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Volumn 79, Issue 9, 2005, Pages 5326-5336

RhoA signaling is required for respiratory syncytial virus-induced syncytium formation and filamentous virion morphology

Author keywords

[No Author keywords available]

Indexed keywords

4 (1 AMINOETHYL) N (4 PYRIDYL)CYCLOHEXANECARBOXAMIDE; ADENOSINE DIPHOSPHATE RIBOSE; EXOENZYME C3; GUANOSINE TRIPHOSPHATASE; RHO KINASE INHIBITOR; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; VIRUS PROTEIN;

EID: 17444422895     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.79.9.5326-5336.2005     Document Type: Article
Times cited : (98)

References (53)
  • 1
    • 0029987340 scopus 로고    scopus 로고
    • Bound simian virus 40 translocates to caveolin-enriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae
    • Anderson, H. A., Y. Chen, and L. C. Norkin. 1996. Bound simian virus 40 translocates to caveolin-enriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae. Mol. Biol. Cell 7:1825-1834.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1825-1834
    • Anderson, H.A.1    Chen, Y.2    Norkin, L.C.3
  • 2
    • 0023812317 scopus 로고
    • Direct observation of the budding and fusion of an enveloped virus by video microscopy of viable cells
    • Bachi, T. 1988. Direct observation of the budding and fusion of an enveloped virus by video microscopy of viable cells. J. Cell Biol. 107:1689-1695.
    • (1988) J. Cell Biol. , vol.107 , pp. 1689-1695
    • Bachi, T.1
  • 3
    • 0015898875 scopus 로고
    • Morphogenesis and ultrastructure of respiratory syncytial virus
    • Bachi, T., and C. Howe. 1973. Morphogenesis and ultrastructure of respiratory syncytial virus. J. Virol. 12:1173-1180.
    • (1973) J. Virol. , vol.12 , pp. 1173-1180
    • Bachi, T.1    Howe, C.2
  • 4
    • 0027435087 scopus 로고
    • Integrins as receptors for virus attachment and cell entry
    • Bergelson, J. M., and R. W. Finberg. 1993. Integrins as receptors for virus attachment and cell entry. Trends Microbiol. 1:287-288.
    • (1993) Trends Microbiol. , vol.1 , pp. 287-288
    • Bergelson, J.M.1    Finberg, R.W.2
  • 5
    • 0036327980 scopus 로고    scopus 로고
    • Respiratory syncytial virus assembly occurs in GM1-rich regions of the host-cell membrane and alters the cellular distribution of tyrosine- phosphorylated caveolin-1
    • Brown, G., H. W. Rixon, and R. J. Sugrue. 2002. Respiratory syncytial virus assembly occurs in GM1-rich regions of the host-cell membrane and alters the cellular distribution of tyrosine-phosphorylated caveolin-1. J. Gen. Virol. 83:1841-1850.
    • (2002) J. Gen. Virol. , vol.83 , pp. 1841-1850
    • Brown, G.1    Rixon, H.W.2    Sugrue, R.J.3
  • 6
    • 0032488234 scopus 로고    scopus 로고
    • Role of cellular actin in the gene expression and morphogenesis of human respiratory syncytial virus
    • Burke, E., L. Dupuy, C. Wall, and S. Barik. 1998. Role of cellular actin in the gene expression and morphogenesis of human respiratory syncytial virus. Virology 252:137-148.
    • (1998) Virology , vol.252 , pp. 137-148
    • Burke, E.1    Dupuy, L.2    Wall, C.3    Barik, S.4
  • 7
    • 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
  • 8
    • 0033540271 scopus 로고    scopus 로고
    • Extracellular simian virus 40 transmits a signal that promotes virus enclosure within caveolae
    • Chen, Y., and L. C. Norkin. 1999. Extracellular simian virus 40 transmits a signal that promotes virus enclosure within caveolae. Exp. Cell Res. 246:83-90.
    • (1999) Exp. Cell Res. , vol.246 , pp. 83-90
    • Chen, Y.1    Norkin, L.C.2
  • 9
    • 0026321755 scopus 로고
    • Post-translational processing oligomerization of the fusion protein of human respiratory syncytial virus
    • Collins, P. L., and G. Mottet. 1991. Post-translational processing oligomerization of the fusion protein of human respiratory syncytial virus. J. Gen. Virol. 72:3095-3101.
