Page 36 - Avian Virology: Current Research and Future Trends
P. 36

Avian Influenza Virus |   29
          Dudek, S.E., Wixler, L., Nordhoff, C., Nordmann, A., Anhlan, D., Wixler,   Flory, E., Kunz, M., Scheller, C., Jassoy, C., Stauber, R., Rapp, U.R., and
            V., and Ludwig, S. (2011). The influenza virus PB1-F2 protein has   Ludwig, S. (2000). Influenza virus-induced NF-kappaB-dependent gene
            interferon antagonistic activity. Biol. Chem. 392, 1135–1144. https://  expression is mediated by overexpression of viral proteins and involves
            doi.org/10.1515/BC.2011.174                           oxidative radicals and activation of IkappaB kinase. J. Biol. Chem. 275,
          Eames, K.T., Webb, C., Thomas, K., Smith, J., Salmon, R., and Temple,   8307–8314.
            J.M. (2010). Assessing the role of contact tracing in a suspected H7N2   Fodor, E., Devenish, L., Engelhardt, O.G., Palese, P., Brownlee, G.G., and
            influenza A outbreak in humans in Wales. BMC Infect. Dis.  10, 141.   García-Sastre, A. (1999). Rescue of influenza A virus from recombinant
            https://doi.org/10.1186/1471-2334-10-141              DNA. J. Virol. 73, 9679–9682.
          Easterday, B.C., and Tumova, B. (1972). Avian influenza viruses: in avian   Foreign Agricultural Service (2017). Livestock and Poultry: World Markets
            species and the natural history of influenza. Adv. Vet. Sci. Comp. Med.   and Trade, United States Department of Agriculture, ed. Washington,
            16, 201–222.                                          DC. Available online: https://www.fas.usda.gov/.
          Easterday, B.C., Trainer, D.O., Tůmová, B., and Pereira, H.G. (1968).   Fouchier, R.A., Schneeberger, P.M., Rozendaal, F.W., Broekman, J.M.,
            Evidence of infection with influenza viruses in migratory waterfowl.   Kemink, S.A., Munster, V., Kuiken, T., Rimmelzwaan, G.F., Schutten,
            Nature 219, 523–524.                                  M., Van Doornum, G.J., et al. (2004). Avian influenza A virus (H7N7)
          Ehrhardt, C., and Ludwig, S. (2009). A new player in a deadly game:   associated with human conjunctivitis and a fatal case of acute respiratory
            influenza viruses and the PI3K/Akt signalling pathway. Cell. Microbiol.   distress syndrome. Proc. Natl. Acad. Sci. U.S.A.  101, 1356–1361.
            11, 863–871. https://doi.org/10.1111/j.1462-5822.2009.01309.x  https://doi.org/10.1073/pnas.0308352100
          Ehrhardt, C., Marjuki, H., Wolff, T., Nürnberg, B., Planz, O., Pleschka, S., and   França, M.S., and Brown, J.D. (2014). Influenza pathobiology and
            Ludwig, S. (2006). Bivalent role of the phosphatidylinositol-3-kinase   pathogenesis in avian species. Curr. Top. Microbiol. Immunol.  385,
            (PI3K)  during  influenza  virus  infection  and host  cell  defence.  Cell.   221–242. https://doi.org/10.1007/82_2014_385
            Microbiol. 8, 1336–1348.                            Freidl, G.S., Meijer, A., de Bruin, E., de Nardi, M., Munoz, O., Capua, I.,
          Eichelberger, M.C., and Wan, H. (2015). Influenza neuraminidase as a   Breed, A.C., Harris, K., Hill, A., Kosmider, R., et al. (2014). Influenza
            vaccine antigen. Curr. Top. Microbiol. Immunol. 386, 275–299. https://  at the animal-human interface: a review of the literature for virological
            doi.org/10.1007/82_2014_398                           evidence of human infection with swine or avian influenza viruses other
          Els, M.C., Air, G.M., Murti, K.G., Webster, R.G., and Laver, W.G. (1985).   than A(H5N1). Euro Surveill. 19, 20793.
            An 18-amino acid deletion in an influenza neuraminidase. Virology 142,   Frensing, T., Kupke, S.Y., Bachmann, M., Fritzsche, S., Gallo-Ramirez, L.E.,
            241–247.                                              and Reichl, U. (2016). Influenza virus intracellular replication dynamics,
          Elster, C., Fourest, E., Baudin, F., Larsen, K., Cusack, S., and Ruigrok, R.W.   release kinetics, and particle morphology during propagation in MDCK
            (1994). A small percentage of influenza virus M1 protein contains zinc   cells. Appl. Microbiol. Biotechnol.  100, 7181–7192. https://doi.
            but zinc does not influence in vitro M1-RNA interaction. J. Gen. Virol.   org/10.1007/s00253-016-7542-4
            75, 37–42. https://doi.org/10.1099/0022-1317-75-1-37  Fujii, K., Fujii, Y., Noda, T., Muramoto, Y., Watanabe, T., Takada, A., Goto,
          Elton, D., Medcalf, E., Bishop, K., and Digard, P. (1999). Oligomerization of   H., Horimoto, T., and Kawaoka, Y. (2005). Importance of both the
            the influenza virus nucleoprotein: identification of positive and negative   coding and the segment-specific noncoding regions of the influenza A
            sequence elements. Virology 260, 190–200. https://doi.org/10.1006/  virus NS segment for its efficient incorporation into virions. J. Virol. 79,
            viro.1999.9818                                        3766–3774.
