.1    Masters, P.S.2
  • 28
    • 0028914568 scopus 로고
    • Oligomerization of a trans-Golgi/trans-Golgi network retained protein occurs in the Golgi complex and may be part of its retention
    • J.K. Locker, D.J. Opstelten, M. Ericsson, M.C. Horzinek, and P.J. Rottier Oligomerization of a trans-Golgi/trans-Golgi network retained protein occurs in the Golgi complex and may be part of its retention J. Biol. Chem. 270 15 1995 8815 8821
    • (1995) J. Biol. Chem. , vol.270 , Issue.15 , pp. 8815-8821
    • Locker, J.K.1    Opstelten, D.J.2    Ericsson, M.3    Horzinek, M.C.4    Rottier, P.J.5
  • 29
    • 0023476246 scopus 로고
    • Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site
    • W. Luytjes, L.S. Sturman, P.J. Bredenbeek, J. Charite, B.A. van der Zeijst, M.C. Horzinek, and W.J. Spaan Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site Virology 161 2 1987 479 487
    • (1987) Virology , vol.161 , Issue.2 , pp. 479-487
    • Luytjes, W.1    Sturman, L.S.2    Bredenbeek, P.J.3    Charite, J.4    Van Der Zeijst, B.A.5    Horzinek, M.C.6    Spaan, W.J.7
  • 30
    • 0023807529 scopus 로고
    • Membrane integration and intracellular transport of the coronavirus glycoprotein E1, a class III membrane glycoprotein
    • T. Mayer, T. Tamura, M. Falk, and H. Niemann Membrane integration and intracellular transport of the coronavirus glycoprotein E1, a class III membrane glycoprotein J. Biol. Chem. 263 29 1988 14956 14963
    • (1988) J. Biol. Chem. , vol.263 , Issue.29 , pp. 14956-14963
    • Mayer, T.1    Tamura, T.2    Falk, M.3    Niemann, H.4
  • 31
    • 0029912922 scopus 로고    scopus 로고
    • Budding of rabies virus particles in the absence of the spike glycoprotein
    • T. Mebatsion, M. Konig, and K.K. Conzelmann Budding of rabies virus particles in the absence of the spike glycoprotein Cell 84 6 1996 941 951
    • (1996) Cell , vol.84 , Issue.6 , pp. 941-951
    • Mebatsion, T.1    Konig, M.2    Conzelmann, K.K.3
  • 32
    • 0030069140 scopus 로고    scopus 로고
    • The cytoplasmic tail of influenza a virus neuraminidase (NA) affects NA incorporation into virions, virion morphology, and virulence in mice but is not essential for virus replication
    • L.J. Mitnaul, M.R. Castrucci, K.G. Murti, and Y. Kawaoka The cytoplasmic tail of influenza A virus neuraminidase (NA) affects NA incorporation into virions, virion morphology, and virulence in mice but is not essential for virus replication J. Virol. 70 2 1996 873 879
    • (1996) J. Virol. , vol.70 , Issue.2 , pp. 873-879
    • Mitnaul, L.J.1    Castrucci, M.R.2    Murti, K.G.3    Kawaoka, Y.4
  • 33
    • 0025053668 scopus 로고
    • Fatty acids on the A/Japan/305/57 influenza virus hemagglutinin have a role in membrane fusion
    • C.W. Naeve, and D. Williams Fatty acids on the A/Japan/305/57 influenza virus hemagglutinin have a role in membrane fusion EMBO J. 9 12 1990 3857 3866
    • (1990) EMBO J. , vol.9 , Issue.12 , pp. 3857-3866
    • Naeve, C.W.1    Williams, D.2
  • 34
    • 0026447375 scopus 로고
    • Effects of altering palmitoylation sites on biosynthesis and function of the influenza virus hemagglutinin
    • H.Y. Naim, B. Amarneh, N.T. Ktistakis, and M.G. Roth Effects of altering palmitoylation sites on biosynthesis and function of the influenza virus hemagglutinin J. Virol. 66 12 1992 7585 7588
    • (1992) J. Virol. , vol.66 , Issue.12 , pp. 7585-7588
    • Naim, H.Y.1    Amarneh, B.2    Ktistakis, N.T.3    Roth, M.G.4
  • 35
    • 0034854123 scopus 로고    scopus 로고
    • Cooperation of an RNA packaging signal and a viral envelope protein in coronavirus RNA packaging
