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Volumn 244, Issue 2, 1998, Pages 483-494

Roles in cell-to-cell fusion of two conserved hydrophobic regions in the murine coronavirus spike protein

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL CELL; ARTICLE; CELL FUSION; CELL MATURATION; CORONAVIRUS; GENETIC CONSERVATION; HYDROPHOBICITY; MEMBRANE FUSION; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; VIRUS TRANSMISSION;

EID: 0032503238     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1998.9121     Document Type: Article
Times cited : (81)

References (49)
  • 2
    • 0023032197 scopus 로고
    • Comparison of the spike precursor sequences of coronavirus IBV strains M41 and 6/82 with that of IBV Beaudette
    • Binns M. M., Boursnell M. E., Tomley F. M., Brown D. K. Comparison of the spike precursor sequences of coronavirus IBV strains M41 and 6/82 with that of IBV Beaudette. J. Gen. Virol. 67:1986;2825-2831.
    • (1986) J. Gen. Virol. , vol.67 , pp. 2825-2831
    • Binns, M.M.1    Boursnell, M.E.2    Tomley, F.M.3    Brown, D.K.4
  • 3
    • 0025070216 scopus 로고
    • Nucleotide sequence of the glycoprotein S gene of bovine enteric coronavirus and comparison with the S proteins of two mouse hepatitis virus strains
    • Boireau P., Cruciere C., Laporte J. Nucleotide sequence of the glycoprotein S gene of bovine enteric coronavirus and comparison with the S proteins of two mouse hepatitis virus strains. J. Gen. Virol. 71:1990;487-492.
    • (1990) J. Gen. Virol. , vol.71 , pp. 487-492
    • Boireau, P.1    Cruciere, C.2    Laporte, J.3
  • 4
    • 0029592197 scopus 로고
    • Mutational analysis of the murine coronavirus spike protein: Effect on cell-to-cell fusion
    • Bos E. C. W., Heunen L., Luytjes W., Spaan W. J. M. Mutational analysis of the murine coronavirus spike protein: effect on cell-to-cell fusion. Virology. 214:1995;453-463.
    • (1995) Virology , vol.214 , pp. 453-463
    • Bos, E.C.W.1    Heunen, L.2    Luytjes, W.3    Spaan, W.J.M.4
  • 5
    • 0026415343 scopus 로고
    • Coronavirus motif
    • Britton P. Coronavirus motif. Nature. 353:1991;394.
    • (1991) Nature , vol.353 , pp. 394
    • Britton, P.1
  • 6
    • 0026744238 scopus 로고
    • A leucine zipper structure present in the measles virus fusion protein is not required for its tetramerization but is essential for fusion
    • Buckland R., Malvoisin E., Beauverger P., Wild F. A leucine zipper structure present in the measles virus fusion protein is not required for its tetramerization but is essential for fusion. J. Gen. Virol. 73:1992;1703-1707.
    • (1992) J. Gen. Virol. , vol.73 , pp. 1703-1707
    • Buckland, R.1    Malvoisin, E.2    Beauverger, P.3    Wild, F.4
  • 7
    • 0021021580 scopus 로고
    • Coronavirus IBV: Structural characterization of the spike protein
    • Cavanagh D. Coronavirus IBV: Structural characterization of the spike protein. J. Gen. Virol. 64:1983;2577-2583.
    • (1983) J. Gen. Virol. , vol.64 , pp. 2577-2583
    • Cavanagh, D.1
  • 8
    • 0002437897 scopus 로고
    • The coronavirus surface glycoprotein
    • New York: Plenum. p. 73-113
    • Cavanagh D. The coronavirus surface glycoprotein. The Coronaviridae. 1995;Plenum, New York. p. 73-113.
    • (1995) The Coronaviridae
    • Cavanagh, D.1
  • 9
    • 17144470972 scopus 로고
    • Coronavirus IBV: Virus retaining spike glycopolypeptide S2 but not S1 is unable to induce virus-neutralizing or hemagglutination-inhibiting antibody, or induce chicken tracheal protection
    • Cavanagh D., Davis P. J., Darbyshire J. H., Peters R. W. Coronavirus IBV: Virus retaining spike glycopolypeptide S2 but not S1 is unable to induce virus-neutralizing or hemagglutination-inhibiting antibody, or induce chicken tracheal protection. J. Gen. Virol. 67:1986;1435-1442.
    • (1986) J. Gen. Virol. , vol.67 , pp. 1435-1442
    • Cavanagh, D.1    Davis, P.J.2    Darbyshire, J.H.3    Peters, R.W.4
  • 10
    • 0018700703 scopus 로고
    • Fluorographic detection of radioactivity in polyacrylamide gels with the water-soluble fluor, sodium salicylate
    • Chamberlain J. P. Fluorographic detection of radioactivity in polyacrylamide gels with the water-soluble fluor, sodium salicylate. Anal. Biochem. 98:1979;132-135.
