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Volumn 7, Issue 11, 2012, Pages

Specific Residues in the 2009 H1N1 Swine-Origin Influenza Matrix Protein Influence Virion Morphology and Efficiency of Viral Spread In Vitro

Author keywords

[No Author keywords available]

Indexed keywords

MATRIX PROTEIN; PROTEIN M1; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84870276860     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0050595     Document Type: Article
Times cited : (29)

References (49)
  • 2
    • 32944478317 scopus 로고    scopus 로고
    • Emerging and re-emerging infectious diseases: influenza as a prototype of the host-pathogen balancing act
    • Fauci AS, (2006) Emerging and re-emerging infectious diseases: influenza as a prototype of the host-pathogen balancing act. Cell 124: 665-670.
    • (2006) Cell , vol.124 , pp. 665-670
    • Fauci, A.S.1
  • 3
    • 67649297821 scopus 로고    scopus 로고
    • Emergence and pandemic potential of swine-origin H1N1 influenza virus
    • Neumann G, Noda T, Kawaoka Y, (2009) Emergence and pandemic potential of swine-origin H1N1 influenza virus. Nature 459: 931-939.
    • (2009) Nature , vol.459 , pp. 931-939
    • Neumann, G.1    Noda, T.2    Kawaoka, Y.3
  • 4
    • 67650407532 scopus 로고    scopus 로고
    • Antigenic and genetic characteristics of swine-origin 2009 A(H1N1) influenza viruses circulating in humans
    • Garten RJ, Davis CT, Russell CA, Shu B, Lindstrom S, et al. (2009) Antigenic and genetic characteristics of swine-origin 2009 A(H1N1) influenza viruses circulating in humans. Science 325: 197-201.
    • (2009) Science , vol.325 , pp. 197-201
    • Garten, R.J.1    Davis, C.T.2    Russell, C.A.3    Shu, B.4    Lindstrom, S.5
  • 6
    • 50849118488 scopus 로고    scopus 로고
    • Human case of swine influenza A (H1N1) triple reassortant virus infection, Wisconsin
    • Newman AP, Reisdorf E, Beinemann J, Uyeki TM, Balish A, et al. (2008) Human case of swine influenza A (H1N1) triple reassortant virus infection, Wisconsin. Emerg Infect Dis 14: 1470-1472.
    • (2008) Emerg Infect Dis , vol.14 , pp. 1470-1472
    • Newman, A.P.1    Reisdorf, E.2    Beinemann, J.3    Uyeki, T.M.4    Balish, A.5
  • 7
    • 67449152290 scopus 로고    scopus 로고
    • Triple-reassortant swine influenza A (H1) in humans in the United States, 2005-2009
    • Shinde V, Bridges CB, Uyeki TM, Shu B, Balish A, et al. (2009) Triple-reassortant swine influenza A (H1) in humans in the United States, 2005-2009. N Engl J Med 360: 2616-2625.
    • (2009) N Engl J Med , vol.360 , pp. 2616-2625
    • Shinde, V.1    Bridges, C.B.2    Uyeki, T.M.3    Shu, B.4    Balish, A.5
  • 8
    • 9644283009 scopus 로고    scopus 로고
    • Assembly and budding of influenza virus
    • Nayak DP, Hui EK, Barman S, (2004) Assembly and budding of influenza virus. Virus Res 106: 147-165.
    • (2004) Virus Res , vol.106 , pp. 147-165
    • Nayak, D.P.1    Hui, E.K.2    Barman, S.3
  • 9
    • 84855259679 scopus 로고    scopus 로고
    • Eurasian-origin gene segments contribute to the transmissibility, aerosol release, and morphology of the 2009 pandemic H1N1 influenza virus
    • Lakdawala SS, Lamirande EW, Suguitan AL Jr, Wang W, Santos CP, et al. (2011) Eurasian-origin gene segments contribute to the transmissibility, aerosol release, and morphology of the 2009 pandemic H1N1 influenza virus. PLoS Pathog 7: e1002443.
    • (2011) PLoS Pathog , vol.7
    • Lakdawala, S.S.1    Lamirande, E.W.2    Suguitan Jr., A.L.3    Wang, W.4    Santos, C.P.5
  • 10
    • 0029794377 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin and neuraminidase glycoproteins stimulate the membrane association of the matrix protein
    • Enami M, Enami K, (1996) Influenza virus hemagglutinin and neuraminidase glycoproteins stimulate the membrane association of the matrix protein. J Virol 70: 6653-6657.
