메뉴 건너뛰기




Volumn 4, Issue 3, 2009, Pages

Interaction of the Coronavirus Infectious Bronchitis Virus Membrane Protein with β-Actin and Its Implication in Virion Assembly and Budding

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; MATRIX PROTEIN; PRIMER DNA;

EID: 66149095115     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0004908     Document Type: Article
Times cited : (50)

References (42)
  • 2
    • 0026934552 scopus 로고
    • Cell biology of viruses that assemble along the biosynthetic pathway
    • Griffiths G, Rottier P, (1992) Cell biology of viruses that assemble along the biosynthetic pathway. Semin Cell Biol 3: 367-381.
    • (1992) Semin Cell Biol , vol.3 , pp. 367-381
    • Griffiths, G.1    Rottier, P.2
  • 3
    • 34548861233 scopus 로고    scopus 로고
    • Cargos and genes: insights into vesicular transport from inherited human disease
    • Gissen P, Maher ER, (2007) Cargos and genes: insights into vesicular transport from inherited human disease. J Med Genet 44: 545-555.
    • (2007) J Med Genet , vol.44 , pp. 545-555
    • Gissen, P.1    Maher, E.R.2
  • 4
    • 0031950008 scopus 로고    scopus 로고
    • Coronavirus Particle Assembly: Primary Structure Requirements of the Membrane Protein
    • de Haan CAM, Kuo L, Masters PS, Vennema H, Rottier PJM, (1998) Coronavirus Particle Assembly: Primary Structure Requirements of the Membrane Protein. J Virol 72: 6838-6850.
    • (1998) J Virol , vol.72 , pp. 6838-6850
    • de Haan, C.A.M.1    Kuo, L.2    Masters, P.S.3    Vennema, H.4    Rottier, P.J.M.5
  • 5
    • 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
    • Krijnse-Locker J, Ericsson M, Rottier PJM, Griffiths G, (1994) 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: 55-70.
    • (1994) J Cell Biol , vol.124 , pp. 55-70
    • Krijnse-Locker, J.1    Ericsson, M.2    Rottier, P.J.M.3    Griffiths, G.4
  • 6
    • 0002753706 scopus 로고
    • The coronavirus membrane glycoprotein
    • In: Siddell SG, editors, New York, NY, Plnum Press
    • Rottier PJM, (1995) The coronavirus membrane glycoprotein. In: Siddell SG, editors. The Coronaviridae New York, NY Plnum Press pp. 115-139.
    • (1995) The Coronaviridae , pp. 115-139
    • Rottier, P.J.M.1
  • 7
    • 0030782149 scopus 로고    scopus 로고
    • Protein interactions during coronavirus assembly
    • Nguyen V-P, Hogue BG, (1997) Protein interactions during coronavirus assembly. J Virol 71: 9278-9284.
    • (1997) J Virol , vol.71 , pp. 9278-9284
    • Nguyen, V.-P.1    Hogue, B.G.2
  • 8
    • 0028133370 scopus 로고
    • Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding
    • Klumperman J, Krijnse-Locker J, Meijer A, Horzinek MC, Geuze HJ, et al.(1994) Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding. J Virol 68: 6523-6534.
    • (1994) J Virol , vol.68 , pp. 6523-6534
    • Klumperman, J.1    Krijnse-Locker, J.2    Meijer, A.3    Horzinek, M.C.4    Geuze, H.J.5
  • 9
    • 0026691820 scopus 로고
    • O-glycosylation of the coronavirus M protein. Differential localization of sialyltransferases in N- and O-linked glycosylation
    • Krijnse-Locker J, Griffiths G, Horzinek G, Rottier PJM, (1992) O-glycosylation of the coronavirus M protein. Differential localization of sialyltransferases in N- and O-linked glycosylation. J Biol Chem 267: 14094-14101.
    • (1992) J Biol Chem , vol.267 , pp. 14094-14101
    • Krijnse-Locker, J.1    Griffiths, G.2    Horzinek, G.3    Rottier, P.J.M.4
  • 10
    • 0029933250 scopus 로고    scopus 로고
    • Nucleocapsid-independent assembly of coronavirus-like particles by coexpression of viral envelope protein genes
    • Vennema H, Godeke G-J, Rossen JWA, Voorhout WF, Horzinek MC, et al.(1996) Nucleocapsid-independent assembly of coronavirus-like particles by coexpression of viral envelope protein genes. EMBO J 15: 2020-2028.
