Cytoplasmic RNA granules and viral infection

Annual Review of Virology

Volumn 1, Issue 1, 2014, Pages 147-170

  Tsai, Wei Chih ^a   Lloyd, Richard E ^a  

^a BAYLOR COLLEGE OF MEDICINE   (United States)

Author keywords

G3BP; P bodies; PKR; Stress granules

Indexed keywords

CYTOPLASMIC RNA GRANULE; GENOMIC RNA; INTERFERON; MESSENGER RNA; MICRORNA 122; NONSTRUCTURAL PROTEIN 1; PROTEIN KINASE R; RNA; TRANSACTIVATOR PROTEIN; UNCLASSIFIED DRUG;

APOPTOSIS; ARTICLE; AUTOPHAGY; CELL FATE; CELL GRANULE; CELL STRESS; CELL STRUCTURE; CORONAVIRIDAE; CYTOPLASM; DNA VIRUS; ENTEROVIRUS; GENE EXPRESSION; GENE FUNCTION; GENE REPRESSION; GENE SILENCING; HEPATITIS C VIRUS; HERPES SIMPLEX VIRUS; HUMAN; HUMAN IMMUNODEFICIENCY VIRUS 1; INNATE IMMUNITY; INTERACTIONS WITH RNA; NEGATIVE-STRAND RNA VIRUS; NONHUMAN; POSITIVE-STRAND RNA VIRUS; PRIORITY JOURNAL; PROTEIN SYNTHESIS; RETROVIRIDAE; RNA PROCESSING; TRANSLATION INITIATION; VIRUS; VIRUS CELL INTERACTION; VIRUS GENE; VIRUS INFECTION; VIRUS PARTICLE; VIRUS PATHOGENESIS; VIRUS REPLICATION; VIRUS STRAIN;

EID: 85016938715     PISSN: 2327056X     EISSN: 23270578     Source Type: Journal    
DOI: 10.1146/annurev-virology-031413-085505     Document Type: Article

References (135)

1. Mao YS, Zhang B, Spector DL. 2011. Biogenesis and function of nuclear bodies. Trends Genet. 27:295-306
2. Caudron-Herger M, Rippe K. 2012. Nuclear architecture by RNA. Curr. Opin. Genet. Dev. 22:179-87
3. Kedersha N, Anderson P. 2007. Mammalian stress granules and processing bodies. Methods Enzymol. 431:61-81
4. Kedersha N, Stoecklin G, Ayodele M, Yacono P, Lykke-Andersen J, et al. 2005. Stress granules and processing bodies are dynamically linked sites of mRNP remodeling. J. Cell Biol. 169:871-84
5. Buchan JR, ParkerR. 2009. Eukaryotic stress granules: the ins and outs of translation. Mol. Cell 36:932-41
6. Mokas S, Mills JR, Garreau C, Fournier MJ, Robert F, et al. 2009. Uncoupling stress granule assembly and translation initiation inhibition. Mol. Biol. Cell 20:2673-83
7. Dang Y, Kedersha N, Low WK, Romo D, Gorospe M, et al. 2006. Eukaryotic initiation factor 2α-independent pathway of stress granule induction by the natural product pateamine A. J. Biol. Chem. 281:32870-78
8. Kedersha NL, Gupta M, Li W, Miller I, Anderson P. 1999. RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2αto the assembly of mammalian stress granules. J. Cell Biol. 147:1431-42
9. Chang TC, Yamashita A, Chen CYA, Yamashita Y, Zhu W, et al. 2004. UNR, a new partner of poly(A)-binding protein, plays a key role in translationally coupled mRNA turnover mediated by the c-fos major coding-region determinant. Genes Dev. 18:2010-23
10. Shyu AB, Wilkinson MF, van Hoof A. 2008. Messenger RNA regulation: to translate or to degrade. EMBO J. 27:471-81
11. Anderson P, Kedersha N. 2008. Stress granules: the Tao of RNA triage. Trends Biochem. Sci. 33:141-50
12. Towers ER, Kelly JJ, Sud R, Gale JE, Dawson SJ. 2011. Caprin-1 is a target of the deafness gene Pou4f3 and is recruited to stress granules in cochlear hair cells in response to ototoxic damage. J. Cell Sci. 124:1145-55
13. Mangiardi DA, McLaughlin-Williamson K, May KE, Messana EP, Mountain DC, Cotanche DA. 2004. Progression of hair cell ejection and molecular markers of apoptosis in the avian cochlea following gentamicin treatment. J. Comp. Neurol. 475:1-18