    • (1996) J Virol , vol.70 , pp. 6653-6657
    • Enami, M.1    Enami, K.2
  • 11
    • 0030991137 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape
    • Jin H, Leser GP, Zhang J, Lamb RA, (1997) Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape. Embo J 16: 1236-1247.
    • (1997) Embo J , vol.16 , pp. 1236-1247
    • Jin, H.1    Leser, G.P.2    Zhang, J.3    Lamb, R.A.4
  • 12
    • 0033858756 scopus 로고    scopus 로고
    • Influenza virus assembly: effect of influenza virus glycoproteins on the membrane association of M1 protein
    • Ali A, Avalos RT, Ponimaskin E, Nayak DP, (2000) Influenza virus assembly: effect of influenza virus glycoproteins on the membrane association of M1 protein. J Virol 74: 8709-8719.
    • (2000) J Virol , vol.74 , pp. 8709-8719
    • Ali, A.1    Avalos, R.T.2    Ponimaskin, E.3    Nayak, D.P.4
  • 13
    • 0032865668 scopus 로고    scopus 로고
    • Association of influenza virus matrix protein with ribonucleoproteins
    • Ye Z, Liu T, Offringa DP, McInnis J, Levandowski RA, (1999) Association of influenza virus matrix protein with ribonucleoproteins. J Virol 73: 7467-7473.
    • (1999) J Virol , vol.73 , pp. 7467-7473
    • Ye, Z.1    Liu, T.2    Offringa, D.P.3    McInnis, J.4    Levandowski, R.A.5
  • 14
    • 0035264603 scopus 로고    scopus 로고
    • In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein
    • Baudin F, Petit I, Weissenhorn W, Ruigrok RW, (2001) In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein. Virology 281: 102-108.
    • (2001) Virology , vol.281 , pp. 102-108
    • Baudin, F.1    Petit, I.2    Weissenhorn, W.3    Ruigrok, R.W.4
  • 15
    • 34547584458 scopus 로고    scopus 로고
    • Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions
    • Noton SL, Medcalf E, Fisher D, Mullin AE, Elton D, et al. (2007) Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions. J Gen Virol 88: 2280-2290.
    • (2007) J Gen Virol , vol.88 , pp. 2280-2290
    • Noton, S.L.1    Medcalf, E.2    Fisher, D.3    Mullin, A.E.4    Elton, D.5
  • 16
    • 0027236576 scopus 로고
    • Molecular assembly of influenza virus: association of the NS2 protein with virion matrix
    • Yasuda J, Nakada S, Kato A, Toyoda T, Ishihama A, (1993) Molecular assembly of influenza virus: association of the NS2 protein with virion matrix. Virology 196: 249-255.
    • (1993) Virology , vol.196 , pp. 249-255
    • Yasuda, J.1    Nakada, S.2    Kato, A.3    Toyoda, T.4    Ishihama, A.5
  • 17
    • 0141737104 scopus 로고    scopus 로고
    • Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2)
    • Akarsu H, Burmeister WP, Petosa C, Petit I, Muller CW, et al. (2003) Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2). Embo J 22: 4646-4655.
    • (2003) Embo J , vol.22 , pp. 4646-4655
    • Akarsu, H.1    Burmeister, W.P.2    Petosa, C.3    Petit, I.4    Muller, C.W.5
  • 18
    • 0033946767 scopus 로고    scopus 로고
    • Role of the influenza virus M1 protein in nuclear export of viral ribonucleoproteins
    • Bui M, Wills EG, Helenius A, Whittaker GR, (2000) Role of the influenza virus M1 protein in nuclear export of viral ribonucleoproteins. J Virol 74: 1781-1786.
    • (2000) J Virol , vol.74 , pp. 1781-1786
    • Bui, M.1    Wills, E.G.2    Helenius, A.3    Whittaker, G.R.4
  • 19
    • 0035450255 scopus 로고    scopus 로고
    • Effect of influenza virus matrix protein and viral RNA on ribonucleoprotein formation and nuclear export
    • Huang X, Liu T, Muller J, Levandowski RA, Ye Z, (2001) Effect of influenza virus matrix protein and viral RNA on ribonucleoprotein formation and nuclear export. Virology 287: 405-416.
    • (2001) Virology , vol.287 , pp. 405-416
    • Huang, X.1    Liu, T.2    Muller, J.3    Levandowski, R.A.4    Ye, Z.5
  • 20
    • 80055120822 scopus 로고    scopus 로고
    • The M segment of the 2009 new pandemic H1N1 influenza virus is critical for its high transmission efficiency in the guinea pig model
    • Chou YY, Albrecht RA, Pica N, Lowen AC, Richt JA, et al. (2011) The M segment of the 2009 new pandemic H1N1 influenza virus is critical for its high transmission efficiency in the guinea pig model. J Virol 85: 11235-11241.
