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Volumn 90, Issue 19, 2016, Pages 8389-8394

To conquer the host, influenza virus is packing it in: Interferon-antagonistic strategies beyond NS1

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE; INTERFERON; INTERFERON REGULATORY FACTOR 3; MELANOMA DIFFERENTIATION ASSOCIATED PROTEIN 5; MYXOVIRUS RESISTANCE PROTEIN A; NONSTRUCTURAL PROTEIN 1; RETINOIC ACID INDUCIBLE PROTEIN I; UNCLASSIFIED DRUG; INS1 PROTEIN, INFLUENZA VIRUS; VIRAL PROTEIN;

EID: 84990192888     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00041-16     Document Type: Article
Times cited : (16)

References (62)
  • 1
    • 84902494505 scopus 로고    scopus 로고
    • Influenza viruses en route from birds to man
    • Klenk HD. 2014. Influenza viruses en route from birds to man. Cell Host Microbe 15:653-654. http://dx.doi.org/10.1016/j.chom.2014.05.019
    • (2014) Cell Host Microbe , vol.15 , pp. 653-654
    • Klenk, H.D.1
  • 2
    • 84922257981 scopus 로고    scopus 로고
    • Structure of influenza A polymerase bound to the viral RNA promoter
    • Pflug A, Guilligay D, Reich S, Cusack S. 2014. Structure of influenza A polymerase bound to the viral RNA promoter. Nature 516:355-360. http://dx.doi.org/10.1038/nature14008
    • (2014) Nature , vol.516 , pp. 355-360
    • Pflug, A.1    Guilligay, D.2    Reich, S.3    Cusack, S.4
  • 5
    • 84921960062 scopus 로고    scopus 로고
    • Functions of the influenza A virus NS1 protein in antiviral defense
    • Krug RM. 2015. Functions of the influenza A virus NS1 protein in antiviral defense. Curr Opin Virol 12:1-6. http://dx.doi.org/10.1016/j.coviro.2015.01.007
    • (2015) Curr Opin Virol , vol.12 , pp. 1-6
    • Krug, R.M.1
  • 6
    • 84967215091 scopus 로고    scopus 로고
    • Viral evasion of intracellular DNA and RNA sensing
    • Chan YK, Gack MU. 2016. Viral evasion of intracellular DNA and RNA sensing. Nat Rev Microbiol 14:360-373. http://dx.doi.org/10.1038/nrmicro.2016.45
    • (2016) Nat Rev Microbiol , vol.14 , pp. 360-373
    • Chan, Y.K.1    Gack, M.U.2
  • 7
    • 84896987305 scopus 로고    scopus 로고
    • Interferon-stimulated genes: a complex web of host defenses
    • Schneider WM, Chevillotte MD, Rice CM. 2014. Interferon-stimulated genes: a complex web of host defenses. Annu Rev Immunol 32:513-545. http://dx.doi.org/10.1146/annurev-immunol-032713-120231
    • (2014) Annu Rev Immunol , vol.32 , pp. 513-545
    • Schneider, W.M.1    Chevillotte, M.D.2    Rice, C.M.3
  • 9
    • 80052143412 scopus 로고    scopus 로고
    • RIG-I-like receptors: cytoplasmic sensors for non-self RNA
    • Kato H, Takahasi K, Fujita T. 2011. RIG-I-like receptors: cytoplasmic sensors for non-self RNA. Immunol Rev 243:91-98. http://dx.doi.org/10.1111/j.1600-065X.2011.01052.x
    • (2011) Immunol Rev , vol.243 , pp. 91-98
    • Kato, H.1    Takahasi, K.2    Fujita, T.3
  • 10
    • 84929630733 scopus 로고    scopus 로고
    • Influenza A virus panhandle structure is directly involved in RIG-I activation and interferon induction
    • Liu G, Park HS, Pyo HM, Liu Q, Zhou Y. 2015. Influenza A virus panhandle structure is directly involved in RIG-I activation and interferon induction. J Virol 89:6067-6079. http://dx.doi.org/10.1128/JVI.00232-15
    • (2015) J Virol , vol.89 , pp. 6067-6079
    • Liu, G.1    Park, H.S.2    Pyo, H.M.3    Liu, Q.4    Zhou, Y.5
  • 11
  • 16
    • 77957997708 scopus 로고    scopus 로고
