ЭВОЛЮЦИОННАЯ ДИНАМИКА СТРУКТУРНЫХ И ФУНКЦИОНАЛЬНЫХ ДОМЕНОВ БЕЛКА NS1 ВИРУСОВ ГРИППА А ЧЕЛОВЕКА

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Белок NS1 вируса гриппа А (ВГА) является одним из ключевых вирусных факторов, отвечающих за взаимодействие с клеткой-хозяином. NS1 противостоит системе клеточной противовирусной защиты, участвует в процессинге и экспорте клеточных мРНК, регулирует активность вирусной РНК-полимеразы и экспрессию вирусных генов, оказывает влияние на сигнальные системы клетки. Многочисленные функции NS1 осуществляются за счёт устоявшихся взаимодействий с клеточными факторами, число которых, по разным данным, превышает сотню. Примечательно, что только два сегмента генома ВГА человека - NS1 и NP - не подвергались реассортации и эволюционировали в процессе генетического дрейфа начиная с пандемии 1918 г. по настоящее время. Этот факт может свидетельствовать о важности NS1 и его многочисленных взаимодействий с клеточными факторами в межвидовой адаптации вируса. В обзоре представлены данные об эволюции белка NS1 ВГА человека и проведён анализ аминокислотных замен, произошедших в основных структурных и функциональных доменах белка NS1 в процессе эволюции.

Об авторах

А. В. Васин

ФГБУ «НИИ гриппа» Минздрава России; ФГАО УВО «Санкт-Петербургский политехнический университет Петра Великого»

Автор, ответственный за переписку.
Email: influenza.spb@gmail.com
Россия

А. В. Петрова-Бродская

ФГБУ «НИИ гриппа» Минздрава России; ФГАО УВО «Санкт-Петербургский политехнический университет Петра Великого»

Email: noemail@neicon.ru
Россия

М. А. Плотникова

ФГБУ «НИИ гриппа» Минздрава России

Email: noemail@neicon.ru
Россия

В. Б. Цветков

ФГБУ «НИИ гриппа» Минздрава России; ФГБУН «Институт нефтехимического синтеза им. А.В. Топчиева» РАН; ФГБУ «Федеральный научно-клинический центр физико-химической медицины» ФМБА

