Hepatitis C virus infection alters P-Body composition but is independent of P-Body granules

Journal of Virology

Volumn 86, Issue 16, 2012, Pages 8740-8749

  Pérez Vilaró, Gemma ^a   Scheller, Nicoletta ^a   Saludes, Verónica ^a,b   Díez, Juana ^a  

^a UNIVERSITAT POMPEU FABRA   (Spain)

^b CIBER EPIDEMIOLOGÍA Y SALUD PÚBLICA CIBERESP   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN DDX6; PROTEIN LSM1; PROTEIN PATL1; PROTEIN RAP55; UNCLASSIFIED DRUG; VIRUS PROTEIN; VIRUS RNA;

ARTICLE; CELL COMPOSITION; CELL GRANULE; CONTROLLED STUDY; HEPATITIS C; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROCESSING BODY; PROTEIN DEPLETION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; REPLICON; VIRUS CELL INTERACTION; VIRUS INHIBITION; VIRUS REPLICATION; VIRUS TRANSCRIPTION;

CELL LINE; CYTOPLASMIC GRANULES; DEAD-BOX RNA HELICASES; DNA-BINDING PROTEINS; HEPACIVIRUS; HEPATOCYTES; HUMANS; PROTEIN TRANSPORT; PROTO-ONCOGENE PROTEINS; RNA-BINDING PROTEINS; VIRUS REPLICATION;

EID: 84865089047     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.07167-11     Document Type: Article

References (45)