    • K. Narayanan, and S. Makino Cooperation of an RNA packaging signal and a viral envelope protein in coronavirus RNA packaging J. Virol. 75 19 2001 9059 9067
    • (2001) J. Virol. , vol.75 , Issue.19 , pp. 9059-9067
    • Narayanan, K.1    Makino, S.2
  • 36
    • 0030782149 scopus 로고    scopus 로고
    • Protein interactions during coronavirus assembly
    • V.P. Nguyen, and B.G. Hogue Protein interactions during coronavirus assembly J. Virol. 71 12 1997 9278 9284
    • (1997) J. Virol. , vol.71 , Issue.12 , pp. 9278-9284
    • Nguyen, V.P.1    Hogue, B.G.2
  • 37
    • 0019833716 scopus 로고
    • Coronavirus glycoprotein E1, a new type of viral glycoprotein
    • H. Niemann, and H.D. Klenk Coronavirus glycoprotein E1, a new type of viral glycoprotein J. Mol. Biol. 153 4 1981 993 1010
    • (1981) J. Mol. Biol. , vol.153 , Issue.4 , pp. 993-1010
    • Niemann, H.1    Klenk, H.D.2
  • 39
    • 0027446386 scopus 로고
    • Cytoplasmic domain requirement for incorporation of a foreign envelope protein into vesicular stomatitis virus
    • R.J. Owens, and J.K. Rose Cytoplasmic domain requirement for incorporation of a foreign envelope protein into vesicular stomatitis virus J. Virol. 67 1 1993 360 365
    • (1993) J. Virol. , vol.67 , Issue.1 , pp. 360-365
    • Owens, R.J.1    Rose, J.K.2
  • 40
    • 0020398151 scopus 로고
    • Expression from cloned cDNA of cell-surface secreted forms of the glycoprotein of vesicular stomatitis virus in eukaryotic cells
    • J.K. Rose, and J.E. Bergmann Expression from cloned cDNA of cell-surface secreted forms of the glycoprotein of vesicular stomatitis virus in eukaryotic cells Cell 30 3 1982 753 762
    • (1982) Cell , vol.30 , Issue.3 , pp. 753-762
    • Rose, J.K.1    Bergmann, J.E.2
  • 41
    • 0002753706 scopus 로고
    • The coronavirus membrane glycoprotein
    • S.G. Siddell Plenum Press New York
    • P.J.M. Rottier The coronavirus membrane glycoprotein S.G. Siddell The coronaviridae 1995 Plenum Press New York
    • (1995) The Coronaviridae
    • Rottier, P.J.M.1
  • 42
    • 0002753706 scopus 로고
    • The coronavirus membrane protein
    • S.G. Siddell Plenum Press New York
    • P.J.M. Rottier The coronavirus membrane protein S.G. Siddell The coronaviridae 1995 Plenum Press New York
    • (1995) The Coronaviridae
    • Rottier, P.J.M.1
  • 43
    • 0019850652 scopus 로고
    • Viral protein synthesis in mouse hepatitis virus strain A59-infected cells: Effect of tunicamycin
    • P.J. Rottier, M.C. Horzinek, and B.A. van der Zeijst Viral protein synthesis in mouse hepatitis virus strain A59-infected cells: effect of tunicamycin J. Virol. 40 2 1981 350 357
    • (1981) J. Virol. , vol.40 , Issue.2 , pp. 350-357
    • Rottier, P.J.1    Horzinek, M.C.2    Van Der Zeijst, B.A.3
  • 44
    • 0036229532 scopus 로고    scopus 로고
    • Fatty acids on the A/USSR/77 influenza virus hemagglutinin facilitate the transition from hemifusion to fusion pore formation
    • T. Sakai, R. Ohuchi, and M. Ohuchi Fatty acids on the A/USSR/77 influenza virus hemagglutinin facilitate the transition from hemifusion to fusion pore formation J. Virol. 76 9 2002 4603 4611
    • (2002) J. Virol. , vol.76 , Issue.9 , pp. 4603-4611
    • Sakai, T.1    Ohuchi, R.2    Ohuchi, M.3
  • 45
    • 0028147383 scopus 로고
    • Sendai virus M protein binds independently to either the F or the HN glycoprotein in vivo
    • C.M. Sanderson, H.H. Wu, and D.P. Nayak Sendai virus M protein binds independently to either the F or the HN glycoprotein in vivo J. Virol. 68 1 1994 69 76
    • (1994) J. Virol. , vol.68 , Issue.1 , pp. 69-76
    • Sanderson, C.M.1    Wu, H.H.2    Nayak, D.P.3
  • 46
    • 0020077726 scopus 로고