Email: noemail@neicon.ru
Россия

С. А. Клотченко

ФГБУ «НИИ гриппа» Минздрава России

Email: noemail@neicon.ru
Россия

Список литературы

  1. Webster R.G., Bean W.J., Gorman O T., Chambers T.M., Kawaoka Y. Evolution and ecology of influenza A viruses. Microbiol. 1992; (56): 152-79.
  2. Taubenberger J.K., Kash J.C. Influenza Virus Evolution, Host Adaptation, and Pandemic Formation. Cell. Host. Microbe. 2010; (7): 440-51.
  3. Noronha J M., Liu M., Squires R.B., Pickett B.E., Hale B.G., Air G.M., et al. Influenza virus sequence feature variant type analysis: evidence of a role for NS1 in influenza virus host range restriction. J. Virol. 2012; (86): 5857-66.
  4. Egorov A., Brandt S., Sereinig S., Romanova J., Ferko B., Katinger D., et al. Transfectant influenza A viruses with long deletions in the NS1 protein grow efficiently in Vero cells. J. Virol. 1998; (72): 6437-41.
  5. Hale B.G., Randall R.E., Ortin J., Jackson D. The multifunctional NS1 protein of influenza A viruses. J. Gen. Virol. 2008; (89): 2359-76.
  6. Marc D. Influenza virus non-structural protein NS1: Interferon antagonism and beyond. J. Gen. Virol. 2014; (95): 2594-611.
  7. Seo S.H., Hoffmann E., Webster R.G. Lethal H5N1 influenza viruses escape host anti-viral cytokine responses. Nat. Med. 2002; (8): 950-4.
  8. Taubenberger J.K., Morens D.M. 1918 Influenza: The mother of all pandemics. Emerg. Infect. Dis. 2006; (12): 15-22.
  9. Morens D.M., Taubenberger J.K., Harvey H.A., Memoli M.J. The 1918 influenza pandemic: lessons for 2009 and the future. Crit. Care Med. 2010; (38): e10-e20.
  10. Smith G.J.D., Bahl J., Vijaykrishna D., Zhang J., Poon L.L.M., Chen H., et al. Dating the emergence of pandemic influenza viruses. Proc. Natl. Acad. Sci. USA. 2009; (106): 11709-12.
  11. Xu J., Zhong H.A., Madrahimov A., Helikar T., Lu G. Molecular phylogeny and evolutionary dynamics of influenza A nonstructural (NS) gene. Infect. Genet. Evol. 2014; (22): 192-200.
  12. Vasin A.V, Petrova A.V., Egorov V.V, Plotnikova M.A., Klotchenko S.A., Karpenko M.N., et al. The influenza A virus NS genome segment displays lineage-specific patterns in predicted RNA secondary structure. BMC Res. Notes. 2016; (9): 279.
  13. Vincent A., Awada L., Brown I., Chen H., Claes F., Dauphin G., et al. Review of Influenza A Virus in Swine Worldwide: A Call for Increased Surveillance and Research. Zoonoses Public Health. 2014; (61): 4-17.
  14. Trifonov V., Khiabanian H., Rabadan R. Geographic dependence, surveillance, and origins of the 2009 influenza A (H1N1) virus. N. Engl. J. Med. 2009; 361: 115-9.
  15. Nakajima K., Desselberger U., Palese P. Recent human influenza A (H1N1) viruses are closely related genetically to strains isolated in 1950. Nature. 1978; 274: 334-9.
  16. Киселёв О.И. Геном пандемического вируса гриппа А/H1N1v-2009. СПб.-М.: Димитрейд График Групп; 2011
  17. Garten R.J., Davis C.T., Russell C.A., Shu B., Lindstrom S., Balish A., et al. Antigenic and genetic characteristics of swine-origin 2009 A(H1N1) influenza viruses circulating in humans. Science. 2009; 325: 197-201.
  18. Komadina N., McVernon J., Hall R., Leder K. A Historical Perspective of Influenza A(H1N2) Virus. Emerg. Infect. Dis. 2014; (20): 6-12.
  19. Gaydos J.C., Top F.H., Hodder R.A., Russell P.K. Swine influenza A outbreak, Fort Dix, New Jersey, 1976. Emerg. Infect. Dis. 2006; (12): 23-8.