    • (1991) J. Gen. Virol. , vol.72 , pp. 3095-3101
    • Collins, P.L.1    Mottet, G.2
  • 10
    • 0023427610 scopus 로고
    • Effects of cytochalasin and phalloidin on actin
    • Cooper, J. A. 1987. Effects of cytochalasin and phalloidin on actin. J. Cell Biol. 105:1473-1478.
    • (1987) J. Cell Biol. , vol.105 , pp. 1473-1478
    • Cooper, J.A.1
  • 11
    • 0018851959 scopus 로고
    • An immunofluorescence study of influenza virus filament formation
    • Cox, J. C., A. W. Hampson, and R. C. Hamilton. 1980. An immunofluorescence study of influenza virus filament formation. Arch. Virol. 63:275-284.
    • (1980) Arch. Virol. , vol.63 , pp. 275-284
    • Cox, J.C.1    Hampson, A.W.2    Hamilton, R.C.3
  • 12
    • 0030957356 scopus 로고    scopus 로고
    • Viral manipulations of the actin cytoskeleton
    • Cudmore, S., I. Reckmann, and M. Way. 1997. Viral manipulations of the actin cytoskeleton. Trends Microbiol. 5:142-148.
    • (1997) Trends Microbiol. , vol.5 , pp. 142-148
    • Cudmore, S.1    Reckmann, I.2    Way, M.3
  • 13
    • 0018608197 scopus 로고
    • Ebola and Marburg viruses. I. Some ultrastructural differences between strains when grown in Vero cells
    • Ellis, D. S., S. Stamford, G. Lloyd, E. T. Bowen, G. S. Platt, H. Way, and D. I. Simpson. 1979. Ebola and Marburg viruses. I. Some ultrastructural differences between strains when grown in Vero cells. J. Med. Virol. 4:201-211.
    • (1979) J. Med. Virol. , vol.4 , pp. 201-211
    • Ellis, D.S.1    Stamford, S.2    Lloyd, G.3    Bowen, E.T.4    Platt, G.S.5    Way, H.6    Simpson, D.I.7
  • 14
    • 0023603605 scopus 로고
    • Sequence similarities between human immunodeficiency virus gp41 and paramyxovirus fusion proteins
    • Gonzalez-Scarano, F., M. N. Waxham, A. M. Ross, and J. A. Hoxie. 1987. Sequence similarities between human immunodeficiency virus gp41 and paramyxovirus fusion proteins. AIDS Res. Hum. Retrovir. 3:245-252.
    • (1987) AIDS Res. Hum. Retrovir. , vol.3 , pp. 245-252
    • Gonzalez-Scarano, F.1    Waxham, M.N.2    Ross, A.M.3    Hoxie, J.A.4
  • 15
    • 0025974686 scopus 로고
    • rab5 controls early endosome fusion in vitro
    • Gorvel, J. P., P. Chavrier, M. Zerial, and J. Gruenberg. 1991. rab5 controls early endosome fusion in vitro. Cell 64:915-925.
    • (1991) Cell , vol.64 , pp. 915-925
    • Gorvel, J.P.1    Chavrier, P.2    Zerial, M.3    Gruenberg, J.4
  • 16
    • 0035837054 scopus 로고    scopus 로고
    • RhoA is activated during respiratory syncytial virus infection
    • Gower, T. L., M. E. Peeples, P. L. Collins, and B. S. Graham. 2001. RhoA is activated during respiratory syncytial virus infection. Virology 283:188-196.
    • (2001) Virology , vol.283 , pp. 188-196
    • Gower, T.L.1    Peeples, M.E.2    Collins, P.L.3    Graham, B.S.4
  • 18
    • 0032559362 scopus 로고    scopus 로고
    • G proteins and small GTPases: Distant relatives keep in touch
    • Hall, A. 1998. G proteins and small GTPases: distant relatives keep in touch. Science 279:509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 19
    • 0034608222 scopus 로고    scopus 로고
    • Iduronic acid-containing glycosaminoglycans on target cells are required for efficient respiratory syncytial virus infection
    • Hallak, L. K., P. L. Collins, W. Knudson, and M. E. Peeples. 2000. Iduronic acid-containing glycosaminoglycans on target cells are required for efficient respiratory syncytial virus infection. Virology 271:264-275.
    • (2000) Virology , vol.271 , pp. 264-275
    • Hallak, L.K.1    Collins, P.L.2    Knudson, W.3    Peeples, M.E.4
  • 21
    • 0033622332 scopus 로고    scopus 로고
    • Integrins alpha2beta1 and alpha4beta1 can mediate SA11 rotavirus attachment and entry into cells
    • Hewish, M. J., Y. Takada, and B. S. Coulson. 2000. Integrins alpha2beta1 and alpha4beta1 can mediate SA11 rotavirus attachment and entry into cells. J. Virol. 74:228-236.
