Plant positive-strand (+)RNA viruses are intracellular infectious agents that reorganize subcellular membranes and rewire the cellular metabolism of host cells to achieve viral replication in elaborate replication compartments. This review describes the viral replication process based on tombusviruses, highlighting common strategies with other plant and animal viruses. Overall, the works on (TBSV) have revealed intriguing and complex functions of co-opted cellular translation factors, heat shock proteins, DEAD-box helicases, lipid transfer proteins, and membrane-deforming proteins in virus replication. The emerging picture is that many of the co-opted host factors are from highly expressed and conserved protein families. By hijacking host proteins, phospholipids, sterols, and the actin network, TBSV exerts supremacy over the host cell to support viral replication in large replication compartments. Altogether, these advances in our understanding of tombusvirus-host interactions are broadly applicable to many other viruses, which also usurp conserved host factors for various viral processes.


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Literature Cited

  1. Hyodo K, Okuno T. 1.  2015. Pathogenesis mediated by proviral host factors involved in translation and replication of plant positive-strand RNA viruses. Curr. Opin. Virol. 17:11–18 [Google Scholar]
  2. Wang A. 2.  2015. Dissecting the molecular network of virus-plant interactions: the complex roles of host factors. Annu. Rev. Phytopathol. 53:45–66 [Google Scholar]
  3. Romero-Brey I, Bartenschlager R. 3.  2014. Membranous replication factories induced by plus-strand RNA viruses. Viruses 6:2826–57 [Google Scholar]
  4. Belov GA, van Kuppeveld FJ. 4.  2012. (+)RNA viruses rewire cellular pathways to build replication organelles. Curr. Opin. Virol. 2:740–47 [Google Scholar]
  5. de Castro IF, Volonte L, Risco C. 5.  2013. Virus factories: biogenesis and structural design. Cell Microbiol 15:24–34 [Google Scholar]
  6. Nagy PD, Pogany J. 6.  2012. The dependence of viral RNA replication on co-opted host factors. Nat. Rev. Microbiol. 10:137–49 [Google Scholar]
  7. Ahlquist P. 7.  2006. Parallels among positive-strand RNA viruses, reverse-transcribing viruses and double-stranded RNA viruses. Nat. Rev. Microbiol. 4:371–82 [Google Scholar]
  8. den Boon JA, Diaz A, Ahlquist P. 8.  2010. Cytoplasmic viral replication complexes. Cell Host Microbe 8:77–85 [Google Scholar]
  9. White KA, Nagy PD. 9.  2004. Advances in the molecular biology of tombusviruses: gene expression, genome replication, and recombination. Prog. Nucleic Acid Res. Mol. Biol. 78:187–226 [Google Scholar]
  10. Russo M, Burgyan J, Martelli GP. 10.  1994. Molecular biology of Tombusviridae. Adv. Virus Res. 44:381–428 [Google Scholar]
  11. Barajas D, Jiang Y, Nagy PD. 11.  2009. A unique role for the host ESCRT proteins in replication of. Tomato bushy stunt virus. PLOS Pathog. 5:e1000705 [Google Scholar]
  12. McCartney AW, Greenwood JS, Fabian MR, White KA, Mullen RT. 12.  2005. Localization of the Tomato bushy stunt virus replication protein p33 reveals a peroxisome-to-endoplasmic reticulum sorting pathway. Plant Cell 17:3513–31 [Google Scholar]
  13. Chuang C, Barajas D, Qin J, Nagy PD. 13.  2014. Inactivation of the host lipin gene accelerates RNA virus replication through viral exploitation of the expanded endoplasmic reticulum membrane. PLOS Pathog 10:e1003944 [Google Scholar]
  14. Jonczyk M, Pathak KB, Sharma M, Nagy PD. 14.  2007. Exploiting alternative subcellular location for replication: tombusvirus replication switches to the endoplasmic reticulum in the absence of peroxisomes. Virology 362:320–30 [Google Scholar]