  20. de Wit E., Munster V.J., van Riel D., Beyer W.E.P., Rimmelzwaan G.F., Kuiken T., et al. Molecular determinants of adaptation of highly pathogenic avian influenza H7N7 viruses to efficient replication in the human host. J. Virol. 2010; (84): 1597-606.
  21. Vasin A.V., Temkina O.A., Egorov V.V., Klotchenko S.A., Plotnikova M.A., Kiselev O.I. Molecular mechanisms enhancing the proteome of influenza A viruses: an overview of recently discovered proteins. Virus Res. 2014; 185: 53-63.
  22. García-Sastre A., Egorov A., Matassov D., Brandt S., Levy D.E., Durbin J.E., et al. Influenza A virus lacking the NS1 gene replicates in interferon-deficient systems. Virology. 1998; 252: 324-30.
  23. Robb N.C., Jackson D., Vreede F.T., Fodor E. Splicing of influenza A virus NS1 mRNA is independent of the viral NS1 protein. J. Gen. Virol. 2010; 91: 2331-40.
  24. Chua M.A., Schmid S., Perez J.T., Langlois R.A., and Tenoever B.R. Influenza A virus utilizes suboptimal splicing to coordinate the timing of infection. Cell Rep. 2013; (3): 23-9.
  25. Paterson D., Fodor E. Emerging Roles for the Influenza A Virus Nuclear Export Protein (NEP). PLoS Pathog. 2012; 8(12): e1003019.
  26. Shaw M.L., Stone K.L., Colangelo C.M., Gulcicek E.E., Palese P. Cellular proteins in influenza virus particles. PLoS Pathog. 2008; (4): 1-13.
  27. Hutchinson E.C., Charles P.D., Hester S.S., Thomas B., Trudgian D., Martinez-Alonso M., et al. Conserved and host-specific features of influenza virion architecture. Nat. Commun. 2014; (5): 4816.
  28. Greenspan D., Palese P., Krystal M. Two nuclear location signals in the influenza virus NS1 nonstructural protein. J. Virol. 1988; 62: 3020-6.
  29. Schneider J., Wolff T. Nuclear functions of the influenza A and B viruses NS1 proteins: Do they play a role in viral mRNA export? Vaccine. 2009; 27: 6312-6.
  30. Li Y., Yamakita Y., Krug R.M. Regulation of a nuclear export signal by an adjacent inhibitory sequence: the effector domain of the influenza virus NS1 protein. Proc. Natl. Acad. Sci. USA. 1998; 95: 4864-9.
  31. Boulo S., Akarsu H., Ruigrok R.W.H., Baudin F. Nuclear traffic of influenza virus proteins and ribonucleoprotein complexes. Virus Res. 2007; 124: 12-21.
  32. Bornholdt Z.A., Prasad B.V.V. X-ray structure of influenza virus NS1 effector domain. Nat. Struct. Mol. Biol. 2006; (13): 559-60.
  33. Carrillo B., Choi J.-M., Bornholdt Z.A., Sankaran B., Rice A.P., Prasad B.V.V. The influenza A virus protein NS1 displays structural polymorphism. J. Virol. 2014; 88: 4113-22.
  34. Hale B.G. Conformational plasticity of the influenza A virus NS1 protein. J. Gen. Virol. 2014; 95(Pt. 10): 2099-105.
  35. Shin Y.K., Li Y., Liu Q., Anderson D.H., Babiuk L.A., Zhou Y. SH3 binding motif 1 in influenza A virus NS1 protein is essential for PI3K/Akt signaling pathway activation. J. Virol. 2007; 81: 12730-9.
  36. Li Y., Anderson D.H., Liu Q., and Zhou Y. Mechanism of influenza A virus NS1 protein interaction with the p85β, but not the p85α, subunit of phosphatidylinositol 3-kinase (PI3K) and up-regulation of PI3K activity. J. Biol. Chem. 2008; 283: 23397-409.
  37. Ehrhardt C., Ludwig S. A new player in a deadly game: influenza viruses and the PI3K/Akt signalling pathway. Cell. Microbiol. 2009; (11): 863-71.
  38. Ehrhardt C., Wolff T., Pleschka S., Planz O., Beermann W., Bode J.G., et al. Influenza A virus NS1 protein activates the PI3K/Akt pathway to mediate antiapoptotic signaling responses. J. Virol. 2007; 81: 3058-67.