    • Acylation of viral spike glycoproteins: A feature of enveloped RNA viruses
    • M.F. Schmidt Acylation of viral spike glycoproteins: a feature of enveloped RNA viruses Virology 116 1 1982 327 338
    • (1982) Virology , vol.116 , Issue.1 , pp. 327-338
    • Schmidt, M.F.1
  • 47
    • 0032843716 scopus 로고    scopus 로고
    • Involvement of the cytoplasmic domain of the hemagglutinin-neuraminidase protein in assembly of the paramyxovirus simian virus 5
    • A.P. Schmitt, B. He, and R.A. Lamb Involvement of the cytoplasmic domain of the hemagglutinin-neuraminidase protein in assembly of the paramyxovirus simian virus 5 J. Virol. 73 10 1999 8703 8712
    • (1999) J. Virol. , vol.73 , Issue.10 , pp. 8703-8712
    • Schmitt, A.P.1    He, B.2    Lamb, R.A.3
  • 48
    • 0036194519 scopus 로고    scopus 로고
    • Requirements for budding of paramyxovirus simian virus 5 virus-like particles
    • A.P. Schmitt, G.P. Leser, D.L. Waning, and R.A. Lamb Requirements for budding of paramyxovirus simian virus 5 virus-like particles J. Virol. 76 8 2002 3952 3964
    • (2002) J. Virol. , vol.76 , Issue.8 , pp. 3952-3964
    • Schmitt, A.P.1    Leser, G.P.2    Waning, D.L.3    Lamb, R.A.4
  • 49
    • 0032473424 scopus 로고    scopus 로고
    • Requirement for a non-specific glycoprotein cytoplasmic domain sequence to drive efficient budding of vesicular stomatitis virus
    • M.J. Schnell, L. Buonocore, E. Boritz, H.P. Ghosh, R. Chernish, and J.K. Rose Requirement for a non-specific glycoprotein cytoplasmic domain sequence to drive efficient budding of vesicular stomatitis virus EMBO J. 17 5 1998 1289 1296
    • (1998) EMBO J. , vol.17 , Issue.5 , pp. 1289-1296
    • Schnell, M.J.1    Buonocore, L.2    Boritz, E.3    Ghosh, H.P.4    Chernish, R.5    Rose, J.K.6
  • 50
    • 0025882934 scopus 로고
    • Deacylation of the hemagglutinin of influenza A/Aichi/2/68 has no effect on membrane fusion properties
    • D.A. Steinhauer, S.A. Wharton, D.C. Wiley, and J.J. Skehel Deacylation of the hemagglutinin of influenza A/Aichi/2/68 has no effect on membrane fusion properties Virology 184 1 1991 445 448
    • (1991) Virology , vol.184 , Issue.1 , pp. 445-448
    • Steinhauer, D.A.1    Wharton, S.A.2    Wiley, D.C.3    Skehel, J.J.4
  • 51
    • 0022397327 scopus 로고
    • Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Activation of cell-fusing activity of virions by trypsin and separation of two different 90 K cleavage fragments
    • L.S. Sturman, C.S. Ricard, and K.V. Holmes Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: activation of cell-fusing activity of virions by trypsin and separation of two different 90 K cleavage fragments J. Virol. 56 3 1985 904 911
    • (1985) J. Virol. , vol.56 , Issue.3 , pp. 904-911
    • Sturman, L.S.1    Ricard, C.S.2    Holmes, K.V.3
  • 52
    • 0026691322 scopus 로고
    • Spike protein-nucleocapsid interactions drive the budding of alphaviruses
    • M. Suomalainen, P. Liljestrom, and H. Garoff Spike protein-nucleocapsid interactions drive the budding of alphaviruses J. Virol. 66 8 1992 4737 4747
    • (1992) J. Virol. , vol.66 , Issue.8 , pp. 4737-4747
    • Suomalainen, M.1    Liljestrom, P.2    Garoff, H.3
  • 53
    • 0029918145 scopus 로고    scopus 로고
    • Analysis of the receptor-binding site of murine coronavirus spike protein
    • H. Suzuki, and F. Taguchi Analysis of the receptor-binding site of murine coronavirus spike protein J. Virol. 70 4 1996 2632 2636
    • (1996) J. Virol. , vol.70 , Issue.4 , pp. 2632-2636
    • Suzuki, H.1    Taguchi, F.2
  • 54
    • 0031775220 scopus 로고    scopus 로고