  15. Xu K, Huang TS, Nagy PD. 15.  2012. Authentic in vitro replication of two tombusviruses in isolated mitochondrial and endoplasmic reticulum membranes. J. Virol. 86:12779–94 [Google Scholar]
  16. Panavas T, Hawkins CM, Panaviene Z, Nagy PD. 16.  2005. The role of the p33:p33/p92 interaction domain in RNA replication and intracellular localization of p33 and p92 proteins of Cucumber necrosis tombusvirus. Virology 338:81–95 [Google Scholar]
  17. Pathak KB, Sasvari Z, Nagy PD. 17.  2008. The host Pex19p plays a role in peroxisomal localization of tombusvirus replication proteins. Virology 379:294–305 [Google Scholar]
  18. de Castro IF, Fernandez JJ, Barajas D, Nagy PD, Risco C. 18.  2016. Three dimensional imaging of the intracellular assembly of a functional viral RNA replicase complex. J. Cell Sci. In press. doi: 10.1242/jcs.181586
  19. Richardson LG, Clendening EA, Sheen H, Gidda SK, White KA, Mullen RT. 19.  2014. A unique N-terminal sequence in the Carnation Italian ringspot virus p36 replicase-associated protein interacts with the host cell ESCRT-I component Vps23. J. Virol. 88:6329–44 [Google Scholar]
  20. Rochon D, Singh B, Reade R, Theilmann J, Ghoshal K. 20.  et al. 2014. The p33 auxiliary replicase protein of Cucumber necrosis virus targets peroxisomes and infection induces de novo peroxisome formation from the endoplasmic reticulum. Virology 452–453:133–42 [Google Scholar]
  21. Pogany J, Panavas T, Serviene E, Nawaz-ul-Rehman MS, Nagy PD. 21.  2010. A high-throughput approach for studying virus replication in yeast. Curr. Protoc. Microbiol. 19:16J.1.1–15 [Google Scholar]
  22. Nawaz-ul-Rehman MS, Prasanth KR, Baker J, Nagy PD. 22.  2013. Yeast screens for host factors in positive-strand RNA virus replication based on a library of temperature-sensitive mutants. Methods 59:207–16 [Google Scholar]
  23. Nawaz-ul-Rehman MS, Martinez-Ochoa N, Pascal H, Sasvari Z, Herbst C. 23.  et al. 2012. Proteome-wide overexpression of host proteins for identification of factors affecting tombusvirus RNA replication: an inhibitory role of protein kinase C. J. Virol. 86:9384–95 [Google Scholar]
  24. Serviene E, Jiang Y, Cheng CP, Baker J, Nagy PD. 24.  2006. Screening of the yeast yTHC collection identifies essential host factors affecting tombusvirus RNA recombination. J. Virol. 80:1231–41 [Google Scholar]
  25. Jiang Y, Serviene E, Gal J, Panavas T, Nagy PD. 25.  2006. Identification of essential host factors affecting tombusvirus RNA replication based on the yeast Tet promoters Hughes Collection. J. Virol. 80:7394–404 [Google Scholar]
  26. Nagy PD, Pogany J, Lin JY. 26.  2014. How yeast can be used as a genetic platform to explore virus-host interactions: from ‘omics’ to functional studies. Trends Microbiol 22:309–16 [Google Scholar]
  27. Nagy PD. 27.  2011. The roles of host factors in tombusvirus RNA recombination. Adv. Virus Res. 81:63–84 [Google Scholar]
  28. Nagy PD, Pogany J. 28.  2010. Global genomics and proteomics approaches to identify host factors as targets to induce resistance against Tomato bushy stunt virus. Adv. Virus Res. 76:123–77 [Google Scholar]
  29. Li Z, Pogany J, Panavas T, Xu K, Esposito AM. 29.  et al. 2009. Translation elongation factor 1A is a component of the tombusvirus replicase complex and affects the stability of the p33 replication co-factor. Virology 385:245–60 [Google Scholar]
  30. Li Z, Barajas D, Panavas T, Herbst DA, Nagy PD. 30.  2008. Cdc34p ubiquitin-conjugating enzyme is a component of the tombusvirus replicase complex and ubiquitinates p33 replication protein. J. Virol. 82:6911–26 [Google Scholar]