  39. Jackson D., Hossain M.J., Hickman D., Perez D.R., Lamb R.A. A new influenza virus virulence determinant: the NS1 protein four C-terminal residues modulate pathogenicity. Proc. Natl. Acad. Sci. USA. 2008; 105: 4381-6.
  40. Golebiewski L., Liu H., Javier R.T., Rice A.P. The avian influenza virus NS1 ESEV PDZ binding motif associates with Dlg1 and Scribble to disrupt cellular tight junctions. J. Virol. 2011; 85: 10639-48.
  41. Bavagnoli L., Dundon W.G., Garbelli A., Zecchin B., Milani A., Parakkal G., et al. The PDZ-ligand and Src-homology type 3 domains of epidemic avian influenza virus NS1 protein modulate human Src kinase activity during viral infection. PLoS One. 2011; (6): 1-12.
  42. Peng X., Chan E.Y., Li Y., Diamond D.L., Korth M.J., Katze M.G. Virus-host interactions: from systems biology to translational research. Curr. Opin. Microbiol. 2009; (12): 432-8.
  43. Geiss G.K., Salvatore M., Tumpey T.M., Carter V.S., Wang X., Basler C.F., et al. Cellular transcriptional profiling in influenza A virus-infected lung epithelial cells: the role of the nonstructural NS1 protein in the evasion of the host innate defense and its potential contribution to pandemic influenza. Proc. Natl. Acad. Sci. USA. 2002; 99: 10736-41.
  44. Kash J.C., Tumpey T.M., Proll S.C., Carter V., Perwitasari O., Thomas M.J., et al. Genomic analysis of increased host immune and cell death responses induced by 1918 influenza virus. Nature. 2006; 443: 578-81.
  45. Плотникова М.А., Васин А.В., Клотченко С.А., Смирнова Т.Д., Даниленко Д.М., Егоров В.В. и др. Сравнение паттерна экспрессии мРНК цитокинов в эпителиальных клетках А-549, инфицированных вирусами гриппа A/H1N1pdm09, A/H3N2 и A/H5N1. Цитокины и воспаление. 2013; (12): 57-65
  46. Mi H., Huang X., Muruganujan A., Tang H., Mills C., Kang D., et al. PANTHER version 11: Expanded annotation data from Gene Ontology and Reactome pathways, and data analysis tool enhancements. Nucleic Acids Res. 2017; 45: D183-9.
  47. Fabregat A., Sidiropoulos K., Garapati P., Gillespie M., Hausmann K., Haw R., et al. The reactome pathway knowledgebase. Nucleic Acids Res. 2016; 44: D481-7.
  48. Davidson S., McCabe T.M., Crotta S., Gad H.H., Hessel E.M., Beinke S., et al. IFNλ is a potent anti-influenza therapeutic without the inflammatory side effects of IFNα treatment. EMBO Mol. Med. 2016; (8): 1099-112.
  49. Shimizu K., Iguchi A., Gomyou R., Ono Y. Influenza virus inhibits cleavage of the HSP70 pre-mRNAs at the polyadenylation site. Virology. 1999; 88: 14078-9.
  50. Cao M., Wei C., Zhao L., Wang J., Jia Q., Wang X., et al. DnaJA1/Hsp40 Is Co-Opted by Influenza A Virus To Enhance Its Viral RNA Polymerase Activity. J. Virol. 2014; 254: 213-9.
  51. Li T., Li X., Zhu W.F., Wang H.Y., Mei L., Wu S.Q., et al. NF90 is a novel influenza A virus NS1-interacting protein that antagonizes the inhibitory role of NS1 on PKR phosphorylation. FEBS Lett. 2016; 590(16): 2797-810.
  52. Downey J., Pernet E., Coulombe F., Allard B., Meunier I., Jaworska J., et al. RIPK3 interacts with MAVS to regulate type I IFN-mediated immunity to Influenza A virus infection. PLoS Pathog. 2017; (13): e1006326.
  53. Thulasi Raman S.N., Zhou Y. Networks of Host Factors that Interact with NS1 Protein of Influenza A Virus. Front. Microbiol. 2016; (7): 654.