    • Preference of RIG-I for short viralRNAmolecules in infected cells revealed by next-generation sequencing
    • Baum A, Sachidanandam R, Garcia-Sastre A. 2010. Preference of RIG-I for short viralRNAmolecules in infected cells revealed by next-generation sequencing. Proc Natl Acad Sci U S A 107:16303-16308. http://dx.doi.org/10.1073/pnas.1005077107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 16303-16308
    • Baum, A.1    Sachidanandam, R.2    Garcia-Sastre, A.3
  • 18
    • 33646453915 scopus 로고    scopus 로고
    • Double-stranded RNA is produced by positive-strand RNA viruses and DNA viruses but not in detectable amounts by negative-strand RNA viruses
    • Weber F, Wagner V, Rasmussen SB, Hartmann R, Paludan SR. 2006. Double-stranded RNA is produced by positive-strand RNA viruses and DNA viruses but not in detectable amounts by negative-strand RNA viruses. J Virol 80:5059-5064. http://dx.doi.org/10.1128/JVI.80.10.5059-5064.2006
    • (2006) J Virol , vol.80 , pp. 5059-5064
    • Weber, F.1    Wagner, V.2    Rasmussen, S.B.3    Hartmann, R.4    Paludan, S.R.5
  • 19
    • 80052285645 scopus 로고    scopus 로고
    • The cellular RNA helicase UAP56 is required for prevention of double-stranded RNA formation during influenza A virus infection
    • Wisskirchen C, Ludersdorfer TH, Muller DA, Moritz E, Pavlovic J. 2011. The cellular RNA helicase UAP56 is required for prevention of double-stranded RNA formation during influenza A virus infection. J Virol 85:8646-8655. http://dx.doi.org/10.1128/JVI.02559-10
    • (2011) J Virol , vol.85 , pp. 8646-8655
    • Wisskirchen, C.1    Ludersdorfer, T.H.2    Muller, D.A.3    Moritz, E.4    Pavlovic, J.5
  • 20
    • 34247565021 scopus 로고    scopus 로고
    • Host-range determinants on the PB2 protein of influenza A viruses control the interaction between the viral polymerase and nucleoprotein in human cells
    • Labadie K, Dos Santos Afonso E, Rameix-Welti MA, van der Werf S, Naffakh N. 2007. Host-range determinants on the PB2 protein of influenza A viruses control the interaction between the viral polymerase and nucleoprotein in human cells. Virology 362:271-282. http://dx.doi.org/10.1016/j.virol.2006.12.027
    • (2007) Virology , vol.362 , pp. 271-282
    • Labadie, K.1    Dos Santos Afonso, E.2    Rameix-Welti, M.A.3    van der Werf, S.4    Naffakh, N.5
  • 21
    • 84953868013 scopus 로고    scopus 로고
    • Mismatches in the influenza A virusRNApanhandle prevent retinoic acid-inducible gene I (RIG-I) sensing by impairing RNA/RIG-I complex formation
    • Anchisi S, Guerra J, Mottet-Osman G, Garcin D. 2015. Mismatches in the influenza A virusRNApanhandle prevent retinoic acid-inducible gene I (RIG-I) sensing by impairing RNA/RIG-I complex formation. J Virol 90:586-590
    • (2015) J Virol , vol.90 , pp. 586-590
    • Anchisi, S.1    Guerra, J.2    Mottet-Osman, G.3    Garcin, D.4
  • 22
    • 84906330873 scopus 로고    scopus 로고
    • Interactions between the influenza A virus RNA polymerase components and retinoic acid-inducible gene I
    • Li W, Chen H, Sutton T, Obadan A, Perez DR. 2014. Interactions between the influenza A virus RNA polymerase components and retinoic acid-inducible gene I. J Virol 88:10432-10447. http://dx.doi.org/10.1128/JVI.01383-14
    • (2014) J Virol , vol.88 , pp. 10432-10447
    • Li, W.1    Chen, H.2    Sutton, T.3    Obadan, A.4    Perez, D.R.5
  • 24
    • 84924767362 scopus 로고    scopus 로고