    • (1996) EMBO J , vol.15 , pp. 2020-2028
    • Vennema, H.1    Godeke, G.-J.2    Rossen, J.W.A.3    Voorhout, W.F.4    Horzinek, M.C.5
  • 11
    • 0033899980 scopus 로고    scopus 로고
    • Characterization of the coronavirus M protein and nucleocapsid interaction in infected cells
    • Narayanan K, Maeda A, Maeda J, Makino S, (2000) Characterization of the coronavirus M protein and nucleocapsid interaction in infected cells. J Virol 74: 8127-8134.
    • (2000) J Virol , vol.74 , pp. 8127-8134
    • Narayanan, K.1    Maeda, A.2    Maeda, J.3    Makino, S.4
  • 12
  • 14
    • 33846074516 scopus 로고    scopus 로고
    • An arginine-to-proline mutation in a domain with undefined function within the RNA helicase protein (NSP13) is lethal to the coronavirus infectious bronchitis virus in cultured cells
    • Fang SG, Chen B, Tay FPL, Liu DX, (2006) An arginine-to-proline mutation in a domain with undefined function within the RNA helicase protein (NSP13) is lethal to the coronavirus infectious bronchitis virus in cultured cells. Virology 358: 136-147.
    • (2006) Virology , vol.358 , pp. 136-147
    • Fang, S.G.1    Chen, B.2    Tay, F.P.L.3    Liu, D.X.4
  • 15
    • 0031058476 scopus 로고    scopus 로고
    • Proteolytic processing of the coronavirus infectious bronchitis virus 1a polyprotein: identification of a 10-kilodalton polypeptide and determination of its cleavage sites
    • Liu DX, Xu HY, Brown TDK, (1997) Proteolytic processing of the coronavirus infectious bronchitis virus 1a polyprotein: identification of a 10-kilodalton polypeptide and determination of its cleavage sites. J Virol 71: 1814-1820.
    • (1997) J Virol , vol.71 , pp. 1814-1820
    • Liu, D.X.1    Xu, H.Y.2    Brown, T.D.K.3
  • 16
    • 0026351776 scopus 로고
    • Association of the infectious bronchitis virus 3c protein with the virion envelope
    • Liu DX, Inglis SC, (1991) Association of the infectious bronchitis virus 3c protein with the virion envelope. Virology 185: 911-917.
    • (1991) Virology , vol.185 , pp. 911-917
    • Liu, D.X.1    Inglis, S.C.2
  • 17
    • 34547808270 scopus 로고    scopus 로고
    • Cell cycle arrest and apoptosis induced by the coronavirus infectious bronchitis virus in the absence of p53
    • Li FQ, Tam JP, Liu DX, (2007) Cell cycle arrest and apoptosis induced by the coronavirus infectious bronchitis virus in the absence of p53. Virology 365: 435-45.
    • (2007) Virology , vol.365 , pp. 435-445
    • Li, F.Q.1    Tam, J.P.2    Liu, D.X.3
  • 18
    • 0020051819 scopus 로고
    • Structural analysis of virion proteins of the avian coronavirus infectious bronchitis virus
    • Stern DF, Burgess L, Sefton BM, (1982) Structural analysis of virion proteins of the avian coronavirus infectious bronchitis virus. J Virol 42: 208-219.
    • (1982) J Virol , vol.42 , pp. 208-219
    • Stern, D.F.1    Burgess, L.2    Sefton, B.M.3
  • 19
    • 0018868438 scopus 로고
    • Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid
    • Sturman LS, Holmes KV, Behnke J, (1980) Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid. J Virol 33: 449-462.
    • (1980) J Virol , vol.33 , pp. 449-462
    • Sturman, L.S.1    Holmes, K.V.2    Behnke, J.3
  • 21
    • 0034067478 scopus 로고    scopus 로고
    • Assembly of the coronavirus envelope: homotypic interactions between the M proteins
    • de Haan CAM, Vennema H, Rottier PJM, (2000) Assembly of the coronavirus envelope: homotypic interactions between the M proteins. J Virol 74: 4967-4978.
    • (2000) J Virol , vol.74 , pp. 4967-4978
    • de Haan, C.A.M.1    Vennema, H.2    Rottier, P.J.M.3
  • 22
    • 0027049212 scopus 로고
    • Cellular proteins bound to immunodeficiency viruses: implications for pathogenesis and vaccines
    • Arthur LO, Bess JW, Sowder RC, Benveniste RE, Mann DL, et al.(1992) Cellular proteins bound to immunodeficiency viruses: implications for pathogenesis and vaccines. Science 258: 1935-1938.