14. Kotani T, Yasuda K, Ota R, Yamashita M. 2013. Cyclin B1 mRNA translation is temporally controlled through formation and disassembly of RNA granules. J. Cell Biol. 202:1041-55
15. Weil TT, Parton RM, Herpers B, Soetaert J, Veenendaal T, et al. 2012. Drosophila patterning is established by differential association of mRNAs with P bodies. Nat. Cell Biol. 14:1305-15
16. Costa A, Pazman C, Sinsimer KS, Wong LC, McLeod I, et al. 2013. Rasputin functions as a positive regulator of Orb in Drosophila oogenesis. PLoS ONE 8:e72864
17. Bentmann E, Haass C, Dormann D. 2013. Stress granules in neurodegeneration-lessons learnt from TAR DNA binding protein of 43 kDa and fused in sarcoma. FEBS J. 280:4348-70
18. Vanderweyde T, Youmans K, Liu-Yesucevitz L, Wolozin B. 2013. Role of stress granules and RNAbinding proteins in neurodegeneration: a mini-review. Gerontology 59:524-33
19. Shelkovnikova TA, Robinson H, Connor-Robson N, Buchman VL. 2013. Recruitment into stress granules prevents irreversible aggregation of FUS protein mislocalized to the cytoplasm. Cell Cycle 12:3194-202
20. Nakamura T, Furuhashi M, Li P, Cao H, Tuncman G, et al. 2010. Double-stranded RNA-dependent protein kinase links pathogen sensing with stress and metabolic homeostasis. Cell 140:338-48
21. Yang X, Nath A, Opperman MJ, Chan C. 2010. The double-stranded RNA-dependent protein kinase differentially regulates insulin receptor substrates 1 and 2 in HepG2 cells. Mol. Biol. Cell 21:3449-58
22. Lu B, Nakamura T, Inouye K, Li J, Tang Y, et al. 2012. Novel role of PKR in inflammasome activation and HMGB1 release. Nature 488:670-74
23. Taghavi N, Samuel CE. 2012. Protein kinase PKR catalytic activity is required for the PKR-dependent activation of mitogen-activated protein kinases and amplification of interferon β induction following virus infection. Virology 427:208-16
24. Steele L, Errington F, Prestwich R, Ilett E, Harrington K, et al. 2011. Pro-inflammatory cytokine/ chemokine production by reovirus treated melanoma cells is PKR/NF-κB mediated and supports innate and adaptive anti-tumour immune priming. Mol. Cancer 10:20-33
25. Garcia MA, Gil J, Ventoso I, Guerra S, Domingo E, et al. 2006. Impact of protein kinase PKR in cell biology: from antiviral to antiproliferative action. Microbiol. Mol. Biol. Rev. 70:1032-60
26. Okonski KM, Samuel CE. 2013. Stress granule formation induced by measles virus is protein kinase PKR dependent and impaired by RNA adenosine deaminase ADAR1. J. Virol. 87:756-66
27. Onomoto K, Jogi M, Yoo JS, Narita R, Morimoto S, et al. 2012. Critical role of an antiviral stress granule containing RIG-I and PKR in viral detection and innate immunity. PLoS ONE 7:e43031
28. Reineke LC, Dougherty JD, Pierre P, Lloyd RE. 2012. Large G3BP-induced granules trigger eIF2α phosphorylation. Mol. Biol. Cell 23:3499-510
29. Dougherty JD, Reineke LC, Lloyd RE. 2014. mRNA decapping enzyme 1a (Dcp1a)-induced translational arrest through PKR activation requires the N-terminal EVH1 domain. J. Biol. Chem. 289:3936-49
30. Ghosh S, May MJ, Kopp EB. 1998. NF-κB and Rel proteins: evolutionarily conserved mediators of immune responses. Annu. Rev. Immunol. 16:225-60