    • A host susceptibility gene, DR1, facilitates influenza A virus replication by suppressing host innate immunity and enhancing viral RNA replication
    • Hsu SF, Su WC, Jeng KS, Lai MM. 2015. A host susceptibility gene, DR1, facilitates influenza A virus replication by suppressing host innate immunity and enhancing viral RNA replication. J Virol 89:3671-3682. http://dx.doi.org/10.1128/JVI.03610-14
    • (2015) J Virol , vol.89 , pp. 3671-3682
    • Hsu, S.F.1    Su, W.C.2    Jeng, K.S.3    Lai, M.M.4
  • 25
    • 84886389616 scopus 로고    scopus 로고
    • Pooled RNAi screen identifies ubiquitin ligase Itch as crucial for influenza A virus release from the endosome during virus entry
    • Su WC, Chen YC, Tseng CH, Hsu PW, Tung KF, Jeng KS, Lai MM. 2013. Pooled RNAi screen identifies ubiquitin ligase Itch as crucial for influenza A virus release from the endosome during virus entry. Proc Natl Acad Sci U S A 110:17516-17521. http://dx.doi.org/10.1073/pnas.1312374110
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 17516-17521
    • Su, W.C.1    Chen, Y.C.2    Tseng, C.H.3    Hsu, P.W.4    Tung, K.F.5    Jeng, K.S.6    Lai, M.M.7
  • 27
    • 79959823372 scopus 로고    scopus 로고
    • The influenza virus protein PB1-F2 inhibits the induction of type I interferon at the level of the MAVS adaptor protein
    • Varga ZT, Ramos I, Hai R, Schmolke M, Garcia-Sastre A, Fernandez-Sesma A, Palese P. 2011. The influenza virus protein PB1-F2 inhibits the induction of type I interferon at the level of the MAVS adaptor protein. PLoS Pathog 7:e1002067. http://dx.doi.org/10.1371/journal.ppat.1002067
    • (2011) PLoS Pathog , vol.7
    • Varga, Z.T.1    Ramos, I.2    Hai, R.3    Schmolke, M.4    Garcia-Sastre, A.5    Fernandez-Sesma, A.6    Palese, P.7
  • 28
    • 84865095316 scopus 로고    scopus 로고
    • Influenza virus protein PB1-F2 inhibits the induction of type I interferon by binding to MAVS and decreasing mitochondrial membrane potential
    • Varga ZT, Grant A, Manicassamy B, Palese P. 2012. Influenza virus protein PB1-F2 inhibits the induction of type I interferon by binding to MAVS and decreasing mitochondrial membrane potential. J Virol 86: 8359-8366. http://dx.doi.org/10.1128/JVI.01122-12
    • (2012) J Virol , vol.86 , pp. 8359-8366
    • Varga, Z.T.1    Grant, A.2    Manicassamy, B.3    Palese, P.4
  • 29
    • 77956634918 scopus 로고    scopus 로고
    • The PB2 subunit of the influenza virus RNA polymerase affects virulence by interacting with the mitochondrial antiviral signaling protein and inhibiting expression of beta interferon
    • Graef KM, Vreede FT, Lau YF, McCall AW, Carr SM, Subbarao K, Fodor E. 2010. The PB2 subunit of the influenza virus RNA polymerase affects virulence by interacting with the mitochondrial antiviral signaling protein and inhibiting expression of beta interferon. J Virol 84:8433-8445. http://dx.doi.org/10.1128/JVI.00879-10
    • (2010) J Virol , vol.84 , pp. 8433-8445
    • Graef, K.M.1    Vreede, F.T.2    Lau, Y.F.3    McCall, A.W.4    Carr, S.M.5    Subbarao, K.6    Fodor, E.7
  • 30
    • 77957757095 scopus 로고    scopus 로고
    • Influenza A virus polymerase inhibits type I interferon induction by binding to interferon beta promoter stimulator 1
    • Iwai A, Shiozaki T, Kawai T, Akira S, Kawaoka Y, Takada A, Kida H, Miyazaki T. 2010. Influenza A virus polymerase inhibits type I interferon induction by binding to interferon beta promoter stimulator 1. J Biol Chem 285:32064-32074. http://dx.doi.org/10.1074/jbc. M110.112458