    • (1979) Anal. Biochem. , vol.98 , pp. 132-135
    • Chamberlain, J.P.1
  • 11
    • 0025678671 scopus 로고
    • Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins
    • Chambers P., Pringle C. R., Easton A. J. Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins. J. Gen. Virol. 71:1990;3075-3080.
    • (1990) J. Gen. Virol. , vol.71 , pp. 3075-3080
    • Chambers, P.1    Pringle, C.R.2    Easton, A.J.3
  • 12
    • 0028328606 scopus 로고
    • Genomic organization of a virulent Taiwanese strain of transmissible gastroenteritis virus
    • Chen C. M., Pocock D. H., Britton P. Genomic organization of a virulent Taiwanese strain of transmissible gastroenteritis virus. Adv. Exp. Med. Biol. 342:1993;23-28.
    • (1993) Adv. Exp. Med. Biol. , vol.342 , pp. 23-28
    • Chen, C.M.1    Pocock, D.H.2    Britton, P.3
  • 13
    • 0001248650 scopus 로고
    • Alpha helical coiled coils - A widespread motif in proteins
    • Cohen C., Parry D. A. Alpha helical coiled coils - A widespread motif in proteins. Trends Biochem. Sci. 11:1986;245-248.
    • (1986) Trends Biochem. Sci. , vol.11 , pp. 245-248
    • Cohen, C.1    Parry, D.A.2
  • 14
    • 0020040263 scopus 로고
    • Monoclonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell-cell fusion
    • Collins A. R., Knobler R. L., Powell H., Buchmeier M. J. Monoclonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell-cell fusion. Virology. 119:1982;358-371.
    • (1982) Virology , vol.119 , pp. 358-371
    • Collins, A.R.1    Knobler, R.L.2    Powell, H.3    Buchmeier, M.J.4
  • 16
    • 0023430389 scopus 로고
    • CDNA cloning and sequence analysis of the gene encoding the peplomer protein of feline infectious peritonitis virus
    • de Groot R. J., Maduro J., Lenstra J. A., Horzinek M. C., van der Zeijst B. A., Spaan W. J. cDNA cloning and sequence analysis of the gene encoding the peplomer protein of feline infectious peritonitis virus. J. Gen. Virol. 68:1987b;2639-2646.
    • (1987) J. Gen. Virol. , vol.68 , pp. 2639-2646
    • De Groot, R.J.1    Maduro, J.2    Lenstra, J.A.3    Horzinek, M.C.4    Van Der Zeijst, B.A.5    Spaan, W.J.6
  • 17
    • 0024411768 scopus 로고
    • Stably expressed FIPV peplomer protein induces cell fusion and elicits neutralizing antibodies in mice
    • de Groot R. J., Van Leen R. W., Dalderup M. J., Vennema H., Horzinek M. C., Spaan W. J. Stably expressed FIPV peplomer protein induces cell fusion and elicits neutralizing antibodies in mice. Virology. 171:1989;493-502.
    • (1989) Virology , vol.171 , pp. 493-502
    • De Groot, R.J.1    Van Leen, R.W.2    Dalderup, M.J.3    Vennema, H.4    Horzinek, M.C.5    Spaan, W.J.6
  • 18
    • 0027911552 scopus 로고
    • Peptide engineering: Catalytic molten globules
    • DeGrado W. F. Peptide engineering: Catalytic molten globules. Nature. 365:1993;488-489.
    • (1993) Nature , vol.365 , pp. 488-489
    • Degrado, W.F.1
  • 19
    • 0029968695 scopus 로고    scopus 로고
    • Mutational analysis of the fusion peptide of the human immunodeficiency virus type 1: Identification of critical glycine residues
    • Delahunty M. D., Rhee I., Freed E. O., Bonifacino J. S. Mutational analysis of the fusion peptide of the human immunodeficiency virus type 1: Identification of critical glycine residues. Virology. 218:1996;94-102.
    • (1996) Virology , vol.218 , pp. 94-102
    • Delahunty, M.D.1    Rhee, I.2    Freed, E.O.3    Bonifacino, J.S.4
  • 20
    • 0025217893 scopus 로고
    • The actions of melittin on membranes
    • Dempsey C. E. The actions of melittin on membranes. Biochim. Biophys. Acta. 1031:1990;143-161.
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 143-161
    • Dempsey, C.E.1
  • 21
    • 0027157736 scopus 로고
    • Folding and assembly of viral membrane proteins
    • Doms R. W., Lamb R. A., Rose J. K., Helenius A. Folding and assembly of viral membrane proteins. Virology. 193:1993;545-562.