31. Gil J, Rullas J, Garcia MA, Alcamí J, Esteban M. 2001. The catalytic activity of dsRNA-dependent protein kinase, PKR, is required for NF-κB activation. Oncogene 20:385-94
32. Bonnet MC, Weil R, Dam E, Hovanessian AG, Meurs EF. 2000. PKR stimulates NF-κB irrespective of its kinase function by interacting with the IκB kinase complex. Mol. Cell. Biol. 20:4532-42
33. Fung G, Ng CS, Zhang J, Shi J, Wong J, et al. 2013. Production of a dominant-negative fragment due to G3BP1 cleavage contributes to the disruption of mitochondria-associated protective stress granules during CVB3 infection. PLoS ONE 8:e79546
34. Ng CS, Jogi M, Yoo JS, Onomoto K, Koike S, et al. 2013. Encephalomyocarditis virus disrupts stress granules, the critical platform for triggering antiviral innate immune responses. J. Virol. 87:9511-22
35. Hebner CM, Wilson R, Rader J, Bidder M, Laimins LA. 2006. Human papillomaviruses target the double-stranded RNA protein kinase pathway. J. Gen. Virol. 87:3183-93
36. Langereis MA, Feng Q, van Kuppeveld FJ. 2013. MDA5 localizes to stress granules, but this localization is not required for the induction of type I interferon. J. Virol. 87:6314-25
37. Khaperskyy DA, Hatchette TF, McCormick C. 2011. InfluenzaAvirus inhibits cytoplasmic stress granule formation. FASEB J. 26:1629-39
38. Wasserman T, Katsenelson K, Daniliuc S, Hasin T, Choder M, Aronheim A. 2010. A novel c-Jun Nterminal kinase ( JNK)-binding proteinWDR62is recruited to stress granules and mediates a nonclassical JNK activation. Mol. Biol. Cell 21:117-30
39. Mazroui R, Sukarieh R, Bordeleau ME, Kaufman RJ, Northcote P, et al. 2006. Inhibition of ribosome recruitment induces stress granule formation independently of eukaryotic initiation factor 2αphosphorylation. Mol. Biol. Cell 17:4212-19
40. Anderson P, Kedersha N. 2009. RNA granules: post-transcriptional and epigenetic modulators of gene expression. Nat. Rev. Mol. Cell Biol. 10:430-36
41. Kedersha N, Ivanov P, Anderson P. 2013. Stress granules and cell signaling: more than just a passing phase? Trends Biochem. Sci. 38:494-506
42. Loschi M, Leishman CC, Berardone N, Boccaccio GL. 2009. Dynein and kinesin regulate stress-granule and P-body dynamics. J. Cell Sci. 122:3973-82
43. Ohn T, Anderson P. 2010. The role of posttranslational modifications in the assembly of stress granules. WIRES RNA 1:486-93
44. Ohn T, Kedersha N, Hickman T, Tisdale S, Anderson P. 2008. A functional RNAi screen links OGlcNAc modification of ribosomal proteins to stress granule and processing body assembly. Nat. Cell Biol. 10:1224-31
45. Weber SC, Brangwynne CP. 2012. Getting RNA and protein in phase. Cell 149:1188-91
46. Kato M, Han TW, Xie S, Shi K, Du X, et al. 2012. Cell-free formation ofRNAgranules: Low complexity sequence domains form dynamic fibers within hydrogels. Cell 149:753-67
47. Han TW, Kato M, Xie S, Wu LC, Mirzaei H, et al. 2012. Cell-free formation of RNA granules: Bound RNAs identify features and components of cellular assemblies. Cell 149:768-79
48. Bentmann E, Neumann M, Tahirovic S, Rodde R, Dormann D, Haass C. 2012. Requirements for stress granule recruitment of fused in sarcoma (FUS) and TAR DNA-binding protein of 43 kDa (TDP-43). J. Biol. Chem. 287:23079-94
49. Li P, Banjade S, ChengHC, Kim S, Chen B, et al. 2012. Phase transitions in the assembly of multivalent signalling proteins. Nature 483:336-40