  31. Mendu V, Chiu M, Barajas D, Li Z, Nagy PD. 31.  2010. Cpr1 cyclophilin and Ess1 parvulin prolyl isomerases interact with the tombusvirus replication protein and inhibit viral replication in yeast model host. Virology 406:342–51 [Google Scholar]
  32. Sasvari Z, Alatriste Gonzalez P, Nagy PD. 32.  2014. Tombusvirus-yeast interactions identify conserved cell-intrinsic viral restriction factors. Front. Plant Sci. 5:383 [Google Scholar]
  33. Serva S, Nagy PD. 33.  2006. Proteomics analysis of the tombusvirus replicase: Hsp70 molecular chaperone is associated with the replicase and enhances viral RNA replication. J. Virol. 80:2162–69 [Google Scholar]
  34. Panaviene Z, Panavas T, Serva S, Nagy PD. 34.  2004. Purification of the Cucumber necrosis virus replicase from yeast cells: role of coexpressed viral RNA in stimulation of replicase activity. J. Virol. 78:8254–63 [Google Scholar]
  35. Pogany J, Stork J, Li Z, Nagy PD. 35.  2008. In vitro assembly of the Tomato bushy stunt virus replicase requires the host Heat shock protein 70. PNAS 105:19956–61 [Google Scholar]
  36. Pogany J, Nagy PD. 36.  2008. Authentic replication and recombination of Tomato bushy stunt virus RNA in a cell-free extract from yeast. J. Virol. 82:5967–80 [Google Scholar]
  37. Navarro B, Russo M, Pantaleo V, Rubino L. 37.  2006. Cytological analysis of Saccharomyces cerevisiae cells supporting cymbidium ringspot virus defective interfering RNA replication. J. Gen. Virol. 87:705–14 [Google Scholar]
  38. Nagy PD. 38.  2015. Viral sensing of the subcellular environment regulates the assembly of new viral replicase complexes during the course of infection. J. Virol. 89:5196–99 [Google Scholar]
  39. Li Z, Pogany J, Tupman S, Esposito AM, Kinzy TG, Nagy PD. 39.  2010. Translation elongation factor 1A facilitates the assembly of the tombusvirus replicase and stimulates minus-strand synthesis. PLOS Pathog 6:e1001175 [Google Scholar]
  40. Wang RY, Stork J, Pogany J, Nagy PD. 40.  2009. A temperature sensitive mutant of heat shock protein 70 reveals an essential role during the early steps of tombusvirus replication. Virology 394:28–38 [Google Scholar]
  41. Wang RY, Stork J, Nagy PD. 41.  2009. A key role for heat shock protein 70 in the localization and insertion of tombusvirus replication proteins to intracellular membranes. J. Virol. 83:3276–87 [Google Scholar]
  42. Kovalev N, Barajas D, Nagy PD. 42.  2012. Similar roles for yeast Dbp2 and Arabidopsis RH20 DEAD-box RNA helicases to Ded1 helicase in tombusvirus plus-strand synthesis. Virology 432:470–84 [Google Scholar]
  43. Sasvari Z, Izotova L, Kinzy TG, Nagy PD. 43.  2011. Synergistic roles of eukaryotic translation elongation factors 1Bγ and 1A in stimulation of tombusvirus minus-strand synthesis. PLOS Pathog 7:e1002438 [Google Scholar]
  44. Prasanth KR, Barajas D, Nagy PD. 44.  2015. The proteasomal Rpn11 metalloprotease suppresses tombusvirus RNA recombination and promotes viral replication via facilitating assembly of the viral replicase complex. J. Virol. 89:2750–63 [Google Scholar]
  45. Saunier R, Esposito M, Dassa EP, Delahodde A. 45.  2013. Integrity of the Saccharomyces cerevisiae Rpn11 protein is critical for formation of proteasome storage granules (PSG) and survival in stationary phase. PLOS ONE 8:e70357 [Google Scholar]
  46. Guerrero C, Milenkovic T, Przulj N, Kaiser P, Huang L. 46.  2008. Characterization of the proteasome interaction network using a QTAX-based tag-team strategy and protein interaction network analysis. PNAS 105:13333–38 [Google Scholar]
  47. Wauer T, Komander D. 47.  2014. The JAMM in the proteasome. Nat. Struct. Mol. Biol. 21:346–48 [Google Scholar]