    • (1992) Science , vol.258 , pp. 1935-1938
    • Arthur, L.O.1    Bess, J.W.2    Sowder, R.C.3    Benveniste, R.E.4    Mann, D.L.5
  • 23
    • 0015579722 scopus 로고
    • Chromatographic and electrophoretic analysis of viral proteins from hamster and chicken cells transformed by rous sarcoma virus
    • Fleissner E, Tress E, (1973) Chromatographic and electrophoretic analysis of viral proteins from hamster and chicken cells transformed by rous sarcoma virus. J Virol 11: 250-262.
    • (1973) J Virol , vol.11 , pp. 250-262
    • Fleissner, E.1    Tress, E.2
  • 24
    • 0017250110 scopus 로고
    • The synthesis of sendai virus polypeptides in infected cells
    • Lamb RA, Mahy BWJ, Choppin PW, (1976) The synthesis of sendai virus polypeptides in infected cells. Virology 69: 116-131.
    • (1976) Virology , vol.69 , pp. 116-131
    • Lamb, R.A.1    Mahy, B.W.J.2    Choppin, P.W.3
  • 25
    • 0017799006 scopus 로고
    • Structural polypeptides of measles virus
    • Tyrrell DLJ, Norrby E, (1978) Structural polypeptides of measles virus. J Gen Virol 39: 219-229.
    • (1978) J Gen Virol , vol.39 , pp. 219-229
    • Tyrrell, D.L.J.1    Norrby, E.2
  • 26
    • 0018159540 scopus 로고
    • Structural polypeptides of mumps virus
    • Örvell C, (1978) Structural polypeptides of mumps virus. J Gen Virol 41: 527-539.
    • (1978) J Gen Virol , vol.41 , pp. 527-539
    • Örvell, C.1
  • 27
    • 0029836852 scopus 로고    scopus 로고
    • Cytoskeletal proteins inside human immunodeficiency virus type 1 virions
    • Ott DE, Coren LV, Kane BP, Busch LK, Johnson DG, et al.(1996) Cytoskeletal proteins inside human immunodeficiency virus type 1 virions. J Virol 70: 7734-7743.
    • (1996) J Virol , vol.70 , pp. 7734-7743
    • Ott, D.E.1    Coren, L.V.2    Kane, B.P.3    Busch, L.K.4    Johnson, D.G.5
  • 28
    • 33645760961 scopus 로고    scopus 로고
    • Rotavirus spike protein VP4 binds to and remodels Actin bundles of the epithelial brush border into Actin bodies
    • Gardet A, Breton M, Fontanges P, Trugnan G, Chwetzoff S, (2006) Rotavirus spike protein VP4 binds to and remodels Actin bundles of the epithelial brush border into Actin bodies. J Virol 80: 3947-3956.
    • (2006) J Virol , vol.80 , pp. 3947-3956
    • Gardet, A.1    Breton, M.2    Fontanges, P.3    Trugnan, G.4    Chwetzoff, S.5
  • 29
    • 33244462037 scopus 로고    scopus 로고
    • Dynamics of membranes driven by actin polymerization
    • Gov NS, Gopinathan A, (2006) Dynamics of membranes driven by actin polymerization. J Biophy 90: 454-469.
    • (2006) J Biophy , vol.90 , pp. 454-469
    • Gov, N.S.1    Gopinathan, A.2
  • 30
    • 0016539731 scopus 로고
    • Polar appearance and nonligand induced spreading of measles virus hemagglutinin at the surface of chronically infected cells
    • Ehrnst A, Sundquist KG, (1975) Polar appearance and nonligand induced spreading of measles virus hemagglutinin at the surface of chronically infected cells. Cell 5: 351-359.
    • (1975) Cell , vol.5 , pp. 351-359
    • Ehrnst, A.1    Sundquist, K.G.2
  • 31
    • 0017211069 scopus 로고
    • The mechanisms of appearance of viral glycoproteins at cell surface membrane
    • Ehrnst A, Sundquist KG, (1976) The mechanisms of appearance of viral glycoproteins at cell surface membrane. Exp Cell Biol 44: 198-225.
    • (1976) Exp Cell Biol , vol.44 , pp. 198-225
    • Ehrnst, A.1    Sundquist, K.G.2
  • 32
    • 0242362835 scopus 로고    scopus 로고
    • Interaction of cellular tubulin with Sendai virus M protein regulates transcription of viral genome
    • Ogino T, Iwama M, Ohsawa Y, Mizumoto K, (2003) Interaction of cellular tubulin with Sendai virus M protein regulates transcription of viral genome. Biochem Biophy Res Commun 311: 283-293.