    • (1993) Virology , vol.193 , pp. 545-562
    • Doms, R.W.1    Lamb, R.A.2    Rose, J.K.3    Helenius, A.4
  • 22
    • 0026652457 scopus 로고
    • Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity
    • Dubay J. W., Roberts S. J., Brody B., Hunter E. Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity. J. Virol. 66:1992;4748-4756.
    • (1992) J. Virol. , vol.66 , pp. 4748-4756
    • Dubay, J.W.1    Roberts, S.J.2    Brody, B.3    Hunter, E.4
  • 23
    • 0022399775 scopus 로고
    • Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Host-dependent differences in proteolytic cleavage and cell fusion
    • Frana M. F., Behnke J. N., Sturman L. S., Holmes K. V. Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Host-dependent differences in proteolytic cleavage and cell fusion. J. Virol. 56:1985;912-920.
    • (1985) J. Virol. , vol.56 , pp. 912-920
    • Frana, M.F.1    Behnke, J.N.2    Sturman, L.S.3    Holmes, K.V.4
  • 24
    • 0000233999 scopus 로고
    • Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase
    • Fuerst T. R., Niles E. G., Studier F. W., Moss B. Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase. Proc. Natl. Acad. Sci. USA. 83:1986;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
  • 25
    • 0029948532 scopus 로고    scopus 로고
    • Murine coronavirus membrane fusion is blocked by modification of thiols buried within the spike protein
    • Gallagher T. M. Murine coronavirus membrane fusion is blocked by modification of thiols buried within the spike protein. J. Virol. 70:1996;4683-4690.
    • (1996) J. Virol. , vol.70 , pp. 4683-4690
    • Gallagher, T.M.1
  • 26
    • 0024564217 scopus 로고
    • Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the "fusion peptide"
    • Harter C., James P., Bachi T., Semenza G., Brunner J. Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the "fusion peptide" J. Biol. Chem. 264:1989;6459-6464.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6459-6464
    • Harter, C.1    James, P.2    Bachi, T.3    Semenza, G.4    Brunner, J.5
  • 27
    • 0026605537 scopus 로고
    • CLUSTAL V: Improved software for multiple sequence alignment
    • Higgins D. G., Bleasby A. J., Fuchs R. CLUSTAL V: Improved software for multiple sequence alignment. Comput. Appl. Biosci. 8:1992;189-191.
    • (1992) Comput. Appl. Biosci. , vol.8 , pp. 189-191
    • Higgins, D.G.1    Bleasby, A.J.2    Fuchs, R.3
  • 29
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld R., Kornfeld S. Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 54:1985;631-664.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 30
    • 0028018126 scopus 로고
    • Localization of neutralizing epitopes and the receptor-binding site within the amino-terminal 330 amino acids of the murine coronavirus spike protein
    • Kubo H., Yamada Y. K., Taguchi F. Localization of neutralizing epitopes and the receptor-binding site within the amino-terminal 330 amino acids of the murine coronavirus spike protein. J. Virol. 68:1994;5403-5410.
    • (1994) J. Virol. , vol.68 , pp. 5403-5410
    • Kubo, H.1    Yamada, Y.K.2    Taguchi, F.3
  • 31
    • 0028840940 scopus 로고
    • Structure and topology of the influenza virus fusion peptide in lipid bilayers
    • Luneberg J., Martin I., Nussler F., Ruysschaert J. M., Herrmann A. Structure and topology of the influenza virus fusion peptide in lipid bilayers. J. Biol. Chem. 270:1995;27606-27614.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27606-27614
    • Luneberg, J.1    Martin, I.2    Nussler, F.3    Ruysschaert, J.M.4    Herrmann, A.5
  • 32
    • 0031015207 scopus 로고    scopus 로고
    • Characterization of two temperature-sensitive mutants of coronavirus mouse hepatitis virus strain A59 with maturation defects in the spike protein
    • Luytjes W., Gerritsma H., Bos E., Spaan W. Characterization of two temperature-sensitive mutants of coronavirus mouse hepatitis virus strain A59 with maturation defects in the spike protein. J. Virol. 71:1997;949-955.
    • (1997) J. Virol. , vol.71 , pp. 949-955
    • Luytjes, W.1    Gerritsma, H.2    Bos, E.3    Spaan, W.4
  • 33
  • 34
    • 0026563680 scopus 로고
    • Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum
    • Marquardt T., Helenius A. Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum. J. Cell Biol. 117:1992;505-513.
    • (1992) J. Cell Biol. , vol.117 , pp. 505-513
    • Marquardt, T.1    Helenius, A.2
  • 35
    • 0028293970 scopus 로고
    • Membrane interaction and conformational properties of the putative fusion peptide of PH-30, a protein active in sperm-egg fusion
    • Muga A., Neugebauer W., Hirama T., Surewicz W. K. Membrane interaction and conformational properties of the putative fusion peptide of PH-30, a protein active in sperm-egg fusion. Biochemistry. 33:1994;4444-4448.