50. Aulas A, Stabile S, Vande Velde C. 2012. Endogenous TDP-43, but not FUS, contributes to stress granule assembly via G3BP. Mol. Neurodegener. 7:54
51. Tourrière H, Chebli K, Zekri L, Courselaud B, Blanchard JM, et al. 2003. The RasGAP-associated endoribonuclease G3BP assembles stress granules. J. Cell Biol. 160:823-31
52. Bikkavilli RK, Malbon CC. 2011. Arginine methylation of G3BP1 in response to Wnt3a regulates β-catenin mRNA. J. Cell Sci. 124:2310-20
53. Dammer EB, Fallini C, Gozal YM, Duong DM, Rossoll W, et al. 2012. Coaggregation of RNA-binding proteins in a model of TDP-43 proteinopathy with selective RGG motif methylation and a role for RRM1 ubiquitination. PLoS ONE 7:e38658
54. White JP, Cardenas AM, Marissen WE, Lloyd RE. 2007. Inhibition of cytoplasmicmRNAstress granule formation by a viral proteinase. Cell Host Microbe 2:295-305
55. Piotrowska J, Hansen SJ, Park N, Jamka K, Sarnow P, Gustin KE. 2010. Stable formation of compositionally unique stress granules in virus-infected cells. J. Virol. 84:3654-65
56. White JP, Lloyd RE. 2011. Poliovirus unlinks TIA1 aggregation and mRNA stress granule formation. J. Virol. 85:12442-54
57. Borghese F, Michiels T. 2011. The leader protein of cardioviruses inhibits stress granule assembly. J. Virol. 85:9614-22
58. Khong A, Jan E. 2011. Modulation of stress granules and P bodies during dicistrovirus infection. J. Virol. 85:1439-51
59. Mok BWY, Song W, Wang P, Tai H, Chen Y, et al. 2012. TheNS1 protein of influenza A virus interacts with cellular processing bodies and stress granules through RNA-associated protein 55 (RAP55) during virus infection. J. Virol. 86:12695-707
60. Montero H, Rojas M, Arias CF, López S. 2008. Rotavirus infection induces the phosphorylation of eIF2αbut prevents the formation of stress granules. J. Virol. 82:1496-504
61. Smith JA, Schmechel SC, Raghavan A, Abelson M, Reilly C, et al. 2006. Reovirus induces and benefits from an integrated cellular stress response. J. Virol. 80:2019-33
62. Qin Q, Hastings C, Miller CL. 2009. Mammalian orthoreovirus particles induce and are recruited into stress granules at early times postinfection. J. Virol. 83:11090-101
63. Qin Q, Carroll K, Hastings C, Miller CL. 2011. Mammalian orthoreovirus escape from host translational shutoff correlates with stress granule disruption and is independent of eIF2αphosphorylation and PKR. J. Virol. 85:8798-810
64. Carroll K, Hastings C, Miller CL. 2014. Amino acids 78 and 79 of mammalian orthoreovirus proteinμNS are necessary for stress granule localization, core protein λ2 interaction, and de novo virus replication. Virology 448:133-45
65. Ruggieri A, Dazert E, Metz P, Hofmann S, Bergeest JP, et al. 2012. Dynamic oscillation of translation and stress granule formation mark the cellular response to virus infection. Cell Host Microbe 12:71-85
66. Paul D, Hoppe S, Saher G, Krijnse-Locker J, Bartenschlager R. 2013. Morphological and biochemical characterization of the membranous hepatitis C virus replication compartment. J. Virol. 87:10612-27
67. Raaben M, Groot Koerkamp MJA, Rottier PJM, De Haan CAM. 2007. Mouse hepatitis coronavirus replication induces host translational shutoff and mRNA decay, with concomitant formation of stress granules and processing bodies. Cell Microbiol. 9:2218-29