    • Cytoplasmic domain of Sendai virus HN protein contains a specific sequence required for its incorporation into virions
    • T. Takimoto, T. Bousse, E.C. Coronel, R.A. Scroggs, and A. Portner Cytoplasmic domain of Sendai virus HN protein contains a specific sequence required for its incorporation into virions J. Virol. 72 12 1998 9747 9754
    • (1998) J. Virol. , vol.72 , Issue.12 , pp. 9747-9754
    • Takimoto, T.1    Bousse, T.2    Coronel, E.C.3    Scroggs, R.A.4    Portner, A.5
  • 55
    • 0021322863 scopus 로고
    • Replication of coronavirus MHV-A59 in sac-cells: Determination of the first site of budding of progeny virions
    • J. Tooze, S. Tooze, and G. Warren Replication of coronavirus MHV-A59 in sac-cells: determination of the first site of budding of progeny virions Eur. J. Cell Biol. 33 2 1984 281 293
    • (1984) Eur. J. Cell Biol. , vol.33 , Issue.2 , pp. 281-293
    • Tooze, J.1    Tooze, S.2    Warren, G.3
  • 56
    • 0023916548 scopus 로고
    • Site of addition of N-acetyl-galactosamine to the E1 glycoprotein of mouse hepatitis virus-A59
    • S.A. Tooze, J. Tooze, and G. Warren Site of addition of N-acetyl-galactosamine to the E1 glycoprotein of mouse hepatitis virus-A59 J. Cell Biol. 106 5 1988 1475 1487
    • (1988) J. Cell Biol. , vol.106 , Issue.5 , pp. 1475-1487
    • Tooze, S.A.1    Tooze, J.2    Warren, G.3
  • 57
    • 0023193669 scopus 로고
    • Fatty acid acylation of viral proteins in murine hepatitis virus-infected cells. Brief report
    • M.F. van Berlo, W.J. van den Brink, M.C. Horzinek, and B.A. van der Zeijst Fatty acid acylation of viral proteins in murine hepatitis virus-infected cells. Brief report Arch. Virol. 95 1-2 1987 123 128
    • (1987) Arch. Virol. , vol.95 , Issue.1-2 , pp. 123-128
    • Van Berlo, M.F.1    Van Den Brink, W.J.2    Horzinek, M.C.3    Van Der Zeijst, B.A.4
  • 58
    • 0025169833 scopus 로고
    • Intracellular transport of recombinant coronavirus spike proteins: Implications for virus assembly
    • H. Vennema, L. Heijnen, A. Zijderveld, M.C. Horzinek, and W.J. Spaan Intracellular transport of recombinant coronavirus spike proteins: implications for virus assembly J. Virol. 64 1 1990 339 346
    • (1990) J. Virol. , vol.64 , Issue.1 , pp. 339-346
    • Vennema, H.1    Heijnen, L.2    Zijderveld, A.3    Horzinek, M.C.4    Spaan, W.J.5
  • 59
    • 0025790535 scopus 로고
    • Enhancement of the vaccinia virus/phage T7 RNA polymerase expression system using encephalomyocarditis virus 5′-untranslated region sequences
    • H. Vennema, R. Rijnbrand, L. Heijnen, M.C. Horzinek, and W.J. Spaan Enhancement of the vaccinia virus/phage T7 RNA polymerase expression system using encephalomyocarditis virus 5′-untranslated region sequences Gene 108 2 1991 201 209
    • (1991) Gene , vol.108 , Issue.2 , pp. 201-209
    • Vennema, H.1    Rijnbrand, R.2    Heijnen, L.3    Horzinek, M.C.4    Spaan, W.J.5
  • 60
    • 0029933250 scopus 로고    scopus 로고
    • Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes
    • H. Vennema, G.J. Godeke, J.W. Rossen, W.F. Voorhout, M.C. Horzinek, D.J. Opstelten, and P.J. Rottier Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes EMBO J. 15 8 1996 2020 2028
    • (1996) EMBO J. , vol.15 , Issue.8 , pp. 2020-2028
    • Vennema, H.1    Godeke, G.J.2    Rossen, J.W.3    Voorhout, W.F.4    Horzinek, M.C.5    Opstelten, D.J.6    Rottier, P.J.7
  • 61
    • 0036720806 scopus 로고    scopus 로고
    • Roles for the cytoplasmic tails of the fusion and hemagglutinin- neuraminidase proteins in budding of the paramyxovirus simian virus 5
    • D.L. Waning, A.P. Schmitt, G.P. Leser, and R.A. Lamb Roles for the cytoplasmic tails of the fusion and hemagglutinin-neuraminidase proteins in budding of the paramyxovirus simian virus 5 J. Virol. 76 18 2002 9284 9297