    • (2010) J Biol Chem , vol.285 , pp. 32064-32074
    • Iwai, A.1    Shiozaki, T.2    Kawai, T.3    Akira, S.4    Kawaoka, Y.5    Takada, A.6    Kida, H.7    Miyazaki, T.8
  • 31
    • 84873745999 scopus 로고    scopus 로고
    • Influenza A polymerase subunit PB2 possesses overlapping binding sites for polymerase subunit PB1 and human MAVS proteins
    • Patel D, Schultz LW, Umland TC. 2013. Influenza A polymerase subunit PB2 possesses overlapping binding sites for polymerase subunit PB1 and human MAVS proteins. Virus Res 172:75-80. http://dx.doi.org/10.1016/j.virusres.2012.12.003
    • (2013) Virus Res , vol.172 , pp. 75-80
    • Patel, D.1    Schultz, L.W.2    Umland, T.C.3
  • 32
    • 77951043137 scopus 로고    scopus 로고
    • Role of host-specific amino acids in the pathogenicity of avian H5N1 influenza viruses in mice
    • Kim JH, Hatta M, Watanabe S, Neumann G, Watanabe T, Kawaoka Y. 2010. Role of host-specific amino acids in the pathogenicity of avian H5N1 influenza viruses in mice. J Gen Virol 91:1284-1289. http://dx.doi.org/10.1099/vir.0.018143-0
    • (2010) J Gen Virol , vol.91 , pp. 1284-1289
    • Kim, J.H.1    Hatta, M.2    Watanabe, S.3    Neumann, G.4    Watanabe, T.5    Kawaoka, Y.6
  • 34
    • 84937639038 scopus 로고    scopus 로고
    • In vivo RNAi screening identifies MDA5 as a significant contributor to the cellular defense against influenza A virus
    • Benitez AA, Panis M, Xue J, Varble A, Shim JV, Frick AL, Lopez CB, Sachs D, tenOever BR. 2015. In vivo RNAi screening identifies MDA5 as a significant contributor to the cellular defense against influenza A virus. Cell Rep 11:1714-1726. http://dx.doi.org/10.1016/j.celrep.2015.05.032
    • (2015) Cell Rep , vol.11 , pp. 1714-1726
    • Benitez, A.A.1    Panis, M.2    Xue, J.3    Varble, A.4    Shim, J.V.5    Frick, A.L.6    Lopez, C.B.7    Sachs, D.8    tenOever, B.R.9
  • 36
    • 84856850841 scopus 로고    scopus 로고
    • Chicken cells sense influenza A virus infection through MDA5 and CARDIF signaling involving LGP2
    • Liniger M, Summerfield A, Zimmer G, McCullough KC, Ruggli N. 2012. Chicken cells sense influenza A virus infection through MDA5 and CARDIF signaling involving LGP2. J Virol 86:705-717. http://dx.doi.org/10.1128/JVI.00742-11
    • (2012) J Virol , vol.86 , pp. 705-717
    • Liniger, M.1    Summerfield, A.2    Zimmer, G.3    McCullough, K.C.4    Ruggli, N.5
  • 38
    • 84961134192 scopus 로고    scopus 로고
    • Hemagglutinin of influenza A virus antagonizes type I interferon (IFN) responses by inducing degradation of type I IFN receptor 1
    • Xia C, Vijayan M, Pritzl CJ, Fuchs SY, McDermott AB, Hahm B. 2016. Hemagglutinin of influenza A virus antagonizes type I interferon (IFN) responses by inducing degradation of type I IFN receptor 1. J Virol 90: 2403-2417. http://dx.doi.org/10.1128/JVI.02749-15
    • (2016) J Virol , vol.90 , pp. 2403-2417
    • Xia, C.1    Vijayan, M.2    Pritzl, C.J.3    Fuchs, S.Y.4    McDermott, A.B.5    Hahm, B.6
  • 39
    • 53349178089 scopus 로고    scopus 로고
    • STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling
    • Ishikawa H, Barber GN. 2008. STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling. Nature 455:674-678. http://dx.doi.org/10.1038/nature07317
    • (2008) Nature , vol.455 , pp. 674-678
    • Ishikawa, H.1    Barber, G.N.2
  • 40
    • 84857937262 scopus 로고    scopus 로고