          Elton, D., Simpson-Holley, M., Archer, K., Medcalf, L., Hallam, R.,   Fujimoto, Y., Tomioka, Y., Takakuwa, H., Uechi, G., Yabuta, T., Ozaki, K.,
            McCauley, J., and Digard, P. (2001). Interaction of the influenza virus   Suyama, H., Yamamoto, S., Morimatsu, M., Mai, L.Q.,  et al. (2016).
            nucleoprotein with the cellular CRM1-mediated nuclear export pathway.   Cross-protective potential of anti-nucleoprotein human monoclonal
            J. Virol. 75, 408–419. https://doi.org/10.1128/JVI.75.1.408-419.2001  antibodies against lethal influenza A virus infection. J. Gen. Virol. 97,
          Engelhardt, O.G. (2013). Many ways to make an influenza virus – review of   2104–2116. https://doi.org/10.1099/jgv.0.000518
            influenza virus reverse genetics methods. Influenza Other Respir. Viruses   Fynan, E.F., Robinson, H.L., and Webster, R.G. (1993). Use of DNA
            7, 249–256. https://doi.org/10.1111/j.1750-2659.2012.00392.x  encoding influenza hemagglutinin as an avian influenza vaccine. DNA
          FAO (Food and Agriculture Organization of the United Nations) (2005).   Cell Biol. 12, 785–789. https://doi.org/10.1089/dna.1993.12.785
            Economic and Social Impacts of Avian Influenza. Rome, Italy. Available   Gabriel, G., Dauber, B., Wolff, T., Planz, O., Klenk, H.D., and Stech, J. (2005).
            online: http://www.fao.org/avianflu/documents/Economic-and-  The viral polymerase mediates adaptation of an avian influenza virus to a
            social-impacts-of-avian-influenza-Geneva.pdf.         mammalian host. Proc. Natl. Acad. Sci. U.S.A. 102, 18590–18595.
          FAO (Food and Agriculture Organization of the United Nations) (2017).   Gabriel, G., Herwig, A., and Klenk, H.D. (2008). Interaction of polymerase
            H7N9 Situation Update, Rome, Italy. Available online:  http://www.  subunit PB2 and NP with importin alpha1 is a determinant of host range
            fao.org/ag/againfo/programmes/en/empres/h7n9/situation_update.  of influenza A virus. PLOS Pathog.  4, e11. https://doi.org/10.1371/
            html.                                                 journal.ppat.0040011
          Feng, K.H., Sun, M., Iketani, S., Holmes, E.C., and Parrish, C.R. (2016).   Gabriel, G., Klingel, K., Otte, A., Thiele, S., Hudjetz, B., Arman-Kalcek, G.,
            Comparing the functions of equine and canine influenza H3N8 virus   Sauter, M., Shmidt, T., Rother, F., Baumgarte, S., et al. (2011). Differential
            PA-X proteins: Suppression of reporter gene expression and modulation   use of importin-α isoforms governs cell tropism and host adaptation of
            of global host gene expression. Virology 496, 138–146.  influenza virus. Nat. Commun. 2, 156.
          Fernandez-Sesma, A. (2007). The influenza virus NS1 protein: inhibitor of   Gabriel, G., Czudai-Matwich, V., and Klenk, H.D. (2013). Adaptive
            innate and adaptive immunity. Infect. Disord. Drug Targets 7, 336–343.  mutations in the H5N1 polymerase complex. Virus Res. 178, 53–62.
          Fernandez-Sesma, A., Marukian, S., Ebersole, B.J., Kaminski, D., Park, M.S.,   https://doi.org/10.1016/j.virusres.2013.05.010
            Yuen,  T., Sealfon,  S.C., García-Sastre, A., and  Moran,  T.M.  (2006).   Gack, M.U., Albrecht, R.A., Urano, T., Inn, K.S., Huang, I.C., Carnero, E.,
            Influenza virus evades innate and adaptive immunity via the NS1 protein.   Farzan, M., Inoue, S., Jung, J.U., and García-Sastre, A. (2009). Influenza
            J. Virol. 80, 6295–6304.                              A virus NS1 targets the ubiquitin ligase TRIM25 to evade recognition
          Finch, C., Li, W., and Perez, D.R. (2015). Design of alternative live attenuated   by the host viral RNA sensor RIG-I. Cell Host Microbe  5, 439–449.
            influenza virus vaccines. Curr. Top. Microbiol. Immunol. 386, 205–235.   https://doi.org/10.1016/j.chom.2009.04.006
            https://doi.org/10.1007/82_2014_404                 Gale, M., and Katze, M.G. (1998). Molecular mechanisms of interferon
          Firth, A.E., Jagger, B.W., Wise, H.M., Nelson, C.C., Parsawar, K., Wills, N.M.,   resistance mediated by viral-directed inhibition of PKR, the
            Napthine, S., Taubenberger, J.K., Digard, P., and Atkins, J.F. (2012).   interferon-induced protein kinase. Pharmacol. Ther. 78, 29–46.
            Ribosomal frameshifting used in influenza A virus expression occurs   Gamblin, S.J., and Skehel, J.J. (2010). Influenza hemagglutinin and
            within the sequence UCC_UUU_CGU and is in the +1 direction. Open   neuraminidase membrane glycoproteins. J. Biol. Chem.  285, 28403–
            Biol. 2, 120109. https://doi.org/10.1098/rsob.120109  28409. https://doi.org/10.1074/jbc.R110.129809
          Flick, R., and Hobom, G. (1999). Interaction of influenza virus polymerase   Gao, H., Sun, Y., Hu, J., Qi, L., Wang, J., Xiong, X., Wang, Y., He, Q., Lin,
            with viral RNA in the ‘corkscrew’ conformation. J. Gen. Virol. 80, 2565–  Y., Kong, W., et al. (2015a). The contribution of PA-X to the virulence
            2572. https://doi.org/10.1099/0022-1317-80-10-2565
   31   32   33   34   35   36   37   38   39   40   41