    • (2011) J Virol , vol.85 , pp. 11235-11241
    • Chou, Y.Y.1    Albrecht, R.A.2    Pica, N.3    Lowen, A.C.4    Richt, J.A.5
  • 21
    • 0028047505 scopus 로고
    • Fine structure of influenza A virus observed by electron cryo-microscopy
    • Fujiyoshi Y, Kume NP, Sakata K, Sato SB, (1994) Fine structure of influenza A virus observed by electron cryo-microscopy. Embo J 13: 318-326.
    • (1994) Embo J , vol.13 , pp. 318-326
    • Fujiyoshi, Y.1    Kume, N.P.2    Sakata, K.3    Sato, S.B.4
  • 22
    • 0037370304 scopus 로고    scopus 로고
    • Reverse genetics studies on the filamentous morphology of influenza A virus
    • Bourmakina SV, Garcia-Sastre A, (2003) Reverse genetics studies on the filamentous morphology of influenza A virus. J Gen Virol 84: 517-527.
    • (2003) J Gen Virol , vol.84 , pp. 517-527
    • Bourmakina, S.V.1    Garcia-Sastre, A.2
  • 23
    • 1642274781 scopus 로고    scopus 로고
    • The M1 matrix protein controls the filamentous phenotype of influenza A virus
    • Elleman CJ, Barclay WS, (2004) The M1 matrix protein controls the filamentous phenotype of influenza A virus. Virology 321: 144-153.
    • (2004) Virology , vol.321 , pp. 144-153
    • Elleman, C.J.1    Barclay, W.S.2
  • 24
    • 11144244386 scopus 로고    scopus 로고
    • Influenza a viruses with mutations in the m1 helix six domain display a wide variety of morphological phenotypes
    • Burleigh LM, Calder LJ, Skehel JJ, Steinhauer DA, (2005) Influenza a viruses with mutations in the m1 helix six domain display a wide variety of morphological phenotypes. J Virol 79: 1262-1270.
    • (2005) J Virol , vol.79 , pp. 1262-1270
    • Burleigh, L.M.1    Calder, L.J.2    Skehel, J.J.3    Steinhauer, D.A.4
  • 25
    • 0000443647 scopus 로고
    • Filamentous forms associated with newly isolated influenza virus
    • Chu CM, Dawson IM, Elford WJ, (1949) Filamentous forms associated with newly isolated influenza virus. Lancet 1: 602.
    • (1949) Lancet , vol.1 , pp. 602
    • Chu, C.M.1    Dawson, I.M.2    Elford, W.J.3
  • 26
    • 0000128765 scopus 로고
    • Genetic studies of influenza viruses. I. Viral morphology and growth capacity as exchangeable genetic traits. Rapid in ovo adaptation of early passage Asian strain isolates by combination with PR8
    • Kilbourne ED, Murphy JS, (1960) Genetic studies of influenza viruses. I. Viral morphology and growth capacity as exchangeable genetic traits. Rapid in ovo adaptation of early passage Asian strain isolates by combination with PR8. J Exp Med 111: 387-406.
    • (1960) J Exp Med , vol.111 , pp. 387-406
    • Kilbourne, E.D.1    Murphy, J.S.2
  • 27
    • 0000283734 scopus 로고
    • Studies of two kinds of virus particles which comprise influenza A2 virus strains. III. Morphological characteristics: independence to morphological and functional traits
    • Choppin PW, Murphy JS, Tamm I, (1960) Studies of two kinds of virus particles which comprise influenza A2 virus strains. III. Morphological characteristics: independence to morphological and functional traits. J Exp Med 112: 945-952.
    • (1960) J Exp Med , vol.112 , pp. 945-952
    • Choppin, P.W.1    Murphy, J.S.2    Tamm, I.3
  • 28
    • 69149093400 scopus 로고    scopus 로고
    • In vitro and in vivo characterization of new swine-origin H1N1 influenza viruses
    • Itoh Y, Shinya K, Kiso M, Watanabe T, Sakoda Y, et al. (2009) In vitro and in vivo characterization of new swine-origin H1N1 influenza viruses. Nature 460: 1021-1025.
