[1] WEBSTER R G, BEAN W J, GORMAN O T, et al. Evolution and ecology of influenza A viruses[J]. Microbiol Mol Biol Rev, 1992, 56(1):152-179.
[2] HARA K, SCHMIDT F I, CROW M, et al. Amino acid residues in the N-terminal region of the PA subunit of influenza A virus RNA polymerase play a critical role in protein stability, endonuclease activity, cap binding, and virion RNA promoter binding[J]. J Virol, 2006, 80(16):7789-7798.
[3] SEYER R, HRINCIUS E R, RITZEL D, et al. Synergistic adaptive mutations in the hemagglutinin and polymerase acidic protein lead to increased virulence of pandemic 2009 H1N1 influenza A virus in mice[J]. J Infect Dis, 2012, 205(2):262-271.
[4] SUN Y P, XU Q, SHEN Y, et al. Naturally occurring mutations in the PA gene are key contributors to increased virulence of pandemic H1N1/09 influenza virus in mice[J]. J Virol, 2014, 88(8):4600-4604.
[5] HULSE-POST D J, FRANKS J, BOYD K, et al. Molecular changes in the polymerase genes (PA and PB1) associated with high pathogenicity of H5N1 influenza virus in mallard ducks[J]. J Virol, 2007, 81(16):8515-8124.
[6] SONG J S, FENG H P, XU J, et al. The PA protein directly contributes to the virulence of H5N1 avian influenza viruses in domestic ducks[J]. J Virol, 2011, 85(5):2180-2188.
[7] DESMET E A, BUSSEY K A, STONE R, et al. Identification of the N-terminal domain of the influenza virus PA responsible for the suppression of host protein synthesis[J]. J Virol, 2013, 87(6):3108-3118.
[8] LLOMPART C M, NIETO A, RODRIGUEZ-FRANDSEN A. Specific residues of PB2 and PA influenza virus polymerase subunits confer the ability for RNA polymerase Ⅱ degradation and virus pathogenicity in mice[J]. J Virol, 2014, 88(6):3455-3463.
[9] HALE B G, JACKSON D, CHEN Y H, et al. Influenza A virus NS1 protein binds p85β and activates phosphatidylinositol-3-kinase signaling[J]. Proc Natl Acad Sci U S A, 2006, 103(38):14194-14199.
[10] GACK M U, ALBRECHT R A, URANO T, et al. Influenza A virus NS1 targets the ubiquitin ligase TRIM25 to evade recognition by the host viral RNA sensor RIG-I[J]. Cell Host Microbe, 2009, 5(5):439-449.
[11] GAO S J, WU J X, LIU R Y, et al. Interaction of NS2 with AIMP2 facilitates the switch from ubiquitination to sumoylation of M1 in influenza A virus-infected cells[J]. J Virol, 2015, 89(1):300-311.
[12] HSU W B, SHIH J L, SHIH J R, et al. Cellular protein HAX1 interacts with the influenza A virus PA polymerase subunit and impedes its nuclear translocation[J]. J Virol, 2013, 87(1):110-123.
[13] HUARTE M, SANZ-EZQUERRO J J, RONCAL F, et al. PA subunit from influenza virus polymerase complex interacts with a cellular protein with homology to a family of transcriptional activators[J]. J Virol, 2001, 75(18):8597-8604.
[14] RODRIGUEZ A, PÉREZ-GONZÉLEZ A, NIETO A. Cellular human CLE/c14orf166 protein interacts with influenza virus polymerase and is required for viral replication[J]. J Virol, 2011, 85(22):12062-12066.
[15] KAWAGUCHI A, NAGATA K. De novo replication of the influenza virus RNA genome is regulated by DNA replicative helicase, MCM[J]. EMBO J, 2007, 26(21):4566-4575.
[16] DENG T, ENGELHARDT O G, THOMAS B, et al. Role of ran binding protein 5 in nuclear import and assembly of the influenza virus RNA polymerase complex[J]. J Virol, 2006, 80(24):11911-11919.