  48. Prasanth KR, Kovalev N, de Castro Martin IF, Baker J, Nagy PD. 48.  2016. Screening a yeast library of temperature-sensitive mutants reveals a role for actin in tombusvirus RNA recombination. Virology 489:233–42 [Google Scholar]
  49. Nawaz-ul-Rehman MS, Prasanth KR, Xu K, Sasvari Z, Kovalev N. 49.  et al. 2016. Viral replication protein inhibits cellular cofilin actin depolymerization factor to regulate the actin network and promote viral replicase assembly. PLOS Pathog 12:e1005440 [Google Scholar]
  50. Kovalev N, Martin IF, Pogany J, Barajas D, Pathak K. 50.  et al. 2016. The role of viral RNA and co-opted cellular ESCRT-I and ESCRT-III factors in formation of tombusvirus spherules harboring the tombusvirus replicase. J. Virol. 90:3611–26 [Google Scholar]
  51. Barajas D, Martin IF, Pogany J, Risco C, Nagy PD. 51.  2014. Noncanonical role for the host Vps4 AAA+ ATPase ESCRT protein in the formation of Tomato bushy stunt virus replicase. PLOS Pathog 10:e1004087 [Google Scholar]
  52. Imura Y, Molho M, Chuang C, Nagy PD. 52.  2015. Cellular Ubc2/Rad6 E2 ubiquitin-conjugating enzyme facilitates tombusvirus replication in yeast and plants. Virology 484:265–75 [Google Scholar]
  53. Barajas D, Nagy PD. 53.  2010. Ubiquitination of tombusvirus p33 replication protein plays a role in virus replication and binding to the host Vps23p ESCRT protein. Virology 397:358–68 [Google Scholar]
  54. Prescher J, Baumgartel V, Ivanchenko S, Torrano AA, Brauchle C. 54.  et al. 2015. Super-resolution imaging of ESCRT-proteins at HIV-1 assembly sites. PLOS Pathog 11:e1004677 [Google Scholar]
  55. Hurley JH. 55.  2015. ESCRTs are everywhere. EMBO J 34:2398–407 [Google Scholar]
  56. Panavas T, Serviene E, Brasher J, Nagy PD. 56.  2005. Yeast genome-wide screen reveals dissimilar sets of host genes affecting replication of RNA viruses. PNAS 102:7326–31 [Google Scholar]
  57. Lorizate M, Krausslich HG. 57.  2011. Role of lipids in virus replication. Cold Spring Harb. Perspect. Biol. 3:a004820 [Google Scholar]
  58. Sharma M, Sasvari Z, Nagy PD. 58.  2010. Inhibition of sterol biosynthesis reduces tombusvirus replication in yeast and plants. J. Virol. 84:2270–81 [Google Scholar]
  59. Barajas D, Xu K, de Castro Martin IF, Sasvari Z, Brandizzi F. 59.  et al. 2014. Co-opted oxysterol-binding ORP and VAP proteins channel sterols to RNA virus replication sites via membrane contact sites. PLOS Pathog 10:e1004388 [Google Scholar]
  60. Weber-Boyvat M, Zhong W, Yan D, Olkkonen VM. 60.  2013. Oxysterol-binding proteins: functions in cell regulation beyond lipid metabolism. Biochem. Pharmacol. 86:89–95 [Google Scholar]
  61. Xu K, Nagy PD. 61.  2015. RNA virus replication depends on enrichment of phosphatidylethanolamine at replication sites in subcellular membranes. PNAS 112:E1782–91 [Google Scholar]
  62. Pogany J, Fabian MR, White KA, Nagy PD. 62.  2003. A replication silencer element in a plus-strand RNA virus. EMBO J 22:5602–11 [Google Scholar]
  63. Pogany J, Nagy PD. 63.  2012. p33-Independent activation of a truncated p92 RNA-dependent RNA polymerase of Tomato bushy stunt virus in yeast cell-free extract. J. Virol. 86:12025–38 [Google Scholar]
  64. Panavas T, Pogany J, Nagy PD. 64.  2002. Internal initiation by the cucumber necrosis virus RNA-dependent RNA polymerase is facilitated by promoter-like sequences. Virology 296:275–87 [Google Scholar]
  65. Panavas T, Pogany J, Nagy PD. 65.  2002. Analysis of minimal promoter sequences for plus-strand synthesis by the Cucumber necrosis virus RNA-dependent RNA polymerase. Virology 296:263–74 [Google Scholar]
  66. Pogany J, Nagy PD. 66.  2015. Activation of Tomato bushy stunt virus RNA-dependent RNA polymerase by cellular heat shock protein 70 is enhanced by phospholipids in vitro. J. Virol. 89:5714–23 [Google Scholar]