68. Sola I, Galán C, Mateos-Gómez PA, Palacio L, Zúniga S, et al. 2011. The polypyrimidine tract-binding protein affects coronavirus RNA accumulation levels and relocalizes viral RNAs to novel cytoplasmic domains different from replication-transcription sites. J. Virol. 85:5136-49
69. Cristea IM, Rozjabek H, Molloy KR, Karki S, White LL, et al. 2010. Host factors associated with the Sindbis virus RNA-dependent RNA polymerase: role for G3BP1 and G3BP2 in virus replication. J. Virol. 84:6720-32
70. Frolova E, Gorchakov R, Garmashova N, Atasheva S, Vergara LA, Frolov I. 2006. Formation of nsP3-specific protein complexes during Sindbis virus replication. J. Virol. 80:4122-34
71. Gorchakov R, Garmashova N, Frolova E, Frolov I. 2008. Different types of nsP3-containing protein complexes in Sindbis virus-infected cells. J. Virol. 82:10088-101
72. Fros JJ, Domeradzka NE, Baggen J, Geertsema C, Flipse J, et al. 2012. Chikungunya virus nsP3 blocks stress granule assembly by recruitment of G3BP into cytoplasmic foci. J. Virol. 86:10873-79
73. Atasheva S, GorchakovR, EnglishR, Frolov I, Frolova E. 2007. Development of Sindbis viruses encoding nsP2/GFP chimeric proteins and their application for studying nsP2 functioning. J. Virol. 81:5046-57
74. McInerney GM, Kedersha NL, Kaufman RJ, Anderson P, Liljeström P. 2005. Importance of eIF2α phosphorylation and stress granule assembly in alphavirus translation regulation. Mol. Biol. Cell 16:3753-63
75. Panas MD, Varjak M, Lulla A, Eng KE, Merits A, et al. 2012. Sequestration of G3BP coupled with efficient translation inhibits stress granules in Semliki Forest virus infection. Mol. Biol. Cell 23:4701-12
76. Matthews JD, Frey TK. 2012. Analysis of subcellular G3BP redistribution during rubella virus infection. J. Gen. Virol. 93:267-74
77. Emara MM, Brinton MA. 2007. Interaction of TIA-1/TIAR with West Nile and dengue virus products in infected cells interferes with stress granule formation and processing body assembly. Proc. Natl. Acad. Sci. USA 104:9041-46
78. Emara MM, Liu H, Davis WG, Brinton MA. 2008. Mutation of mapped TIA-1/TIAR binding sites in the 3' terminal stem-loop of West Nile virus minus-strand RNA in an infectious clone negatively affects genomic RNA amplification. J. Virol. 82:10657-70
79. Li W, Li Y, Kedersha N, Anderson P, Emara M, et al. 2002. Cell proteins TIA-1 and TIAR interact with the 3' stem-loop of the West Nile virus complementary minus-strand RNA and facilitate virus replication. J. Virol. 76:11989-2000
80. Katoh H, Okamoto T, Fukuhara T, Kambara H, Morita E, et al. 2013. Japanese encephalitis virus core protein inhibits stress granule formation through an interaction with Caprin-1 and facilitates viral propagation. J. Virol. 87:489-502
81. Pager CT, Schütz S, Abraham TM, Luo G, Sarnow P. 2013. Modulation of hepatitis C virus RNA abundance and virus release by dispersion of processing bodies and enrichment of stress granules. Virology 435:472-84
82. Ariumi Y, Kuroki M, Kushima Y, Osugi K, Hijikata M, et al. 2011. Hepatitis C virus hijacks P-body and stress granule components around lipid droplets. J. Virol. 85:6882-92
83. Garaigorta U, Heim MH, Boyd B, Wieland S, Chisari FV. 2012. Hepatitis C virus induces the formation of stress granules whose proteins regulate HCV RNA replication, virus assembly and egress. J. Virol. 86:11043-56
