Page 42 - Avian Virology: Current Research and Future Trends
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Avian Influenza Virus | 35
Neri, L.M., Borgatti, P., Capitani, S., and Martelli, A.M. (2002). The nuclear Oishi, K., Yamayoshi, S., and Kawaoka, Y. (2015). Mapping of a region of the
phosphoinositide 3-kinase/AKT pathway: a new second messenger PA-X protein of influenza A virus that is important for its shutoff activity.
system. Biochim. Biophys. Acta 1584, 73–80. J. Virol. 89, 8661–8665. https://doi.org/10.1128/JVI.01132-15
Neumann, G., Castrucci, M.R., and Kawaoka, Y. (1997). Nuclear import and Okabe, N., Hashimoto, G., Abo, T., Wright, P.F., and Karzon, D.T. (1983).
export of influenza virus nucleoprotein. J. Virol. 71, 9690–9700. Characterization of the human peripheral blood effector cells mediating
Neumann, G., Watanabe, T., Ito, H., Watanabe, S., Goto, H., Gao, P., Hughes, antibody-dependent cell-mediated cytotoxicity against respiratory
M., Perez, D.R., Donis, R., Hoffmann, E., et al. (1999). Generation of syncytial virus. Clin. Immunol. Immunopathol. 27, 200–209.
influenza A viruses entirely from cloned cDNAs. Proc. Natl. Acad. Sci. O’Neill, R.E., and Palese, P. (1995). NPI-1, the human homolog of SRP-1,
U.S.A. 96, 9345–9350. interacts with influenza virus nucleoprotein. Virology 206, 116–125.
Neumann, G., Hughes, M.T., and Kawaoka, Y. (2000). Influenza A virus O’Neill, R.E., Jaskunas, R., Blobel, G., Palese, P., and Moroianu, J. (1995).
NS2 protein mediates vRNP nuclear export through NES-independent Nuclear import of influenza virus RNA can be mediated by viral
interaction with hCRM1. EMBO J. 19, 6751–6758. https://doi. nucleoprotein and transport factors required for protein import. J. Biol.
org/10.1093/emboj/19.24.6751 Chem. 270, 22701–22704.
Newcomb, L.L., Kuo, R.L., Ye, Q., Jiang, Y., Tao, Y.J., and Krug, R.M. (2009). O’Neill, R.E., Talon, J., and Palese, P. (1998). The influenza virus NEP (NS2
Interaction of the influenza a virus nucleocapsid protein with the viral protein) mediates the nuclear export of viral ribonucleoproteins. EMBO
RNA polymerase potentiates unprimed viral RNA replication. J. Virol. J. 17, 288–296. https://doi.org/10.1093/emboj/17.1.288
83, 29–36. https://doi.org/10.1128/JVI.02293-07 Ortega, J., Martín-Benito, J., Zürcher, T., Valpuesta, J.M., Carrascosa, J.L., and
Ng, A.K., Chan, W.H., Choi, S.T., Lam, M.K., Lau, K.F., Chan, P.K., Au, Ortín, J. (2000). Ultrastructural and functional analyses of recombinant
S.W., Fodor, E., and Shaw, P.C. (2012). Influenza polymerase activity influenza virus ribonucleoproteins suggest dimerization of nucleoprotein
correlates with the strength of interaction between nucleoprotein and during virus amplification. J. Virol. 74, 156–163.
PB2 through the host-specific residue K/E627. PLOS ONE 7, e36415. Owen, R.E., Yamada, E., Thompson, C.I., Phillipson, L.J., Thompson, C.,
https://doi.org/10.1371/journal.pone.0036415 Taylor, E., Zambon, M., Osborn, H.M., Barclay, W.S., and Borrow, P.
Nieto, A., de la Luna, S., Bárcena, J., Portela, A., Valcárcel, J., Melero, J.A., (2007). Alterations in receptor binding properties of recent human
and Ortín, J. (1992). Nuclear transport of influenza virus polymerase PA influenza H3N2 viruses are associated with reduced natural killer cell
protein. Virus Res. 24, 65–75. lysis of infected cells. J. Virol. 81, 11170–11178.
Nieto, A., de la Luna, S., Bárcena, J., Portela, A., and Ortín, J. (1994). Ozawa, M., Maeda, J., Iwatsuki-Horimoto, K., Watanabe, S., Goto,
Complex structure of the nuclear translocation signal of influenza H., Horimoto, T., and Kawaoka, Y. (2009). Nucleotide sequence
virus polymerase PA subunit. J. Gen. Virol. 75, 29–36. https://doi. requirements at the 5′ end of the influenza A virus M RNA segment
org/10.1099/0022-1317-75-1-29 for efficient virus replication. J. Virol. 83, 3384–3388. https://doi.
Nimmerjahn, F., Dudziak, D., Dirmeier, U., Hobom, G., Riedel, A., Schlee, org/10.1128/JVI.02513-08
M., Staudt, L.M., Rosenwald, A., Behrends, U., Bornkamm, G.W., et al. Pahl, H.L., and Baeuerle, P.A. (1995). Expression of influenza virus
(2004). Active NF-kappaB signalling is a prerequisite for influenza virus hemagglutinin activates transcription factor NF-kappa B. J. Virol. 69,
infection. J. Gen. Virol. 85, 2347–2356. 1480–1484.