[17] BRADEL-TRETHEWAY B G, MATTIACIO J L, KRASNOSELSKY A, et al. Comprehensive proteomic analysis of influenza virus polymerase complex reveals a novel association with mitochondrial proteins and RNA polymerase accessory factors[J]. J Virol, 2011, 85(17):8569-8581.
[18] MAYER D, MOLAWI K, MARTINEZ-SOBRIDO L, et al. Identification of cellular interaction partners of the influenza virus ribonucleoprotein complex and polymerase complex using proteomic-based approaches[J]. J Proteome Res, 2007, 6(2):672-682.
[19] LI W Z, CHEN H J, SUTTON T, et al. Interactions between the influenza A virus RNA polymerase components and retinoic acid-inducible gene I[J]. J Virol, 2014, 88(18):10432-10447.
[20] HU J, ZHAO K, LIU X, et al. Two highly pathogenic avian influenza H5N1 viruses of clade 2. 3. 2. 1 with similar genetic background but with different pathogenicity in mice and ducks[J]. Transbound Emerg Dis, 2013, 60(2):127-139.
[21] GAO Z, HU J, LIANG Y Y, et al. Generation and comprehensive analysis of host cell interactome of the PA Protein of the highly pathogenic H5N1 avian influenza virus in mammalian cells[J]. Front Microbiol, 2017, 8:739.
[22] LAMKANFI M, DIXIT V M. Manipulation of host cell death pathways during microbial infections[J]. Cell Host Microbe, 2010, 8(1):44-54.
[23] SAKABE S, OZAWA M, TAKANO R, et al. Mutations in PA, NP, and HA of a pandemic (H1N1) 2009 influenza virus contribute to its adaptation to mice[J]. Virus Res, 2011, 158(1-2):124-129.
[24] HUANG C H, CHEN C J, YEN C T, et al. Caspase-1 deficient mice are more susceptible to influenza A virus infection with PA variation[J]. J Infect Dis, 2013, 208(11):1898-1905.
[25] HU J, MO Y Q, WANG X Q, et al. PA-X decreases the pathogenicity of highly pathogenic H5N1 influenza A virus in avian species by inhibiting virus replication and host response[J]. J Virol, 2015, 89(8):4126-4142.
[26] BERRI F, LÊ V B, JANDROT-PERRUS M, et al. Switch from protective to adverse inflammation during influenza:Viral determinants and hemostasis are caught as culprits[J]. Cell Mol Life Sci, 2014, 71(5):885-898.
[27] GAUR P, MUNJAL A, LAL S K. Influenza virus and cell signaling pathways[J]. Med Sci Monit, 2011, 17(6):RA148-RA154.
[28] EHRHARDT C, MARJUKI H, WOLFF T, et al. Bivalent role of the phosphatidylinositol-3-kinase (PI3K) during influenza virus infection and host cell defence[J]. Cell Microbiol, 2006, 8(8):1336-1348.
[29] LEE C J, LIAO C L, LIN Y L. Flavivirus activates phosphatidylinositol 3-kinase signaling to block caspase-dependent apoptotic cell death at the early stage of virus infection[J]. J Virol, 2005, 79(13):8388-8399.
[30] ABBAS W, KUMAR A, HERBEIN G. The eEF1A proteins:at the crossroads of oncogenesis, apoptosis, and viral infections[J]. Front Oncol, 2015, 5:75.
[31] BLANCH A, ROBINSON F, WATSON I R, et al. Eukaryotic translation elongation factor 1-alpha 1 inhibits p53 and p73 dependent apoptosis and chemotherapy sensitivity[J]. PLoS One, 2013, 8(6):e66436.
[32] MUÑOZ-FONTELA C, PAZOS M, DELGADO I, et al. p53 serves as a host antiviral factor that enhances innate and adaptive immune responses to influenza A virus[J]. J Immunol, 2011, 187(12):6428-6236. |