    • STING specifies IRF3 phosphorylation by TBK1 in the cytosolic DNA signaling pathway
    • Tanaka Y, Chen ZJ. 2012. STING specifies IRF3 phosphorylation by TBK1 in the cytosolic DNA signaling pathway. Sci Signal 5:ra20. http://dx.doi.org/10.1126/scisignal.2002521
    • (2012) Sci Signal , vol.5
    • Tanaka, Y.1    Chen, Z.J.2
  • 41
    • 77950539082 scopus 로고    scopus 로고
    • Association of RIG-I with innate immunity of ducks to influenza
    • Barber MR, Aldridge JR, Jr, Webster RG, Magor KE. 2010. Association of RIG-I with innate immunity of ducks to influenza. Proc Natl Acad Sci U S A 107:5913-5918. http://dx.doi.org/10.1073/pnas.1001755107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 5913-5918
    • Barber, M.R.1    Aldridge, J.R.2    Webster, R.G.3    Magor, K.E.4
  • 42
    • 84943566927 scopus 로고    scopus 로고
    • Chicken STING mediates activation of the IFN gene independently of the RIG-I gene
    • Cheng Y, Sun Y, Wang H, Yan Y, Ding C, Sun J. 2015. Chicken STING mediates activation of the IFN gene independently of the RIG-I gene. J Immunol 195:3922-3936. http://dx.doi.org/10.4049/jimmunol.1500638
    • (2015) J Immunol , vol.195 , pp. 3922-3936
    • Cheng, Y.1    Sun, Y.2    Wang, H.3    Yan, Y.4    Ding, C.5    Sun, J.6
  • 43
    • 84893683041 scopus 로고    scopus 로고
    • Chicken MDA5 senses short double-stranded RNA with implications for antiviral response against avian influenza viruses in chicken
    • Hayashi T, Watanabe C, Suzuki Y, Tanikawa T, Uchida Y, Saito T. 2014. Chicken MDA5 senses short double-stranded RNA with implications for antiviral response against avian influenza viruses in chicken. J Innate Immun 6:58-71. http://dx.doi.org/10.1159/000351583
    • (2014) J Innate Immun , vol.6 , pp. 58-71
    • Hayashi, T.1    Watanabe, C.2    Suzuki, Y.3    Tanikawa, T.4    Uchida, Y.5    Saito, T.6
  • 44
    • 84855480986 scopus 로고    scopus 로고
    • Highly pathogenic avian influenza virus H5N1 controls type I IFN induction in chicken macrophage HD-11 cells: a polygenic trait that involves NS1 and the polymerase complex
    • Liniger M, Moulin HR, Sakoda Y, Ruggli N, Summerfield A. 2012. Highly pathogenic avian influenza virus H5N1 controls type I IFN induction in chicken macrophage HD-11 cells: a polygenic trait that involves NS1 and the polymerase complex. Virol J 9:7. http://dx.doi.org/10.1186/1743-422X-9-7
    • (2012) Virol J , vol.9 , pp. 7
    • Liniger, M.1    Moulin, H.R.2    Sakoda, Y.3    Ruggli, N.4    Summerfield, A.5
  • 45
    • 84925410974 scopus 로고    scopus 로고
    • Mx GTPases: dynamin-like antiviral machines of innate immunity
    • Haller O, Staeheli P, Schwemmle M, Kochs G. 2015. Mx GTPases: dynamin-like antiviral machines of innate immunity. Trends Microbiol 23:154-163. http://dx.doi.org/10.1016/j.tim.2014.12.003
    • (2015) Trends Microbiol , vol.23 , pp. 154-163
    • Haller, O.1    Staeheli, P.2    Schwemmle, M.3    Kochs, G.4
  • 46
    • 84952884939 scopus 로고    scopus 로고
    • Host genetics of severe influenza: from mouse Mx1 to human IRF7
    • Ciancanelli MJ, Abel L, Zhang SY, Casanova JL. 2016. Host genetics of severe influenza: from mouse Mx1 to human IRF7. Curr Opin Immunol 38:109-120. http://dx.doi.org/10.1016/j.coi.2015.12.002
    • (2016) Curr Opin Immunol , vol.38 , pp. 109-120
    • Ciancanelli, M.J.1    Abel, L.2    Zhang, S.Y.3    Casanova, J.L.4
  • 47
    • 80755153638 scopus 로고    scopus 로고