    • (2000) J. Virol. , vol.74 , pp. 228-236
    • Hewish, M.J.1    Takada, Y.2    Coulson, B.S.3
  • 23
    • 0029939555 scopus 로고    scopus 로고
    • Adenovirus interaction with distinct integrins mediates separate events in cell entry and gene delivery to hematopoietic cells
    • Huang, S., T. Kamata, Y. Takada, Z. M. Ruggeri, and G. R. Nemerow. 1996. Adenovirus interaction with distinct integrins mediates separate events in cell entry and gene delivery to hematopoietic cells. J. Virol. 70:4502-4508.
    • (1996) J. Virol. , vol.70 , pp. 4502-4508
    • Huang, S.1    Kamata, T.2    Takada, Y.3    Ruggeri, Z.M.4    Nemerow, G.R.5
  • 24
    • 0032529672 scopus 로고    scopus 로고
    • A core trimer of the paramyxovirus fusion protein: Parallels to influenza virus hemagglutinin and HIV-1 gp41
    • Joshi, S. B., R. E. Dutch, and R. A. Lamb. 1998. A core trimer of the paramyxovirus fusion protein: parallels to influenza virus hemagglutinin and HIV-1 gp41. Virology 248:20-34.
    • (1998) Virology , vol.248 , pp. 20-34
    • Joshi, S.B.1    Dutch, R.E.2    Lamb, R.A.3
  • 25
    • 0015834450 scopus 로고
    • Electron microscopic studies of respiratory syncytial temperature-sensitive mutants
    • Kalica, A. R., P. F. Wright, F. M. Hetrick, and R. M. Chanock. 1973. Electron microscopic studies of respiratory syncytial temperature-sensitive mutants. Arch. Gesamte Virusforsch. 41:248-258.
    • (1973) Arch. Gesamte Virusforsch. , vol.41 , pp. 248-258
    • Kalica, A.R.1    Wright, P.F.2    Hetrick, F.M.3    Chanock, R.M.4
  • 26
    • 0029913350 scopus 로고    scopus 로고
    • Complementation of M gene mutants of vesicular stomatitis virus by plasmid-derived M protein converts spherical extracellular particles into native bullet shapes
    • Lyles, D. S., M. O. McKenzie, P. E. Kaptur, K. W. Grant, and W. G. Jerome. 1996. Complementation of M gene mutants of vesicular stomatitis virus by plasmid-derived M protein converts spherical extracellular particles into native bullet shapes. Virology 217:76-87.
    • (1996) Virology , vol.217 , pp. 76-87
    • Lyles, D.S.1    McKenzie, M.O.2    Kaptur, P.E.3    Grant, K.W.4    Jerome, W.G.5
  • 27
    • 0037302372 scopus 로고    scopus 로고
    • Role of plasma membrane lipid microdomains in respiratory syncytial virus filament formation
    • McCurdy, L. H., and B. S. Graham. 2003. Role of plasma membrane lipid microdomains in respiratory syncytial virus filament formation. J. Virol. 77:1747-1756.
    • (2003) J. Virol. , vol.77 , pp. 1747-1756
    • McCurdy, L.H.1    Graham, B.S.2
  • 28
    • 0029912922 scopus 로고    scopus 로고
    • Budding of rabies virus particles in the absence of the spike glycoprotein
    • Mebatsion, T., M. Konig, and K. K. Conzelmann. 1996. Budding of rabies virus particles in the absence of the spike glycoprotein. Cell 84:941-951.
    • (1996) Cell , vol.84 , pp. 941-951
    • Mebatsion, T.1    Konig, M.2    Conzelmann, K.K.3
  • 29
    • 0033597894 scopus 로고    scopus 로고
    • Polarized distribution of endogenous Rac1 and RhoA at the cell surface
    • Michaely, P. A., C. Mineo, Y. S. Ying, and R. G. Anderson. 1999. Polarized distribution of endogenous Rac1 and RhoA at the cell surface. J. Biol. Chem. 274:21430-21436.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21430-21436
    • Michaely, P.A.1    Mineo, C.2    Ying, Y.S.3    Anderson, R.G.4
  • 30
    • 0029791373 scopus 로고    scopus 로고
    • The small GTPase Rho: Cellular functions and signal transduction
    • Narumiya, S. 1996. The small GTPase Rho: cellular functions and signal transduction. J. Biochem. 120:215-228.