    • (2009) Nature , vol.460 , pp. 1021-1025
    • Itoh, Y.1    Shinya, K.2    Kiso, M.3    Watanabe, T.4    Sakoda, Y.5
  • 29
    • 76649133449 scopus 로고    scopus 로고
    • The first autopsy case of pandemic influenza (A/H1N1pdm) virus infection in Japan: detection of a high copy number of the virus in type II alveolar epithelial cells by pathological and virological examination
    • Nakajima N, Hata S, Sato Y, Tobiume M, Katano H, et al. (2010) The first autopsy case of pandemic influenza (A/H1N1pdm) virus infection in Japan: detection of a high copy number of the virus in type II alveolar epithelial cells by pathological and virological examination. Jpn J Infect Dis 63: 67-71.
    • (2010) Jpn J Infect Dis , vol.63 , pp. 67-71
    • Nakajima, N.1    Hata, S.2    Sato, Y.3    Tobiume, M.4    Katano, H.5
  • 30
    • 0032484479 scopus 로고    scopus 로고
    • The M1 and M2 proteins of influenza A virus are important determinants in filamentous particle formation
    • Roberts PC, Lamb RA, Compans RW, (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
  • 31
    • 0036935791 scopus 로고    scopus 로고
    • Association of influenza virus matrix protein with ribonucleoproteins may control viral growth and morphology
    • Liu T, Muller J, Ye Z, (2002) Association of influenza virus matrix protein with ribonucleoproteins may control viral growth and morphology. Virology 304: 89-96.
    • (2002) Virology , vol.304 , pp. 89-96
    • Liu, T.1    Muller, J.2    Ye, Z.3
  • 32
    • 33746810932 scopus 로고    scopus 로고
    • Distinct domains of the influenza a virus M2 protein cytoplasmic tail mediate binding to the M1 protein and facilitate infectious virus production
    • McCown MF, Pekosz A, (2006) Distinct domains of the influenza a virus M2 protein cytoplasmic tail mediate binding to the M1 protein and facilitate infectious virus production. J Virol 80: 8178-8189.
    • (2006) J Virol , vol.80 , pp. 8178-8189
    • McCown, M.F.1    Pekosz, A.2
  • 33
    • 33646718791 scopus 로고    scopus 로고
    • The cytoplasmic tail of the influenza A virus M2 protein plays a role in viral assembly
    • Iwatsuki-Horimoto K, Horimoto T, Noda T, Kiso M, Maeda J, et al. (2006) The cytoplasmic tail of the influenza A virus M2 protein plays a role in viral assembly. J Virol 80: 5233-5240.
    • (2006) J Virol , vol.80 , pp. 5233-5240
    • Iwatsuki-Horimoto, K.1    Horimoto, T.2    Noda, T.3    Kiso, M.4    Maeda, J.5
  • 34
    • 58149526763 scopus 로고    scopus 로고
    • Studies of an influenza A virus temperature-sensitive mutant identify a late role for NP in the formation of infectious virions
    • Noton SL, Simpson-Holley M, Medcalf E, Wise HM, Hutchinson EC, et al. (2009) Studies of an influenza A virus temperature-sensitive mutant identify a late role for NP in the formation of infectious virions. J Virol 83: 562-571.
    • (2009) J Virol , vol.83 , pp. 562-571
    • Noton, S.L.1    Simpson-Holley, M.2    Medcalf, E.3    Wise, H.M.4    Hutchinson, E.C.5
  • 35
    • 77951437276 scopus 로고    scopus 로고
    • Influenza virus m2 ion channel protein is necessary for filamentous virion formation
    • Rossman JS, Jing X, Leser GP, Balannik V, Pinto LH, et al. (2010) Influenza virus m2 ion channel protein is necessary for filamentous virion formation. J Virol 84: 5078-5088.
    • (2010) J Virol , vol.84 , pp. 5078-5088
    • Rossman, J.S.1    Jing, X.2    Leser, G.P.3    Balannik, V.4    Pinto, L.H.5
  • 36
    • 77956270840 scopus 로고    scopus 로고
    • Formation of virus-like particles from human cell lines exclusively expressing influenza neuraminidase
    • Lai JC, Chan WW, Kien F, Nicholls JM, Peiris JS, et al. (2010) Formation of virus-like particles from human cell lines exclusively expressing influenza neuraminidase. J Gen Virol 91: 2322-2330.