Noah, D.L., Twu, K.Y., and Krug, R.M. (2003). Cellular antiviral responses Palese, P. (1977). The genes of influenza virus. Cell 10, 1–10.
against influenza A virus are countered at the posttranscriptional level by Palese, P., Tobita, K., Ueda, M., and Compans, R.W. (1974). Characterization
the viral NS1A protein via its binding to a cellular protein required for of temperature sensitive influenza virus mutants defective in
the 3’ end processing of cellular pre-mRNAS. Virology 307, 386–395. neuraminidase. Virology 61, 397–410.
Noda, T. (2011). Native morphology of influenza virions. Front. Microbiol. Palese, P., Ritchey, M.B., and Schulman, J.L. (1977). Mapping of the
2, 269. https://doi.org/10.3389/fmicb.2011.00269 influenza virus genome. II. Identification of the P1, P2, and P3 genes.
Noda, T., and Kawaoka, Y. (2010). Structure of influenza virus Virology 76, 114–121.
ribonucleoprotein complexes and their packaging into virions. Rev. Med. Pantin-Jackwood, M.J., and Swayne, D.E. (2009). Pathogenesis and
Virol. 20, 380–391. https://doi.org/10.1002/rmv.666 pathobiology of avian influenza virus infection in birds. Rev. Sci. Tech.
Noda, T., and Kawaoka, Y. (2012). Packaging of influenza virus genome: 28, 113–136.
robustness of selection. Proc. Natl. Acad. Sci. U.S.A. 109, 8797–8798. Pantin-Jackwood, M.J., Costa-Hurtado, M., Bertran, K., DeJesus, E., Smith,
https://doi.org/10.1073/pnas.1206736109 D., and Swayne, D.E. (2017). Infectivity, transmission and pathogenicity
Noda, T., Murakami, S., Nakatsu, S., Imai, H., Muramoto, Y., Shindo, K., of H5 highly pathogenic avian influenza clade 2.3.4.4 (H5N8 and H5N2)
Sagara, H., and Kawaoka, Y. (2018). Importance of the 1+7 configuration United States index viruses in Pekin ducks and Chinese geese. Vet. Res.
of ribonucleoprotein complexes for influenza A virus genome packaging. 48, 33. https://doi.org/10.1186/s13567-017-0435-4
Nat. Commun. 9, 54. https://doi.org/10.1038/s41467-017-02517-w Park, K.S., Seo, Y.B., Lee, J.Y., Im, S.J., Seo, S.H., Song, M.S., Choi, Y.K.,
Nogales, A., Baker, S.F., and Martínez-Sobrido, L. (2015). and Sung, Y.C. (2011). Complete protection against a H5N2 avian
Replication-competent influenza A viruses expressing a red fluorescent influenza virus by a DNA vaccine expressing a fusion protein of H1N1
protein. Virology 476, 206–216. HA and M2e. Vaccine 29, 5481–5487. https://doi.org/10.1016/j.
Noton, S.L., Medcalf, E., Fisher, D., Mullin, A.E., Elton, D., and Digard, P. vaccine.2011.05.062
(2007). Identification of the domains of the influenza A virus M1 matrix Parkin, N.T., Chiu, P., and Coelingh, K. (1997). Genetically engineered live
protein required for NP binding, oligomerization and incorporation into attenuated influenza A virus vaccine candidates. J. Virol. 71, 2772–2778.
virions. J. Gen. Virol. 88, 2280–2290. Parvin, J.D., Palese, P., Honda, A., Ishihama, A., and Krystal, M. (1989).
Ohkura, T., Momose, F., Ichikawa, R., Takeuchi, K., and Morikawa, Y. Promoter analysis of influenza virus RNA polymerase. J. Virol. 63,
(2014). Influenza A virus hemagglutinin and neuraminidase mutually 5142–5152.
accelerate their apical targeting through clustering of lipid rafts. J. Virol. Paterson, D., and Fodor, E. (2012). Emerging roles for the influenza A virus
88, 10039–10055. https://doi.org/10.1128/JVI.00586-14 nuclear export protein (NEP). PLOS Pathog. 8, e1003019. https://doi.
OIE (World Organisation for Animal Health) (2015). Highly pathogenic org/10.1371/journal.ppat.1003019
avian influenza. In Terrestrial Animal Health Code (World Organization Paterson, D., te Velthuis, A.J., Vreede, F.T., and Fodor, E. (2014). Host
for Animal Health, Office International des Epizooties). Available online: restriction of influenza virus polymerase activity by PB2 627E is
http://www.oie.int/standard-setting/terrestrial-manual/access-online/ diminished on short viral templates in a nucleoprotein-independent
(accessed 18 October 2017). manner. J. Virol. 88, 339–344. https://doi.org/10.1128/JVI.02022-13
OIE (World Organisation for Animal Health ) (2017). Avian Influenza Portal. Pauli, E.K., Schmolke, M., Wolff, T., Viemann, D., Roth, J., Bode, J.G., and
Available online: http://www.oie.int/en/animal-health-in-the-world/ Ludwig, S. (2008). Influenza A virus inhibits type I IFN signaling via
web-portal-on-avian-influenza/early-detection-warning-diagnostic- NF-kappaB-dependent induction of SOCS-3 expression. PLOS Pathog.
confirmation/ (accessed 18 December 2017). 4, e1000196. https://doi.org/10.1371/journal.ppat.1000196