  67. Chuang C, Prasanth KR, Nagy PD. 67.  2015. Coordinated function of cellular DEAD-box helicases in suppression of viral RNA recombination and maintenance of viral genome integrity. PLOS Pathog 11:e1004680 [Google Scholar]
  68. Jankowsky E. 68.  2011. RNA helicases at work: binding and rearranging. Trends Biochem. Sci. 36:19–29 [Google Scholar]
  69. Nagy PD, Simon AE. 69.  1997. New insights into the mechanisms of RNA recombination. Virology 235:1–9 [Google Scholar]
  70. Ding SW, Voinnet O. 70.  2007. Antiviral immunity directed by small RNAs. Cell 130:413–26 [Google Scholar]
  71. Kovalev N, Pogany J, Nagy PD. 71.  2014. Template role of double-stranded RNA in tombusvirus replication. J. Virol. 88:5638–51 [Google Scholar]
  72. Qu F. 72.  2010. Plant viruses versus RNAi: simple pathogens reveal complex insights on plant antimicrobial defense. Wiley Interdiscip. Rev. RNA 1:22–33 [Google Scholar]
  73. Zou J, Chang M, Nie P, Secombes CJ. 73.  2009. Origin and evolution of the RIG-I like RNA helicase gene family. BMC Evol. Biol. 9:85 [Google Scholar]
  74. Stork J, Kovalev N, Sasvari Z, Nagy PD. 74.  2011. RNA chaperone activity of the tombusviral p33 replication protein facilitates initiation of RNA synthesis by the viral RdRp in vitro. Virology 409:338–47 [Google Scholar]
  75. Kovalev N, Pogany J, Nagy PD. 75.  2012. A co-opted DEAD-box RNA helicase enhances tombusvirus plus-strand synthesis. PLOS Pathog 8:e1002537 [Google Scholar]
  76. Huang TS, Nagy PD. 76.  2011. Direct inhibition of tombusvirus plus-strand RNA synthesis by a dominant negative mutant of a host metabolic enzyme, glyceraldehyde-3-phosphate dehydrogenase, in yeast and plants. J. Virol. 85:9090–102 [Google Scholar]
  77. Wang RY, Nagy PD. 77.  2008. Tomato bushy stunt virus co-opts the RNA-binding function of a host metabolic enzyme for viral genomic RNA synthesis. Cell Host Microbe 3:178–87 [Google Scholar]
  78. Kovalev N, Nagy PD. 78.  2014. The expanding functions of cellular helicases: the tombusvirus RNA replication enhancer co-opts the plant eIF4AIII-like AtRH2 and the DDX5-like AtRH5 DEAD-box RNA helicases to promote viral asymmetric RNA replication. PLOS Pathog 10:e1004051 [Google Scholar]
  79. Panavas T, Nagy PD. 79.  2005. Mechanism of stimulation of plus-strand synthesis by an RNA replication enhancer in a tombusvirus. J. Virol. 79:9777–85 [Google Scholar]
  80. Nagy PD, Barajas D, Pogany J. 80.  2012. Host factors with regulatory roles in tombusvirus replication. Curr. Opin. Virol. 2:685–92 [Google Scholar]
  81. Miyashita S, Ishibashi K, Kishino H, Ishikawa M. 81.  2015. Viruses roll the dice: the stochastic behavior of viral genome molecules accelerates viral adaptation at the cell and tissue levels. PLOS Biol 13:e1002094 [Google Scholar]
  82. Li Z, Gonzalez PA, Sasvari Z, Kinzy TG, Nagy PD. 82.  2014. Methylation of translation elongation factor 1A by the METTL10-like See1 methyltransferase facilitates tombusvirus replication in yeast and plants. Virology 448C:43–54 [Google Scholar]
  83. Sharma M, Sasvari Z, Nagy PD. 83.  2011. Inhibition of phospholipid biosynthesis decreases the activity of the tombusvirus replicase and alters the subcellular localization of replication proteins. Virology 415:141–52 [Google Scholar]
  84. Barajas D, Kovalev N, Qin J, Nagy PD. 84.  2015. Novel mechanism of regulation of Tomato bushy stunt virus replication by cellular WW-domain proteins. J. Virol. 89:2064–79 [Google Scholar]
  85. Qin J, Barajas D, Nagy PD. 85.  2012. An inhibitory function of WW domain-containing host proteins in RNA virus replication. Virology 426:106–19 [Google Scholar]