84. Yi Z, Pan T, Wu X, Song W, Wang S, et al. 2011. Hepatitis C virus co-opts Ras-GTPase-activating protein-binding protein 1 for its genome replication. J. Virol. 85:6996-7004
85. Abrahamyan LG, Chatel-Chaix L, Ajamian L, Milev MP, Monette A, et al. 2010. Novel Staufen1 ribonucleoproteins prevent formation of stress granules but favour encapsidation of HIV-1 genomic RNA. J. Cell Sci. 123:369-83
86. Thomas MG, Tosar LJM, Desbats MA, Leishman CC, Boccaccio GL. 2009. Mammalian Staufen 1 is recruited to stress granules and impairs their assembly. J. Cell Sci. 122:563-73
87. Legros S, Boxus M, Gatot JS, Van Lint C, Kruys V, et al. 2011. The HTLV-1 Tax protein inhibits formation of stress granules by interacting with histone deacetylase 6. Oncogene 30:4050-62
88. Kwon S, Zhang Y, Matthias P. 2007. The deacetylase HDAC6 is a novel critical component of stress granules involved in the stress response. Genes Dev. 21:3381-94
89. Takahashi M, Higuchi M, Makokha GN, Matsuki H, Yoshita M, et al. 2013. HTLV-1 Tax oncoprotein stimulates ROS production and apoptosis in T cells by interacting with USP10. Blood 122:715-25
90. Linero FN, Thomas MG, Boccaccio GL, Scolaro LA. 2011. Junin virus infection impairs stress-granule formation in Vero cells treatedwith arsenite via inhibition of eIF2αphosphorylation. J. Virol. 92:2889-99
91. BairdNL, York J, Nunberg JH. 2012. Arenavirus infection induces discrete cytosolic structures for RNA replication. J. Virol. 86:11301-10
92. Pfaller CK, Li Z, George CX, Samuel CE. 2011. Protein kinase PKR and RNA adenosine deaminase ADAR1: new roles for old players as modulators of the interferon response. Curr. Opin. Immunol. 23:573-82
93. Dinh PX, Beura LK, Das PB, Panda D, Das A, Pattnaik AK. 2013. Induction of stress granule-like structures in vesicular stomatitis virus-infected cells. J. Virol. 87:372-83
94. Lindquist ME, Mainou BA, Dermody TS, Crowe JE. 2011. Activation of protein kinase R is required for induction of stress granules by respiratory syncytial virus but dispensable for viral replication. Virology 413:103-10
95. Lindquist ME, LiflandAW,Utley TJ, Santangelo PJ, Crowe JE. 2010. Respiratory syncytial virus induces host RNA stress granules to facilitate viral replication. J. Virol. 84:12274-84
96. Hanley LL, McGivern DR, Teng MN, Djang R, Collins PL, Fearns R. 2010. Roles of the respiratory syncytial virus trailer region: effects of mutations on genome production and stress granule formation. Virology 406:241-52
97. Iseni F, Garcin D, Nishio M, Kedersha N, Anderson P, Kolakofsky D. 2002. Sendai virus trailer RNA binds TIAR, a cellular protein involved in virus-induced apoptosis. EMBO J. 21:5141-50
98. Katsafanas GC, Moss B. 2007. Colocalization of transcription and translationwithin cytoplasmic poxvirus factories coordinates viral expression and subjugates host functions. Cell Host Microbe 2:221-28
99. Katsafanas GC, Moss B. 2004. Vaccinia virus intermediate stage transcription is complemented by Ras-GTPase-activating protein SH3 domain-binding protein (G3BP) and cytoplasmic activation/ proliferation-associated protein (p137) individually or as a heterodimer. J. Biol. Chem. 279:52210-17