    • (1996) J. Biochem. , vol.120 , pp. 215-228
    • Narumiya, S.1
  • 31
    • 0029156668 scopus 로고
    • CD44 exhibits a cell type dependent interaction with Triton X-100 insoluble, lipid rich, plasma membrane domains
    • Neame, S. J., C. R. Uff, H. Sheikh, S. C. Wheatley, and C. M. Isacke. 1995. CD44 exhibits a cell type dependent interaction with Triton X-100 insoluble, lipid rich, plasma membrane domains. J. Cell Sci. 108:3127-3135.
    • (1995) J. Cell Sci. , vol.108 , pp. 3127-3135
    • Neame, S.J.1    Uff, C.R.2    Sheikh, H.3    Wheatley, S.C.4    Isacke, C.M.5
  • 32
    • 0034015604 scopus 로고    scopus 로고
    • Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts
    • Nguyen, D. H., and J. E. Hildreth. 2000. Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts. J. Virol. 74:3264-3272.
    • (2000) J. Virol. , vol.74 , pp. 3264-3272
    • Nguyen, D.H.1    Hildreth, J.E.2
  • 33
    • 0037333988 scopus 로고    scopus 로고
    • Infectivity of a human respiratory syncytial virus lacking the SH, G, and F proteins is efficiently mediated by the vesicular stomatitis virus G protein
    • Oomens, A. G. P., A. G. Megaw, and G. W. Wertz. 2003. Infectivity of a human respiratory syncytial virus lacking the SH, G, and F proteins is efficiently mediated by the vesicular stomatitis virus G protein. J. Virol. 77:3785-3798.
    • (2003) J. Virol. , vol.77 , pp. 3785-3798
    • Oomens, A.G.P.1    Megaw, A.G.2    Wertz, G.W.3
  • 34
    • 0032567361 scopus 로고    scopus 로고
    • Phosphorylation of moesin by Rho-associated kinase (Rho-kinase) plays a crucial role in the formation of microvilli-like structures
    • Oshiro, N., Y. Fukata, and K. Kaibuchi. 1998. Phosphorylation of moesin by Rho-associated kinase (Rho-kinase) plays a crucial role in the formation of microvilli-like structures. J. Biol. Chem. 273:34663-34666.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34663-34666
    • Oshiro, N.1    Fukata, Y.2    Kaibuchi, K.3
  • 35
    • 0018701944 scopus 로고
    • Pneumoviruses: The cell surface of lytically and persistently infected cells
    • Parry, J. E., P. V. Shirodaria, and C. R. Pringle. 1979. Pneumoviruses: the cell surface of lytically and persistently infected cells. J. Gen. Virol. 44:479-491.
    • (1979) J. Gen. Virol. , vol.44 , pp. 479-491
    • Parry, J.E.1    Shirodaria, P.V.2    Pringle, C.R.3
  • 36
    • 0030747154 scopus 로고    scopus 로고
    • Analysis of bovine respiratory syncytial virus envelope glycoproteins in cell fusion
    • Pastey, M. K., and S. K. Samal. 1997. Analysis of bovine respiratory syncytial virus envelope glycoproteins in cell fusion. J. Gen. Virol. 78:1885-1889.
    • (1997) J. Gen. Virol. , vol.78 , pp. 1885-1889
    • Pastey, M.K.1    Samal, S.K.2
  • 37
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A. J., and A. Hall. 1992. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70:389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 38
    • 0032484479 scopus 로고    scopus 로고
    • The M1 and M2 proteins of influenza a virus are important determinants in filamentous particle formation
    • Roberts, P. C., R. A. Lamb, and R. W. Compans. 1998. The M1 and M2 proteins of influenza A virus are important determinants in filamentous particle formation. Virology 240:127-137.
    • (1998) Virology , vol.240 , pp. 127-137
    • Roberts, P.C.1    Lamb, R.A.2    Compans, R.W.3
  • 39
  • 40
    • 0031045966 scopus 로고    scopus 로고
    • Analysis of the cellular functions of the small GTP-binding protein rho p21 with Clostridium botulinum C3 exoenzyme
    • Saito, Y. 1997. Analysis of the cellular functions of the small GTP-binding protein rho p21 with Clostridium botulinum C3 exoenzyme. Nippon Yakurigaku Zasshi 109:13-17.