    • Structure of myxovirus resistance protein A reveals intra-and intermolecular domain interactions required for the antiviral function
    • Gao S, von der Malsburg A, Dick A, Faelber K, Schroder GF, Haller O, Kochs G, Daumke O. 2011. Structure of myxovirus resistance protein A reveals intra-and intermolecular domain interactions required for the antiviral function. Immunity 35:514-525. http://dx.doi.org/10.1016/j.immuni.2011.07.012
    • (2011) Immunity , vol.35 , pp. 514-525
    • Gao, S.1    von der Malsburg, A.2    Dick, A.3    Faelber, K.4    Schroder, G.F.5    Haller, O.6    Kochs, G.7    Daumke, O.8
  • 48
    • 0033548268 scopus 로고    scopus 로고
    • GTP-bound human MxA protein interacts with the nucleocapsids of Thogoto virus (Orthomyxoviridae)
    • Kochs G, Haller O. 1999. GTP-bound human MxA protein interacts with the nucleocapsids of Thogoto virus (Orthomyxoviridae). J Biol Chem 274: 4370-4376. http://dx.doi.org/10.1074/jbc.274.7.4370
    • (1999) J Biol Chem , vol.274 , pp. 4370-4376
    • Kochs, G.1    Haller, O.2
  • 49
    • 84949666240 scopus 로고    scopus 로고
    • Oligomerization and GTP-binding requirements of MxA for viral target recognition and antiviral activity against influenza A virus
    • Nigg PE, Pavlovic J. 2015. Oligomerization and GTP-binding requirements of MxA for viral target recognition and antiviral activity against influenza A virus. J Biol Chem 290:29893-29906. http://dx.doi.org/10.1074/jbc. M115.681494
    • (2015) J Biol Chem , vol.290 , pp. 29893-29906
    • Nigg, P.E.1    Pavlovic, J.2
  • 50
    • 1342285200 scopus 로고    scopus 로고
    • Nuclear MxA proteins form a complex with influenza virus NP and inhibit the transcription of the engineered influenza virus genome
    • Turan K, Mibayashi M, Sugiyama K, Saito S, Numajiri A, Nagata K. 2004. Nuclear MxA proteins form a complex with influenza virus NP and inhibit the transcription of the engineered influenza virus genome. Nucleic Acids Res 32:643-652. http://dx.doi.org/10.1093/nar/gkh192
    • (2004) Nucleic Acids Res , vol.32 , pp. 643-652
    • Turan, K.1    Mibayashi, M.2    Sugiyama, K.3    Saito, S.4    Numajiri, A.5    Nagata, K.6
  • 51
    • 84870671459 scopus 로고    scopus 로고
    • Interferon-inducible protein Mx1 inhibits influenza virus by interfering with functional viral ribonucleoprotein complex assembly
    • Verhelst J, Parthoens E, Schepens B, Fiers W, Saelens X. 2012. Interferon-inducible protein Mx1 inhibits influenza virus by interfering with functional viral ribonucleoprotein complex assembly. J Virol 86:13445-13455 http://dx.doi.org/10.1128/JVI.01682-12
    • (2012) J Virol , vol.86 , pp. 13445-13455
    • Verhelst, J.1    Parthoens, E.2    Schepens, B.3    Fiers, W.4    Saelens, X.5
  • 52
    • 80053422068 scopus 로고    scopus 로고
    • Interferon-induced antiviral protein MxA interacts with the cellular RNA helicases UAP56 and URH49
    • Wisskirchen C, Ludersdorfer TH, Muller DA, Moritz E, Pavlovic J. 2011. Interferon-induced antiviral protein MxA interacts with the cellular RNA helicases UAP56 and URH49. J Biol Chem 286:34743-34751. http://dx.doi.org/10.1074/jbc. M111.251843
    • (2011) J Biol Chem , vol.286 , pp. 34743-34751
    • Wisskirchen, C.1    Ludersdorfer, T.H.2    Muller, D.A.3    Moritz, E.4    Pavlovic, J.5
  • 53
    • 84887131870 scopus 로고    scopus 로고
    • The human interferon-induced MxA protein inhibits early stages of influenza A virus infection by retaining the incoming viral genome in the cytoplasm