  86. Dorobantu CM, Albulescu L, Harak C, Feng Q, van Kampen M. 86.  et al. 2015. Modulation of the host lipid landscape to promote RNA virus replication: the picornavirus encephalomyocarditis virus converges on the pathway used by hepatitis C virus. PLOS Pathog 11:e1005185 [Google Scholar]
  87. Roulin PS, Lotzerich M, Torta F, Tanner LB, van Kuppeveld FJ. 87.  et al. 2014. Rhinovirus uses a phosphatidylinositol 4-phosphate/cholesterol counter-current for the formation of replication compartments at the ER-Golgi interface. Cell Host Microbe 16:677–90 [Google Scholar]
  88. Diaz A, Zhang J, Ollwerther A, Wang X, Ahlquist P. 88.  2015. Host ESCRT proteins are required for bromovirus RNA replication compartment assembly and function. PLOS Pathog 11:e1004742 [Google Scholar]
  89. Li D, Wei T, Abbott CM, Harrich D. 89.  2013. The unexpected roles of eukaryotic translation elongation factors in RNA virus replication and pathogenesis. Microbiol. Mol. Biol. Rev. 77:253–66 [Google Scholar]
  90. Davis WG, Blackwell JL, Shi PY, Brinton MA. 90.  2007. Interaction between the cellular protein eEF1A and the 3′-terminal stem-loop of West Nile virus genomic RNA facilitates viral minus-strand RNA synthesis. J. Virol. 81:10172–87 [Google Scholar]
  91. Alam SB, Rochon D. 91.  2016. Cucumber necrosis virus recruits cellular heat shock protein 70 homologs at several stages of infection. J. Virol. 90:3302–17 [Google Scholar]
  92. Nagy PD, Wang RY, Pogany J, Hafren A, Makinen K. 92.  2011. Emerging picture of host chaperone and cyclophilin roles in RNA virus replication. Virology 411:374–82 [Google Scholar]
  93. Taguwa S, Maringer K, Li X, Bernal-Rubio D, Rauch JN. 93.  et al. 2015. Defining Hsp70 subnetworks in dengue virus replication reveals key vulnerability in flavivirus infection. Cell 163:1108–23 [Google Scholar]
  94. Hyodo K, Taniguchi T, Manabe Y, Kaido M, Mise K. 94.  et al. 2015. Phosphatidic acid produced by phospholipase D promotes RNA replication of a plant RNA virus. PLOS Pathog 11:e1004909 [Google Scholar]
  95. Xu K, Nagy PD. 95.  2014. Expanding use of multi-origin subcellular membranes by positive-strand RNA viruses during replication. Curr. Opin. Virol. 9:119–26 [Google Scholar]
  96. Ye J, Chen Z, Zhang B, Miao H, Zohaib A. 96.  et al. 2013. Heat shock protein 70 is associated with replicase complex of Japanese encephalitis virus and positively regulates viral genome replication. PLOS ONE 8:e75188 [Google Scholar]
  97. Munday DC, Wu W, Smith N, Fix J, Noton SL. 97.  et al. 2015. Interactome analysis of the human respiratory syncytial virus RNA polymerase complex identifies protein chaperones as important cofactors that promote L-protein stability and RNA synthesis. J. Virol. 89:917–30 [Google Scholar]
  98. Jiang S, Lu Y, Li K, Lin L, Zheng H. 98.  et al. 2014. Heat shock protein 70 is necessary for Rice stripe virus infection in plants. Mol. Plant Pathol. 15:907–17 [Google Scholar]
  99. Manzoor R, Kuroda K, Yoshida R, Tsuda Y, Fujikura D. 99.  et al. 2014. Heat shock protein 70 modulates influenza A virus polymerase activity. J. Biol. Chem. 289:7599–614 [Google Scholar]
  100. Mine A, Hyodo K, Tajima Y, Kusumanegara K, Taniguchi T. 100.  et al. 2012. Differential roles of Hsp70 and Hsp90 in the assembly of the replicase complex of a positive-strand RNA plant virus. J. Virol. 86:12091–104 [Google Scholar]
  101. Gonzalez O, Fontanes V, Raychaudhuri S, Loo R, Loo J. 101.  et al. 2009. The heat shock protein inhibitor Quercetin attenuates hepatitis C virus production. Hepatology 50:1756–64 [Google Scholar]
  102. Snyder JC, Samson RY, Brumfield SK, Bell SD, Young MJ. 102.  2013. Functional interplay between a virus and the ESCRT machinery in Archaea. PNAS 110:10783–87 [Google Scholar]