    • (2002) J. Virol. , vol.76 , Issue.18 , pp. 9284-9297
    • Waning, D.L.1    Schmitt, A.P.2    Leser, G.P.3    Lamb, R.A.4
  • 62
    • 0025375789 scopus 로고
    • Monoclonal antibodies to the peplomer glycoprotein of coronavirus mouse hepatitis virus identify two subunits and detect a conformational change in the subunit released under mild alkaline conditions
    • D.G. Weismiller, L.S. Sturman, M.J. Buchmeier, J.O. Fleming, and K.V. Holmes Monoclonal antibodies to the peplomer glycoprotein of coronavirus mouse hepatitis virus identify two subunits and detect a conformational change in the subunit released under mild alkaline conditions J. Virol. 64 6 1990 3051 3055
    • (1990) J. Virol. , vol.64 , Issue.6 , pp. 3051-3055
    • Weismiller, D.G.1    Sturman, L.S.2    Buchmeier, M.J.3    Fleming, J.O.4    Holmes, K.V.5
  • 63
    • 0026326156 scopus 로고
    • Fatty acid acylation is not required for membrane fusion activity or glycoprotein assembly into VSV virions
    • M.A. Whitt, and J.K. Rose Fatty acid acylation is not required for membrane fusion activity or glycoprotein assembly into VSV virions Virology 185 2 1991 875 878
    • (1991) Virology , vol.185 , Issue.2 , pp. 875-878
    • Whitt, M.A.1    Rose, J.K.2
  • 64
    • 0026741425 scopus 로고
    • Retained in vitro infectivity and cytopathogenicity of HIV-1 despite truncation of the C-terminal tail of the env gene product
    • T. Wilk, T. Pfeiffer, and V. Bosch Retained in vitro infectivity and cytopathogenicity of HIV-1 despite truncation of the C-terminal tail of the env gene product Virology 189 1 1992 167 177
    • (1992) Virology , vol.189 , Issue.1 , pp. 167-177
    • Wilk, T.1    Pfeiffer, T.2    Bosch, V.3
  • 65
    • 0030198535 scopus 로고    scopus 로고
    • Palmitoylation of the murine leukemia virus envelope glycoprotein transmembrane subunits
    • C. Yang, and R.W. Compans Palmitoylation of the murine leukemia virus envelope glycoprotein transmembrane subunits Virology 221 1 1996 87 97
    • (1996) Virology , vol.221 , Issue.1 , pp. 87-97
    • Yang, C.1    Compans, R.W.2
  • 66
    • 0025961121 scopus 로고
    • The S2 subunit of the spike glycoprotein of bovine coronavirus mediates membrane fusion in insect cells
    • D.W. Yoo, M.D. Parker, and L.A. Babiuk The S2 subunit of the spike glycoprotein of bovine coronavirus mediates membrane fusion in insect cells Virology 180 1 1991 395 399
    • (1991) Virology , vol.180 , Issue.1 , pp. 395-399
    • Yoo, D.W.1    Parker, M.D.2    Babiuk, L.A.3
  • 67
    • 0034630492 scopus 로고    scopus 로고
    • The cytoplasmic tails of the influenza virus spike glycoproteins are required for normal genome packaging
    • J. Zhang, G.P. Leser, A. Pekosz, and R.A. Lamb The cytoplasmic tails of the influenza virus spike glycoproteins are required for normal genome packaging Virology 269 2 2000 325 334
    • (2000) Virology , vol.269 , Issue.2 , pp. 325-334
    • Zhang, J.1    Leser, G.P.2    Pekosz, A.3    Lamb, R.A.4
  • 68
    • 0027965259 scopus 로고
    • A tyrosine-based motif in the cytoplasmic domain of the alphavirus envelope protein is essential for budding
    • H. Zhao, B. Lindqvist, H. Garoff, C.H. von Bonsdorff, and P. Liljestrom A tyrosine-based motif in the cytoplasmic domain of the alphavirus envelope protein is essential for budding EMBO J. 13 18 1994 4204 4211
    • (1994) EMBO J. , vol.13 , Issue.18 , pp. 4204-4211
    • Zhao, H.1    Lindqvist, B.2    Garoff, H.3    Von Bonsdorff, C.H.4    Liljestrom, P.5


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