  54. Zhang C., Yang Y., Zhou X., Yang Z., Liu X., Cao Z., et al. The NS1 protein of influenza a virus interacts with heat shock protein Hsp90 in human alveolar basal epithelial cells: Implication for virus-induced apoptosis. Virol. J. 2011; (8): 181.
  55. Wang L., Fu B., Li W., Patil G., Liu L., Dorf M.E., et al. Comparative influenza protein interactomes identify the role of plakophilin 2 in virus restriction. Nat. Commun. 2017; (8): 13876.
  56. de Chassey B., Aublin-Gex A., Ruggieri A., Meyniel-Schicklin L., Pradezynski F., Davoust N., et al. The Interactomes of Influenza Virus NS1 and NS2 Proteins Identify New Host Factors and Provide Insights for ADAR1 Playing a Supportive Role in Virus Replication. PLoS Pathog. 2013. (9): e1003440.
  57. Shapira S.D., Gat-Viks I., Shum B.O.V., Dricot A., de Grace M.M., et al. A Physical and Regulatory Map of Host-Influenza Interactions Reveals Pathways in H1N1 Infection. Cell. 2009; 139: 1255-67.
  58. Ayllon J., García-Sastre A. The ns1 protein: A multitasking virulence factor. Curr. Top. Microbiol. Immunol. 2015; 386: 73-107.
  59. Calderone A., Licata L., Cesareni G. VirusMentha: A new resource for virus-host protein interactions. Nucleic Acids Res. 2015; 43: D588-92.
  60. Marc D., Barbachou S., Soubieux D. The RNA-binding domain of influenzavirus non-structural protein-1 cooperatively binds to virus-specific RNA sequences in a structure-dependent manner. Nucleic Acids Res. 2013; 41: 434-49.
  61. Cheng A., Wong S.M., Yuan Y.A. Structural basis for dsRNA recognition by NS1 protein of influenza A virus. Cell Res. 2009; 19: 187-95.
  62. Yin C., Khan J.A., Swapna G.V.T., Ertekin A., Krug R.M., Tong L., et al. Conserved surface features form the double-stranded RNA binding site of non-structural protein 1 (NS1) from influenza A and B viruses. J. Biol. Chem. 2007; 282: 20584-92.
  63. Melén K., Kinnunen L., Fagerlund R., Ikonen N., Twu K.Y., Krug R.M., et al. Nuclear and nucleolar targeting of influenza A virus NS1 protein: striking differences between different virus subtypes. J. Virol. 2007; 81: 5995-6006.
  64. Liu J., Lynch P.A., Chien C.Y., Montelione G.T., Krug R.M., Berman H.M. Crystal structure of the unique RNA-binding domain of the influenza virus NS1 protein. Nat. Struct. Biol. 1997; (4): 896-9.
  65. Wang W., Riedel K., Lynch P., Chien C.Y., Montelione G.T., Krug R.M. RNA binding by the novel helical domain of the influenza virus NS1 protein requires its dimer structure and a small number of specific basic amino acids. RNA. 1999; 5: 195-205.
  66. Long J.X., Peng D.X., Liu Y.L., Wu Y.T., Liu X.F. Virulence of H5N1 avian influenza virus enhanced by a 15-nucleotide deletion in the viral nonstructural gene. Virus Genes. 2008; 36: 471-8.
  67. Zhou H., Zhu J., Tu J., Zou W., Hu Y., Yu Z., et al. Effect on virulence and pathogenicity of H5N1 influenza A virus through truncations of NS1 eIF4GI binding domain. J. Infect. Dis. 2010; 202: 1338-46.
  68. Gallacher M., Brown S.G., Hale B.G., Fearns R., Olver R E., Randall R.E., et al. Cation currents in human airway epithelial cells induced by infection with influenza A virus. J. Physiol. 2009; 587: 3159-73.
  69. Hale B.G., Jackson D., Chen Y.-H., Lamb R.A., Randall R.E. Influenza A virus NS1 protein binds p85beta and activates phosphatidylinositol-3-kinase signaling. Proc. Natl. Acad. Sci. USA. 2006; 103:14194-9.