  103. Lambert C, Doring T, Prange R. 103.  2007. Hepatitis B virus maturation is sensitive to functional inhibition of ESCRT-III, Vps4, and γ2-adaptin. J. Virol. 81:9050–60 [Google Scholar]
  104. Soh TK, Whelan SP. 104.  2015. Tracking the fate of genetically distinct vesicular stomatitis virus matrix proteins highlights the role for late domains in assembly. J. Virol. 89:11750–60 [Google Scholar]
  105. Corless L, Crump CM, Griffin SD, Harris M. 105.  2010. Vps4 and the ESCRT-III complex are required for the release of infectious hepatitis C virus particles. J. Gen. Virol. 91:362–72 [Google Scholar]
  106. Wang H, Perry JW, Lauring AS, Neddermann P, De Francesco R, Tai AW. 106.  2014. Oxysterol-binding protein is a phosphatidylinositol 4-kinase effector required for HCV replication membrane integrity and cholesterol trafficking. Gastroenterology 146:1373–85.e11 [Google Scholar]
  107. Yamaji Y, Sakurai K, Hamada K, Komatsu K, Ozeki J. 107.  et al. 2010. Significance of eukaryotic translation elongation factor 1A in tobacco mosaic virus infection. Arch. Virol. 155:263–68 [Google Scholar]
  108. Wei T, Li D, Marcial D, Khan M, Lin MH. 108.  et al. 2014. The eukaryotic elongation factor 1A is critical for genome replication of the paramyxovirus respiratory syncytial virus. PLOS ONE 9:e114447 [Google Scholar]
  109. Thivierge K, Cotton S, Dufresne PJ, Mathieu I, Beauchemin C. 109.  et al. 2008. Eukaryotic elongation factor 1A interacts with Turnip mosaic virus RNA-dependent RNA polymerase and VPg-Pro in virus-induced vesicles. Virology 377:216–25 [Google Scholar]
  110. Komoda K, Ishibashi K, Kawamura-Nagaya K, Ishikawa M. 110.  2014. Possible involvement of eEF1A in Tomato spotted wilt virus RNA synthesis. Virology 468–470:81–87 [Google Scholar]
  111. Li S, Feng S, Wang JH, He WR, Qin HY. 111.  et al. 2015. eEF1A interacts with the NS5A protein and inhibits the growth of classical swine fever virus. Viruses 7:4563–81 [Google Scholar]
  112. Hwang J, Lee S, Lee JH, Kang WH, Kang JH. 112.  et al. 2015. Plant translation elongation factor 1Bβ facilitates Potato virus X (PVX) infection and interacts with PVX triple gene block protein 1. PLOS ONE 10:e0128014 [Google Scholar]
  113. Ariumi Y, Kuroki M, Abe K, Dansako H, Ikeda M. 113.  et al. 2007. DDX3 DEAD-box RNA helicase is required for hepatitis C virus RNA replication. J. Virol. 81:13922–26 [Google Scholar]
  114. Goh PY, Tan YJ, Lim SP, Tan YH, Lim SG. 114.  et al. 2004. Cellular RNA helicase p68 relocalization and interaction with the hepatitis C virus (HCV) NS5B protein and the potential role of p68 in HCV RNA replication. J. Virol. 78:5288–98 [Google Scholar]
  115. Li C, Ge LL, Li PP, Wang Y, Sun MX. 115.  et al. 2013. The DEAD-box RNA helicase DDX5 acts as a positive regulator of Japanese encephalitis virus replication by binding to viral 3′ UTR. Antivir. Res. 100:487–99 [Google Scholar]
  116. Lin L, Li Y, Pyo HM, Lu X, Raman SN. 116.  et al. 2012. Identification of RNA helicase A as a cellular factor that interacts with influenza A virus NS1 protein and its role in the virus life cycle. J. Virol. 86:1942–54 [Google Scholar]
  117. Huang TS, Wei T, Laliberte JF, Wang A. 117.  2010. A host RNA helicase-like protein, AtRH8, interacts with the potyviral genome-linked protein, VPg, associates with the virus accumulation complex, and is essential for infection. Plant Physiol 152:255–66 [Google Scholar]
  118. Lawrence P, Rieder E. 118.  2009. Identification of RNA helicase A as a new host factor in the replication cycle of foot-and-mouth disease virus. J. Virol. 83:11356–66 [Google Scholar]