    • (2010) J Gen Virol , vol.91 , pp. 2322-2330
    • Lai, J.C.1    Chan, W.W.2    Kien, F.3    Nicholls, J.M.4    Peiris, J.S.5
  • 37
    • 77950789595 scopus 로고    scopus 로고
    • The lack of an inherent membrane targeting signal is responsible for the failure of the matrix (M1) protein of influenza A virus to bud into virus-like particles
    • Wang D, Harmon A, Jin J, Francis DH, Christopher-Hennings J, et al. (2010) The lack of an inherent membrane targeting signal is responsible for the failure of the matrix (M1) protein of influenza A virus to bud into virus-like particles. J Virol 84: 4673-4681.
    • (2010) J Virol , vol.84 , pp. 4673-4681
    • Wang, D.1    Harmon, A.2    Jin, J.3    Francis, D.H.4    Christopher-Hennings, J.5
  • 38
    • 77956637693 scopus 로고    scopus 로고
    • Influenza virus M2 protein mediates ESCRT-independent membrane scission
    • Rossman JS, Jing X, Leser GP, Lamb RA, (2010) Influenza virus M2 protein mediates ESCRT-independent membrane scission. Cell 142: 902-913.
    • (2010) Cell , vol.142 , pp. 902-913
    • Rossman, J.S.1    Jing, X.2    Leser, G.P.3    Lamb, R.A.4
  • 41
    • 33750569806 scopus 로고    scopus 로고
    • Review of aerosol transmission of influenza A virus
    • Tellier R, (2006) Review of aerosol transmission of influenza A virus. Emerg Infect Dis 12: 1657-1662.
    • (2006) Emerg Infect Dis , vol.12 , pp. 1657-1662
    • Tellier, R.1
  • 42
    • 79952069060 scopus 로고    scopus 로고
    • Influenza virus assembly and budding
    • Rossman JS, Lamb RA, (2011) Influenza virus assembly and budding. Virology 411: 229-236.
    • (2011) Virology , vol.411 , pp. 229-236
    • Rossman, J.S.1    Lamb, R.A.2
  • 43
    • 0034630492 scopus 로고    scopus 로고
    • The cytoplasmic tails of the influenza virus spike glycoproteins are required for normal genome packaging
    • Zhang J, Leser GP, Pekosz A, Lamb RA, (2000) The cytoplasmic tails of the influenza virus spike glycoproteins are required for normal genome packaging. Virology 269: 325-334.
    • (2000) Virology , vol.269 , pp. 325-334
    • Zhang, J.1    Leser, G.P.2    Pekosz, A.3    Lamb, R.A.4
  • 44
    • 53749092893 scopus 로고    scopus 로고
    • The influenza virus M2 protein cytoplasmic tail interacts with the M1 protein and influences virus assembly at the site of virus budding
    • Chen BJ, Leser GP, Jackson D, Lamb RA, (2008) The influenza virus M2 protein cytoplasmic tail interacts with the M1 protein and influences virus assembly at the site of virus budding. J Virol 82: 10059-10070.
    • (2008) J Virol , vol.82 , pp. 10059-10070
    • Chen, B.J.1    Leser, G.P.2    Jackson, D.3    Lamb, R.A.4
  • 45
    • 27644440465 scopus 로고    scopus 로고
    • Influenza virus assembly and budding in raft-derived microdomains: a quantitative analysis of the surface distribution of HA, NA and M2 proteins
    • Leser GP, Lamb RA, (2005) Influenza virus assembly and budding in raft-derived microdomains: a quantitative analysis of the surface distribution of HA, NA and M2 proteins. Virology 342: 215-227.
    • (2005) Virology , vol.342 , pp. 215-227
    • Leser, G.P.1    Lamb, R.A.2
  • 46
    • 26944491901 scopus 로고    scopus 로고
    • Influenza virus assembly and budding at the viral budozone
    • Schmitt AP, Lamb RA, (2005) Influenza virus assembly and budding at the viral budozone. Adv Virus Res 64: 383-416.
    • (2005) Adv Virus Res , vol.64 , pp. 383-416
    • Schmitt, A.P.1    Lamb, R.A.2
  • 48
    • 77950835010 scopus 로고    scopus 로고
    • PB2 residue 271 plays a key role in enhanced polymerase activity of influenza A viruses in mammalian host cells
    • Bussey KA, Bousse TL, Desmet EA, Kim B, Takimoto T, (2010) PB2 residue 271 plays a key role in enhanced polymerase activity of influenza A viruses in mammalian host cells. J Virol 84: 4395-4406.
    • (2010) J Virol , vol.84 , pp. 4395-4406
    • Bussey, K.A.1    Bousse, T.L.2    Desmet, E.A.3    Kim, B.4    Takimoto, T.5


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