    • (2003) Biochem Biophy Res Commun , vol.311 , pp. 283-293
    • Ogino, T.1    Iwama, M.2    Ohsawa, Y.3    Mizumoto, K.4
  • 33
    • 47049088603 scopus 로고    scopus 로고
    • The nucleocapsid protein of severe acute respiratory syndrome coronavirus inhibits cell cytokinesis and proliferation by interacting with translation elongation factor 1alpha
    • Zhou B, Liu J, Wang Q, Liu X, Li X, et al.(2008) The nucleocapsid protein of severe acute respiratory syndrome coronavirus inhibits cell cytokinesis and proliferation by interacting with translation elongation factor 1alpha. J Virol 82: 6962-71.
    • (2008) J Virol , vol.82 , pp. 6962-6971
    • Zhou, B.1    Liu, J.2    Wang, Q.3    Liu, X.4    Li, X.5
  • 34
    • 6344233443 scopus 로고    scopus 로고
    • The SARS coronavirus nucleocapsid protein induces actin reorganization and apoptosis in COS-1 cells in the absence of growth factors
    • Surjit M, Liu B, Jameel S, Chow VT, Lal SK, (2004) The SARS coronavirus nucleocapsid protein induces actin reorganization and apoptosis in COS-1 cells in the absence of growth factors. Biochem J 383: 13-8.
    • (2004) Biochem J , vol.383 , pp. 13-18
    • Surjit, M.1    Liu, B.2    Jameel, S.3    Chow, V.T.4    Lal, S.K.5
  • 37
    • 0024829631 scopus 로고
    • Opposite effects of alpha-actinin and of fructose 1,6 -bisphosphate aldolase on the microfilament network. The role of orthophosphate revisited
    • Grazi E, Guidoboni M, (1989) Opposite effects of alpha-actinin and of fructose 1,6-bisphosphate aldolase on the microfilament network. The role of orthophosphate revisited. Biochem Int 19: 1345-1353.
    • (1989) Biochem Int , vol.19 , pp. 1345-1353
    • Grazi, E.1    Guidoboni, M.2
  • 38
    • 0027503487 scopus 로고
    • Identification of an actin binding region in aldolase
    • O'Reilly G, Clarke F, (1993) Identification of an actin binding region in aldolase. FEBS lett 321: 69-72.
    • (1993) FEBS Lett , vol.321 , pp. 69-72
    • O'Reilly, G.1    Clarke, F.2
  • 39
    • 0035861660 scopus 로고    scopus 로고
    • Carcinoembryonic antigen cell adhesion molecule 1 directly associates with cytoskeleton proteins actin and tropomyosin
    • Schumann D, Chen C-J, Kaplan B, Shively JE, (2001) Carcinoembryonic antigen cell adhesion molecule 1 directly associates with cytoskeleton proteins actin and tropomyosin. J Biol Chem 276: 47421-47433.
    • (2001) J Biol Chem , vol.276 , pp. 47421-47433
    • Schumann, D.1    Chen, C.-J.2    Kaplan, B.3    Shively, J.E.4
  • 40
    • 0035157384 scopus 로고    scopus 로고
    • The membrane M protein carboxy terminus binds to transmissible gastroenteritis coronavirus core and contributes to core stability
    • Escors D, Ortego J, Laude H, Enjuanes L, (2001) The membrane M protein carboxy terminus binds to transmissible gastroenteritis coronavirus core and contributes to core stability. J Virol 75: 1312-1324.
    • (2001) J Virol , vol.75 , pp. 1312-1324
    • Escors, D.1    Ortego, J.2    Laude, H.3    Enjuanes, L.4
  • 41
    • 0037369042 scopus 로고    scopus 로고
    • Nucleocapsid-independent specific viral RNA packaging via viral envelope protein and viral RNA signal
    • Narayanan K, Chen CJ, Maeda J, Makino S, (2003) Nucleocapsid-independent specific viral RNA packaging via viral envelope protein and viral RNA signal. J Virol 77: 2922-2927.
    • (2003) J Virol , vol.77 , pp. 2922-2927
    • Narayanan, K.1    Chen, C.J.2    Maeda, J.3    Makino, S.4
  • 42
    • 0032565393 scopus 로고    scopus 로고
    • Cellular factors in the transcription and replication of viral RNA genomes: a parallel to DNA-dependent RNA transcription
    • Lai MNC, (1998) Cellular factors in the transcription and replication of viral RNA genomes: a parallel to DNA-dependent RNA transcription. Virology 244: 1-12.
    • (1998) Virology , vol.244 , pp. 1-12
    • Lai, M.N.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.