100. Zaborowska I, Kellner K, Henry M, Meleady P, Walsh D. 2012. Recruitment of host translation initiation factor eIF4G by the vaccinia virus ssDNA-binding protein I3. Virology 425:11-22
101. Walsh D, Arias C, Perez C,Halladin D, Escandon M, et al. 2008. Eukaryotic translation initiation factor 4F architectural alterations accompany translation initiation factor redistribution in poxvirus-infected cells. Mol. Cell. Biol. 28:2648-58
102. Simpson-Holley M, Kedersha N, Dower K, Rubins KH, Anderson P, et al. 2011. Formation of antiviral cytoplasmic granules during orthopoxvirus infection. J. Virol. 85:1581-93
103. Dougherty JD, White JP, Lloyd RE. 2011. Poliovirus-mediated disruption of cytoplasmic processing bodies. J. Virol. 85:64-75
104. Zheng D, Ezzeddine N, Chen CYA, Zhu W, He X, Shyu AB. 2008. Deadenylation is prerequisite for P-body formation and mRNA decay in mammalian cells. J. Cell Biol. 182:89-101
105. Rzeczkowski K, Beuerlein K,Müller H, Dittrich-Breiholz O, Schneider H, et al. 2011. c-Jun N-terminal kinase phosphorylates DCP1a to control formation of P bodies. J. Cell Biol. 194:581-96
106. Aizer A, Brody Y, Ler LW, Sonenberg N, Singer RH, Shav-Tal Y. 2008. The dynamics of mammalian P body transport, assembly, and disassembly in vivo. Mol. Biol. Cell 19:4154-66
107. Greer AE, Hearing P, Ketner G. 2011. The adenovirus E4 11k protein binds and relocalizes the cytoplasmic P-body component Ddx6 to aggresomes. Virology 417:161-68
108. Chahar HS, Chen S, Manjunath N. 2013. P-body components LSM1, GW182, DDX3, DDX6 and XRN1 are recruited to WNV replication sites and positively regulate viral replication. Virology 436:1-7
109. Ward AM, Bidet K, Yinglin A, Ler SG, Hogue K, et al. 2011. Quantitative mass spectrometry of DENV-2 RNA-interacting proteins reveals that the DEAD-box RNA helicase DDX6 binds the DB1 and DB2 3' UTR structures. RNA Biol. 8:1173-86
110. Ernoult-Lange M, Baconnais S, Harper M, Minshall N, Souquere S, et al. 2012. Multiple binding of repressed mRNAs by the P-body protein Rck/p54. RNA 18:1702-15
111. Silva PAGC, Pereira CF, Dalebout TJ, Spaan WJM, Bredenbeek PJ. 2010. An RNA pseudoknot is required for production of yellow fever virus subgenomic RNA by the host nuclease XRN1. J. Virol. 84:11395-406
112. Pijlman GP, Funk A, Kondratieva N, Leung J, Torres S, et al. 2008. A highly structured, nucleaseresistant, noncoding RNA produced by flaviviruses is required for pathogenicity. Cell Host Microbe 4:579-91
113. Moon SL, Anderson JR, Kumagai Y, Wilusz CJ, Akira S, et al. 2012. A noncoding RNA produced by arthropod-borne flaviviruses inhibits the cellular exoribonuclease XRN1 and alters host mRNA stability. RNA 18:2029-40
114. Schnettler E, Sterken MG, Leung JY, Metz SW, Geertsema C, et al. 2012. Noncoding flavivirus RNA displays RNA interference suppressor activity in insect and mammalian cells. J. Virol. 86:13486-500
115. Angus AGN, Dalrymple D, Boulant S, McGivern DR, Clayton RF, et al. 2010. Requirement of cellular DDX3 for hepatitis C virus replication is unrelated to its interaction with the viral core protein. J. Gen. Virol. 91:122-32
116. Mamiya N, Worman HJ. 1999. Hepatitis C virus core protein binds to a DEAD box RNA helicase. J. Biol. Chem. 274:15751-56
117. You LR, Chen CM, Yeh TS, Tsai TY, Mai RT, et al. 1999. Hepatitis C virus core protein interacts with cellular putative RNA helicase. J. Virol. 73:2841-53