    • Xiao H, Killip MJ, Staeheli P, Randall RE, Jackson D. 2013. The human interferon-induced MxA protein inhibits early stages of influenza A virus infection by retaining the incoming viral genome in the cytoplasm. J Virol 87:13053-13058. http://dx.doi.org/10.1128/JVI.02220-13
    • (2013) J Virol , vol.87 , pp. 13053-13058
    • Xiao, H.1    Killip, M.J.2    Staeheli, P.3    Randall, R.E.4    Jackson, D.5
  • 54
    • 0026729086 scopus 로고
    • Overexpression of the influenza virus polymerase can titrate out inhibition by the murine Mx1 protein
    • Huang T, Pavlovic J, Staeheli P, Krystal M. 1992. Overexpression of the influenza virus polymerase can titrate out inhibition by the murine Mx1 protein. J Virol 66:4154-4160
    • (1992) J Virol , vol.66 , pp. 4154-4160
    • Huang, T.1    Pavlovic, J.2    Staeheli, P.3    Krystal, M.4
  • 55
    • 0025331030 scopus 로고
    • Resistance to influenza virus and vesicular stomatitis virus conferred by expression of human MxA protein
    • Pavlovic J, Zurcher T, Haller O, Staeheli P. 1990. Resistance to influenza virus and vesicular stomatitis virus conferred by expression of human MxA protein. J Virol 64:3370-3375
    • (1990) J Virol , vol.64 , pp. 3370-3375
    • Pavlovic, J.1    Zurcher, T.2    Haller, O.3    Staeheli, P.4
  • 56
    • 0027372154 scopus 로고
    • Function of the mouse Mx1 protein is inhibited by overexpression of the Pb2 protein of influenza virus
    • Stranden AM, Staeheli P, Pavlovic J. 1993. Function of the mouse Mx1 protein is inhibited by overexpression of the Pb2 protein of influenza virus. Virology 197:642-651. http://dx.doi.org/10.1006/viro.1993.1639
    • (1993) Virology , vol.197 , pp. 642-651
    • Stranden, A.M.1    Staeheli, P.2    Pavlovic, J.3
  • 57
    • 41149143074 scopus 로고    scopus 로고
    • Influenza A virus strains differ in sensitivity to the antiviral action of Mx-GTPase
    • Dittmann J, Stertz S, Grimm D, Steel J, Garcia-Sastre A, Haller O, Kochs G. 2008. Influenza A virus strains differ in sensitivity to the antiviral action of Mx-GTPase. J Virol 82:3624-3631. http://dx.doi.org/10.1128/JVI.01753-07
    • (2008) J Virol , vol.82 , pp. 3624-3631
    • Dittmann, J.1    Stertz, S.2    Grimm, D.3    Steel, J.4    Garcia-Sastre, A.5    Haller, O.6    Kochs, G.7
  • 58
    • 84875985517 scopus 로고    scopus 로고
    • Pandemic influenza A viruses escape from restriction by human MxA through adaptive mutations in the nucleoprotein
    • Mänz B, Dornfeld D, Gotz V, Zell R, Zimmermann P, Haller O, Kochs G, Schwemmle M. 2013. Pandemic influenza A viruses escape from restriction by human MxA through adaptive mutations in the nucleoprotein. PLoS Pathog 9:e1003279. http://dx.doi.org/10.1371/journal.ppat.1003279
    • (2013) PLoS Pathog , vol.9
    • Mänz, B.1    Dornfeld, D.2    Gotz, V.3    Zell, R.4    Zimmermann, P.5    Haller, O.6    Kochs, G.7    Schwemmle, M.8
  • 59
    • 79961202011 scopus 로고    scopus 로고
    • The viral nucleoprotein determines Mx sensitivity of influenza A viruses
    • Zimmermann P, Manz B, Haller O, Schwemmle M, Kochs G. 2011. The viral nucleoprotein determines Mx sensitivity of influenza A viruses. J Virol 85:8133-8140. http://dx.doi.org/10.1128/JVI.00712-11
    • (2011) J Virol , vol.85 , pp. 8133-8140
    • Zimmermann, P.1    Manz, B.2    Haller, O.3    Schwemmle, M.4    Kochs, G.5


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