    • (1997) Nippon Yakurigaku Zasshi , vol.109 , pp. 13-17
    • Saito, Y.1
  • 41
    • 0023460714 scopus 로고
    • The role of the target membrane structure in fusion with Sendai virus
    • Sarkar, D. P., and R. Blumenthal. 1988. The role of the target membrane structure in fusion with Sendai virus. Membrane Biochem. 7:231-247.
    • (1988) Membrane Biochem. , vol.7 , pp. 231-247
    • Sarkar, D.P.1    Blumenthal, R.2
  • 42
    • 0036194519 scopus 로고    scopus 로고
    • Requirements for budding of paramyxovirus simian virus 5 virus-like particles
    • Schmitt, A. P., G. P. Leser, D. L. Waning, and R. A. Lamb. 2002. Requirements for budding of paramyxovirus simian virus 5 virus-like particles. J. Virol. 76:3952-3964.
    • (2002) J. Virol. , vol.76 , pp. 3952-3964
    • Schmitt, A.P.1    Leser, G.P.2    Waning, D.L.3    Lamb, R.A.4
  • 43
    • 0024353843 scopus 로고
    • Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase
    • Sekine, A., M. Fijuwara, and S. Narumiya. 1989. Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase. J. Biol. Chem. 264:8602-8605.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8602-8605
    • Sekine, A.1    Fijuwara, M.2    Narumiya, S.3
  • 44
    • 0031907484 scopus 로고    scopus 로고
    • RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/ actin protrusions in fibroblasts
    • Shaw, R. J., M. Henry, F. Solomon, and T. Jacks. 1998. RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/ actin protrusions in fibroblasts. Mol. Biol. Cell 9:403-419.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 403-419
    • Shaw, R.J.1    Henry, M.2    Solomon, F.3    Jacks, T.4
  • 45
    • 0028168008 scopus 로고
    • A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles
    • Sogaard, M., K. Tani, R. R. Ye, S. Geromanos, P. Tempst, T. Kirchhausen, J. E. Rothman, and T. Sollner. 1994. A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles. Cell 78:937-948.
    • (1994) Cell , vol.78 , pp. 937-948
    • Sogaard, M.1    Tani, K.2    Ye, R.R.3    Geromanos, S.4    Tempst, P.5    Kirchhausen, T.6    Rothman, J.E.7    Sollner, T.8
  • 46
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • Sollner, T., M. K. Bennett, S. W. Whiteheart, R. H. Scheller, and J. E. Rothman. 1993. A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 75:409-418.
    • (1993) Cell , vol.75 , pp. 409-418
    • Sollner, T.1    Bennett, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 50
    • 0031744016 scopus 로고    scopus 로고
    • Novel entry pathway of bovine herpes virus 1 and 5
    • Wild, P., E. M. Schraner, J. Peter, E. Loepfe, and M. Engels. 1998. Novel entry pathway of bovine herpes virus 1 and 5. J. Virol. 72:9561-9566.
    • (1998) J. Virol. , vol.72 , pp. 9561-9566
    • Wild, P.1    Schraner, E.M.2    Peter, J.3    Loepfe, E.4    Engels, M.5
  • 51
    • 0034093648 scopus 로고    scopus 로고
    • Filamentous particle formation by human parainfluenza virus type 2
    • Yao, Q., and R. W. Compans. 2000. Filamentous particle formation by human parainfluenza virus type 2. J. Gen. Virol. 81:1305-1312.
    • (2000) J. Gen. Virol. , vol.81 , pp. 1305-1312
    • Yao, Q.1    Compans, R.W.2
  • 52
    • 0033995067 scopus 로고    scopus 로고
    • Influenza virus assembly and lipid raft microdomains: A role for the cytoplasmic tails of the spike glycoproteins
    • Zhang, J., A. Pekosz, and R. A. Lamb. 2000. Influenza virus assembly and lipid raft microdomains: a role for the cytoplasmic tails of the spike glycoproteins. J. Virol. 74:4634-4644.
    • (2000) J. Virol. , vol.74 , pp. 4634-4644
    • Zhang, J.1    Pekosz, A.2    Lamb, R.A.3
  • 53
    • 0034687711 scopus 로고    scopus 로고
    • Structural characterization of the human respiratory syncytial virus fusion protein core
    • Zhao, X., M. Singh, V. N. Malashkevich, and P. S. Kim. 2000. Structural characterization of the human respiratory syncytial virus fusion protein core. Proc. Natl. Acad. Sci. USA 97:14172-14177.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14172-14177
    • Zhao, X.1    Singh, M.2    Malashkevich, V.N.3    Kim, P.S.4


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