  119. Xu Z, Hobman TC. 119.  2012. The helicase activity of DDX56 is required for its role in assembly of infectious West Nile virus particles. Virology 433:226–35 [Google Scholar]
  120. Ko C, Lee S, Windisch MP, Ryu WS. 120.  2014. DDX3 DEAD-box RNA helicase is a host factor that restricts hepatitis B virus replication at the transcriptional level. J. Virol. 88:13689–98 [Google Scholar]
  121. Chen G, Liu CH, Zhou L, Krug RM. 121.  2014. Cellular DDX21 RNA helicase inhibits influenza A virus replication but is counteracted by the viral NS1 protein. Cell Host Microbe 15:484–93 [Google Scholar]
  122. Kaido M, Abe K, Mine A, Hyodo K, Taniguchi T. 122.  et al. 2014. GAPDH-A recruits a plant virus movement protein to cortical virus replication complexes to facilitate viral cell-to-cell movement. PLOS Pathog 10:e1004505 [Google Scholar]
  123. Yang SH, Liu ML, Tien CF, Chou SJ, Chang RY. 123.  2009. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) interaction with 3′ ends of Japanese encephalitis virus RNA and colocalization with the viral NS5 protein. J. Biomed. Sci 1640 [Google Scholar]
  124. Prasanth KR, Huang YW, Liou MR, Wang RY, Hu CC. 124.  et al. 2011. Glyceraldehyde 3-phosphate dehydrogenase negatively regulates the replication of Bamboo mosaic virus and its associated satellite RNA. J. Virol. 85:8829–40 [Google Scholar]
  125. Galan C, Sola I, Nogales A, Thomas B, Akoulitchev A. 125.  et al. 2009. Host cell proteins interacting with the 3′ end of TGEV coronavirus genome influence virus replication. Virology 391:304–14 [Google Scholar]
  126. Yi M, Schultz DE, Lemon SM. 126.  2000. Functional significance of the interaction of hepatitis A virus RNA with glyceraldehyde 3-phosphate dehydrogenase (GAPDH): opposing effects of GAPDH and polypyrimidine tract binding protein on internal ribosome entry site function. J. Virol. 74:6459–68 [Google Scholar]
  127. Koga R, Sugita Y, Noda T, Yanagi Y, Ohno S. 127.  2015. Actin-modulating protein cofilin is involved in the formation of measles virus ribonucleoprotein complex at the perinuclear region. J. Virol. 89:10524–31 [Google Scholar]
  128. He F, Ling L, Liao Y, Li S, Han W. 128.  et al. 2014. β-Actin interacts with the E2 protein and is involved in the early replication of classical swine fever virus. Virus Res 179:161–68 [Google Scholar]
  129. Xu H, Hao X, Wang S, Wang Z, Cai M. 129.  et al. 2015. Real-time imaging of rabies virus entry into living Vero cells. Sci. Rep. 5:11753 [Google Scholar]
  130. Lu J, Qu Y, Liu Y, Jambusaria R, Han Z. 130.  et al. 2013. Host IQGAP1 and Ebola virus VP40 interactions facilitate virus-like particle egress. J. Virol. 87:7777–80 [Google Scholar]
  131. Spuul P, Balistreri G, Kaariainen L, Ahola T. 131.  2010. Phosphatidylinositol 3-kinase-, actin-, and microtubule-dependent transport of Semliki Forest virus replication complexes from the plasma membrane to modified lysosomes. J. Virol. 84:7543–57 [Google Scholar]
  132. Cui X, Wei T, Chowda-Reddy RV, Sun G, Wang A. 132.  2010. The Tobacco etch virus P3 protein forms mobile inclusions via the early secretory pathway and traffics along actin microfilaments. Virology 397:56–63 [Google Scholar]
  133. Lai CK, Jeng KS, Machida K, Lai MM. 133.  2008. Association of hepatitis C virus replication complexes with microtubules and actin filaments is dependent on the interaction of NS3 and NS5A. J. Virol. 82:8838–48 [Google Scholar]
  134. Avilov SV, Moisy D, Naffakh N, Cusack S. 134.  2012. Influenza A virus progeny vRNP trafficking in live infected cells studied with the virus-encoded fluorescently tagged PB2 protein. Vaccine 30:7411–17 [Google Scholar]

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