  70. Hale B.G., Kerry P.S., Jackson D., Precious B.L., Gray A., Killip M.J., et al. E., and Russell R.J. Structural insights into phosphoinositide 3-kinase activation by the influenza A virus NS1 protein. Proc. Natl. Acad. Sci. USA. 2010; 107: 1954-9.
  71. Gack M.U., Albrecht R.A., Urano T., Inn K.-S., Huang I.-C., Carnero E., et al. Influenza A virus NS1 targets the ubiquitin ligase TRIM25 to evade recognition by the host viral RNA sensor RIG-I. Cell Host Microbe. 2009; (5): 439-49.
  72. Spesock A., Malur M., Hossain M.J., Chen L.-M., Njaa B.L., Davis C.T., et al. The virulence of 1997 H5N1 influenza viruses in the mouse model is increased by correcting a defect in their NS1 proteins. J. Virol. 2011; 85: 7048-58.
  73. Kuo R.-L., Krug R.M. Influenza a virus polymerase is an integral component of the CPSF30-NS1A protein complex in infected cells. J. Virol. 2009; 83: 1611-6.
  74. Kochs G., García-Sastre A., Martínez-Sobrido L. Multiple anti-interferon actions of the influenza A virus NS1 protein. J. Virol. 2007; 81: 7011-21.
  75. Das K., Ma L.-C., Xiao R., Radvansky B., Aramini J., Zhao L., et al. Structural basis for suppression of a host antiviral response by influenza A virus. Proc. Natl. Acad. Sci. USA. 2008; 105: 13093-8.
  76. Hale B.G., Steel J., Medina R.A., Manicassamy B., Ye J., Hickman D., et al. Inefficient control of host gene expression by the 2009 pandemic H1N1 influenza A virus NS1 protein. J. Virol. 2010; 84: 6909-22.
  77. Noah D.L., Twu K.Y., Krug R.M. Cellular antiviral responses against influenza A virus are countered at the posttranscriptional level by the viral NS1A protein via its binding to a cellular proteinrequired for the 3’ end processing of cellular pre-mRNAS. Virology. 2003; 307: 386-95.
  78. Twu K.Y., Kuo R.-L., Marklund J., Krug R.M. The H5N1 influenza virus NS genes selected after 1998 enhance virus replication in mammalian cells. J. Virol. 2007; 81: 8112-21.
  79. Min J.-Y., Li S., Sen G.C., Krug R.M. A site on the influenza A virus NS1 protein mediates both inhibition of PKR activation and temporal regulation of viral RNA synthesis. Virology. 2007; 363: 236-43.
  80. Narasaraju T., Sim M.K., Ng H.H., Phoon M.C., Shanker N., Lal S.K., et al. Adaptation of human influenza H3N2 virus in a mouse pneumonitis model: insights into viral virulence, tissue tropism and host pathogenesis. Microbes Infect. 2009; (11): 2-11.
  81. Hale B.G., Barclay W.S., Randall R.E., Russell R.J. Structure of an avian influenza A virus NS1 protein effector domain. Virology. 2008; 378: 1-5.
  82. Imai H., Shinya K., Takano R., Kiso M., Muramoto Y., Sakabe S., et al. The HA and NS genes of human H5N1 influenza A virus contribute to high virulence in ferrets. PLoS Pathog. 2010; (6): e1001106.
  83. Heikkinen L.S., Kazlauskas A., Melén K., Wagner R., Ziegler T., Julkunen I., et al. Avian and 1918 Spanish influenza a virus NS1 proteins bind to Crk/CrkL Src homology 3 domains to activate host cell signaling. J. Biol. Chem. 2008; 283: 5719-27.
  84. Hale B.G., Knebel A., Botting C.H., Galloway C.S., Precious B.L., Jackson D., et al. CDK/ERK-mediated phosphorylation of the human influenza A virus NS1 protein at threonine-215. Virology. 2009; 383: 6-11.
  85. Li Y., Chen Z.Y., Wang W., Baker C.C., Krug R.M. The 3’-end-processing factor CPSF is required for the splicing of single-intron pre-mRNAs in vivo. RNA. 2001; (7): 920-31.
  86. Chen Z., Li Y., Krug R.M. Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3’-end processing machinery. EMBO J. 1999; (18): 2273-83.