118. Ariumi Y, Kuroki M, Abe KI, Dansako H, Ikeda M, et al. 2007. DDX3 DEAD-box RNA helicase is required for hepatitis C virus RNA replication. J. Virol. 81:13922-26
119. Yu SF, Lujan P, Jackson DL, Emerman M, Linial ML. 2011. The DEAD-box RNA helicase DDX6 is required for efficient encapsidation of a retroviral genome. PLoS Pathog. 7:e1002303
120. Scheller N, Mina LB, Galão RP, Chari A, Giménez-Barcons M, et al. 2009. Translation and replication of hepatitis C virus genomic RNA depends on ancient cellular proteins that control mRNA fates. Proc. Natl. Acad. Sci. USA 106:13517-22
121. Jangra RK, Yi M, Lemon SM. 2010.DDX6(Rck/p54) is required for efficient hepatitisCvirus replication but not for internal ribosome entry site-directed translation. J. Virol. 84:6810-24
122. Berezhna SY, Supekova L, Sever MJ, Schultz PG, Deniz AA. 2011. Dual regulation of hepatitis C viral RNA by cellular RNAi requires partitioning of Ago2 to lipid droplets and P-bodies. RNA 17:1831-45
123. Huys A, Thibault PA, Wilson JA. 2013. Modulation of hepatitis C virus RNA accumulation and translation by DDX6 and miR-122 are mediated by separate mechanisms. PLoS ONE 8:e67437
124. Roberts APE, Lewis AP, Jopling CL. 2011. miR-122 activates hepatitisCvirus translation by a specialized mechanism requiring particular RNA components. Nucleic Acids Res. 39:7716-29
125. Pérez-Vilar ó G, Scheller N, Saludes V, Díez J. 2012. Hepatitis C virus infection alters P-body composition but is independent of P-body granules. J. Virol. 86:8740-49
126. Mir MA, Duran WA, Hjelle BL, Ye C, Panganiban AT. 2008. Storage of cellular 5' mRNA caps in P bodies for viral cap-snatching. Proc. Natl. Acad. Sci. USA 105:19294-99
127. Mir MA, Panganiban AT. 2008. A protein that replaces the entire cellular eIF4F complex. EMBO J. 27:3129-39
128. Noueiry AO,Díez J, Falk SP, Chen J, Ahlquist P. 2003. Yeast Lsm1p-7p/Pat1p deadenylation-dependent mRNA-decapping factors are required for brome mosaic virus genomic RNA translation. Mol. Cell. Biol. 23:4094-106
129. Beckham CJ, Light HR, Nissan TA, Ahlquist P, Parker R, Noueiry A. 2007. Interactions between brome mosaic virus RNAs and cytoplasmic processing bodies. J. Virol. 81:9759-68
130. Wang X, Lee WM, Watanabe T, Schwartz M, Janda M, Ahlquist P. 2005. Brome mosaic virus 1a nucleoside triphosphatase/helicase domain plays crucial roles in recruiting RNA replication templates. J. Virol. 79:13747-58
131. Yasuda-Inoue M, Kuroki M, Ariumi Y. 2013. DDX3 RNA helicase is required for HIV-1 Tat function. Biochem. Biophys. Res. Commun. 441:607-11
132. Izumi T, Burdick R, Shigemi M, Plisov S, Hu WS, Pathak VK. 2013. Mov10 and APOBEC3G localization to processing bodies is not required for virion incorporation and antiviral activity. J. Virol. 87:11047-62
133. Phalora PK, Sherer NM, Wolinsky SM, Swanson CM, Malim MH. 2012. HIV-1 replication and APOBEC3 antiviral activity are not regulated by P bodies. J. Virol. 86:11712-24
134. Lu C, Contreras X, Peterlin BM. 2011. P bodies inhibit retrotransposition of endogenous intracisternal A particles. J. Virol. 85:6244-51
135. Lu C, Luo Z, Jäger S, Krogan NJ, Peterlin BM. 2012. Moloney leukemia virus type 10 inhibits reverse transcription and retrotransposition of intracisternal A particles. J. Virol. 86:10517-23