    • (1994) Biochemistry , vol.33 , pp. 4444-4448
    • Muga, A.1    Neugebauer, W.2    Hirama, T.3    Surewicz, W.K.4
  • 36
    • 0028218423 scopus 로고
    • Interaction of the HIV-1 fusion peptide with phospholipid vesicles: Different structural requirements for fusion and leakage
    • Nieva J. L., Nir S., Muga A., Goni F. M., Wilschut J. Interaction of the HIV-1 fusion peptide with phospholipid vesicles: Different structural requirements for fusion and leakage. Biochemistry. 33:1994;3201-3209.
    • (1994) Biochemistry , vol.33 , pp. 3201-3209
    • Nieva, J.L.1    Nir, S.2    Muga, A.3    Goni, F.M.4    Wilschut, J.5
  • 37
    • 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., Broder C. C., Berger E. A. Fusogenic mechanisms of enveloped-virus glycoproteins analyzed by a novel recombinant vaccinia virus-based assay quantitating cell fusion-dependent reporter gene activation. J. Virol. 68:1994;5411-5422.
    • (1994) J. Virol. , vol.68 , pp. 5411-5422
    • Nussbaum, O.1    Broder, C.C.2    Berger, E.A.3
  • 41
    • 0028116668 scopus 로고
    • Muta-tions in the fusion peptide and heptad repeat regions of the Newcastle disease virus fusion protein block fusion
    • Sergel-Germano T., McQuain C., Morrison T. Muta-tions in the fusion peptide and heptad repeat regions of the Newcastle disease virus fusion protein block fusion. J. Virol. 68:1994;7654-7658.
    • (1994) J. Virol. , vol.68 , pp. 7654-7658
    • Sergel-Germano, T.1    McQuain, C.2    Morrison, T.3
  • 43
    • 0024226792 scopus 로고
    • Coronaviruses: Structure and genome expression
    • Spaan W., Cavanagh D., Horzinek M. C. Coronaviruses: Structure and genome expression. J. Gen. Virol. 69:1988;2939-2952.
    • (1988) J. Gen. Virol. , vol.69 , pp. 2939-2952
    • Spaan, W.1    Cavanagh, D.2    Horzinek, M.C.3
  • 44
    • 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 90K cleavage fragments
    • Sturman L. S., Ricard C. S., Holmes K. V. Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Activation of cell-fusing activity of virions by trypsin and separation of two different 90K cleavage fragments. J. Virol. 56:1985;904-911.
    • (1985) J. Virol. , vol.56 , pp. 904-911
    • Sturman, L.S.1    Ricard, C.S.2    Holmes, K.V.3
  • 45
    • 0028818244 scopus 로고
    • The S2 subunit of the murine coronavirus spike protein is not involved in receptor binding
    • Taguchi F. The S2 subunit of the murine coronavirus spike protein is not involved in receptor binding. J. Virol. 69:1995;7260-7263.
    • (1995) J. Virol. , vol.69 , pp. 7260-7263
    • Taguchi, F.1
  • 46
    • 0025169833 scopus 로고
    • Intracellular transport of recombinant coronavirus spike proteins: Implications for virus assembly
    • Vennema H., Heijnen L., Zijderveld A., Horzinek M. C., Spaan W. J. Intracellular transport of recombinant coronavirus spike proteins: implications for virus assembly. J. Virol. 64:1990;339-346.
    • (1990) J. Virol. , vol.64 , pp. 339-346
    • Vennema, H.1    Heijnen, L.2    Zijderveld, A.3    Horzinek, M.C.4    Spaan, W.J.5
  • 47
    • 0025276435 scopus 로고
    • Viral and cellular membrane fusion proteins
    • White J. M. Viral and cellular membrane fusion proteins. Annu. Rev. Physiol. 52:1990;675-697.
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 675-697
    • White, J.M.1
  • 48
    • 0026492542 scopus 로고
    • Membrane fusion
    • White J. M. Membrane fusion. Science. 258:1992;917-924.
    • (1992) Science , vol.258 , pp. 917-924
    • White, J.M.1
  • 49
    • 0027967960 scopus 로고
    • Insertion of a coiled-coil peptide from influenza virus hemagglutinin into membranes
    • Yu Y. G., King D. S., Shin Y. K. Insertion of a coiled-coil peptide from influenza virus hemagglutinin into membranes. Science. 266:1994;274-276.
    • (1994) Science , vol.266 , pp. 274-276
    • Yu, Y.G.1    King, D.S.2    Shin, Y.K.3


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