  87. Zielecki F., Semmler I., Kalthoff D., Voss D., Mauel S., Gruber A.D., et al. Virulence determinants of avian H5N1 influenza A virus in mammalian and avian hosts: role of the C-terminal ESEV motif in the viral NS1 protein. J. Virol. 2010; (84): 10708-18.
  88. Soubies S.M., Volmer C., Croville G., Loupias J., Peralta B., Costes P., et al. Species-specific contribution of the four C-terminal amino acids of influenza A virus NS1 protein to virulence. J. Virol. 2010; (84): 6733-47.
  89. Liu H., Golebiewski L., Dow E.C., Krug R.M., Javier R.T., Rice A.P. The ESEV PDZ-binding motif of the avian influenza A virus NS1 protein protects infected cells from apoptosis by directly targeting Scribble. J. Virol. 2010; 84: 11164-74.
  90. Obenauer J.C., Denson J., Mehta P.K., Su X., Mukatira S., Finkelstein D.B., et al. Large-scale sequence analysis of avian influenza isolates. Science. 2006; 311: 1576-80.
  91. Engel D.A. The influenza virus NS1 protein as a therapeutic target. Antiviral Res. 2013; 99: 409-16.
  92. Chien C., Xu Y., Xiao R., Aramini J.M., Sahasrabudhe P.V, Krug R.M., et al. Biophysical characterization of the complex between double-stranded RNA and the N-terminal domain of the NS1 protein from influenza A virus: evidence for a novel RNA-binding mode. Biochemistry. 2004; 43: 1950-62.
  93. Jiao P., Tian G., Li Y., Deng G., Jiang Y., Liu C., et al. A single-amino-acid substitution in the NS1 protein changes the pathogenicity of H5N1 avian influenza viruses in mice. J. Virol. 2008; 82: 1146-54.
  94. Aragón T., de la Luna S., Novoa I., Carrasco L., Ortín J., Nieto A. Eukaryotic translation initiation factor 4GI is a cellular target for NS1 protein, a translational activator of influenza virus. Mol. Cell. Biol. 2000; (20): 6259-68.
  95. Plant E.P., Ilyushina N.A., Sheikh F., Donnelly R.P., Ye Z. Influenza Virus NS1 Protein Mutations at Position 171 Impact Innate Interferon Responses by Respiratory Epithelial Cells. Virus Res. 2017; 240: 81-6.
  96. Han X., Li Z., Chen H., Wang H., Mei L., Wu S., et al. Influenza virus A/Beijing/501/2009(H1N1) NS1 interacts with β-tubulin and induces disruption of the microtubule network and apoptosis on A549 cells. PLoS One. 2012; (7): e48340.
  97. Murayama R., Harada Y., Shibata T., Kuroda K., Hayakawa S., Shimizu K., et al. Influenza A virus non-structural protein 1 (NS1) interacts with cellular multifunctional protein nucleolin during infection. Biochem. Biophys. Res. Commun. 2007; 362: 880-5.
  98. Melén K., Tynell J., Fagerlund R., Roussel P., Hernandez-Verdun D., Julkunen I. Influenza A H3N2 subtype virus NS1 protein targets into the nucleus and binds primarily via its C-terminal NLS2/NoLS to nucleolin and fibrillarin. Virol. J. 2012; (9): 167.
  99. Kumar M., Liu H., Rice A.P., Nourry C., Grant S., Borg J., et al. Regulation of Interferon-β by MAGI-1 and Its Interaction with Influenza A Virus NS1 Protein with ESEV PBM. PLoS One. 2012; (7): e41251.
  100. Yu J., Li X., Wang Y., Li B., Li H., Li Y., et al. PDlim2 selectively interacts with the PDZ binding motif of highly pathogenic avian H5N1 influenza a virus NS1. PLoS One. 2011; (6): e19511.
  101. Zhao L., Xu L., Zhou X., Zhu Q., Yang Z., Zhang C., et al. Interaction of influenza virus NS1 protein with growth arrest-specific protein 8. Virol. J. 2009; (6): 218.

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