1. Aizer A, et al. 2008. The dynamics of mammalian P body transport, assembly, and disassembly in vivo. Mol. Biol. Cell 19:4154-4166.
2. Alves-Rodrigues I, Galao RP, Meyerhans A, Diez J. 2006. Saccharomyces cerevisiae: a useful model host to study fundamental biology of viral replication. Virus Res. 120:49-56.
3. Andrei MA, et al. 2005. A role for eIF4E and eIF4E-transporter in targeting mRNPs to mammalian processing bodies. RNA 11:717-727.
4. Angus AG, 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. 91:122-132.
5. Ariumi Y, et al. 2007. DDX3 DEAD-box RNA helicase is required for hepatitis C virus RNA replication. J. Virol. 81:13922-13926.
6. Ariumi Y, et al. 2011. Hepatitis C virus hijacks P-body and stress granule components around lipid droplets. J. Virol. 85:6882-6892.
7. Bartenschlager R, Cosset FL, Lohmann V. 2010. Hepatitis C virus replication cycle. J. Hepatol. 53:583-585.
8. Beckham CJ, Parker R. 2008. P bodies, stress granules, and viral life cycles. Cell Host Microbe 3:206-212.
9. Bhattacharyya SN, Habermacher R, Martine U, Closs EI, Filipowicz W. 2006. Relief of microRNA-mediated translational repression in human cells subjected to stress. Cell 125:1111-1124.
10. Blight KJ, McKeating JA, Rice CM. 2002. Highly permissive cell lines for subgenomic and genomic hepatitis C virus RNA replication. J. Virol. 76: 13001-13014.
11. Boson B, Granio O, Bartenschlager R, Cosset FL. 2011. A concerted action of hepatitis C virus p7 and nonstructural protein 2 regulates core localization at the endoplasmic reticulum and virus assembly. PLoS Pathog. 7:e1002144. doi:10.1371/journal.ppat.1002144.
12. Brengues M, Teixeira D, Parker R. 2005. Movement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodies. Science 310:486-489.
13. Coller J, Parker R. 2004. Eukaryotic mRNA decapping. Annu. Rev. Biochem. 73:861-890.
14. Coller J, Parker R. 2005. General translational repression by activators of mRNA decapping. Cell 122:875-886.
15. Cougot N, Babajko S, Seraphin B. 2004. Cytoplasmic foci are sites of mRNA decay in human cells. J. Cell Biol. 165:31-40.
16. Dougherty JD, White JP, Lloyd RE. 2011. Poliovirus-mediated disruption of cytoplasmic processing bodies. J. Virol. 85:64-75.
17. 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. U. S. A. 104:9041-9046.
18. Erickson SL, Lykke-Andersen J. 2011. Cytoplasmic mRNP granules at a glance. J. Cell Sci. 124:293-297.
19. Eulalio A, Behm-Ansmant I, Schweizer D, Izaurralde E. 2007. P-body formation is a consequence, not the cause, of RNA-mediated gene silencing. Mol. Cell. Biol. 27:3970-3981.
20. Fontanes V, Raychaudhuri S, Dasgupta A. 2009. A cell-permeable peptide inhibits hepatitis C virus replication by sequestering IRES transacting factors. Virology 394:82-90.
21. Franks TM, Lykke-Andersen J. 2008. The control of mRNA decapping and P-body formation. Mol. Cell 32:605-615.
22. Franks TM, Lykke-Andersen J. 2007. TTP and BRF proteins nucleate processing body formation to silence mRNAs with AU-rich elements. Genes Dev. 21:719-735.
23. Gimenez-Barcons M, Diez J. 2011. Yeast processing bodies and stress granules: self-assembly ribonucleoprotein particles. Microb. Cell Fact. 10:73.
24. Gravitz L. 2011. A smouldering public-health crisis. Nature 474:S2-S4.
25. Ingelfinger D, Arndt-Jovin DJ, Luhrmann R, Achsel T. 2002. The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci. RNA 8:1489-1501.
26. Jangra RK, Yi M, Lemon SM. 2010. DDX6 (Rck/p54) is required for efficient hepatitis C virus replication but not for internal ribosome entry site-directed translation. J. Virol. 84:6810-6824.
27. Kedersha N, et al. 2005. Stress granules and processing bodies are dynamically linked sites of mRNP remodeling. J. Cell Biol. 169:871-884.
28. Khong A, Jan E. 2011. Modulation of stress granules and P bodies during dicistrovirus infection. J. Virol. 85:1439-1451.
29. Lindenbach BD, et al. 2005. Complete replication of hepatitis C virus in cell culture. Science 309:623-626.
30. Lohmann V, Korner F, Dobierzewska A, Bartenschlager R. 2001. Mutations in hepatitis C virus RNAs conferring cell culture adaptation. J. Virol. 75:1437-1449.
31. Mas A, Alves-Rodrigues I, Noueiry A, Ahlquist P, Diez J. 2006. Host deadenylation-dependent mRNA decapping factors are required for a key step in brome mosaic virus RNA replication. J. Virol. 80:246-251.
32. Migliaccio G, et al. 2003. Characterization of resistance to non-obligate chain-terminating ribonucleoside analogs that inhibit hepatitis C virus replication in vitro. J. Biol. Chem. 278:49164-49170.
33. Miyanari Y, et al. 2007. The lipid droplet is an important organelle for hepatitis C virus production. Nat. Cell Biol. 9:1089-1097.
34. Nissan T, Rajyaguru P, She M, Song H, Parker R. 2010. Decapping activators in Saccharomyces cerevisiae act by multiple mechanisms. Mol. Cell 39:773-783.
35. Noueiry AO, Diez 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. 23:4094-4106.
36. Ramachandran V, Shah KH, Herman PK. 2011. The cAMP-dependent protein kinase signaling pathway is a key regulator of P body foci formation. Mol. Cell 43:973-981.
37. Randall G, et al. 2007. Cellular cofactors affecting hepatitis C virus infection and replication. Proc. Natl. Acad. Sci. U. S. A. 104:12884-12889.
38. Scheller N, 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. U. S. A. 106:13517-13522.
39. Scheller N, et al. 2007. Identification of PatL1, a human homolog to yeast P body component Pat1. Biochim. Biophys. Acta 1773:1786-1792.
40. Teixeira D, Sheth U, Valencia-Sanchez MA, Brengues M, Parker R. 2005. Processing bodies require RNA for assembly and contain nontranslating mRNAs. RNA 11:371-382.
41. Tharun S, Parker R. 2001. Targeting an mRNA for decapping: displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs. Mol. Cell 8:1075-1083.
42. Yang WH, Yu JH, Gulick T, Bloch KD, Bloch DB. 2006. RNA-associated protein 55 (RAP55) localizes to mRNA processing bodies and stress granules. RNA 12:547-554.
43. 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. doi:10.1371/ journal.ppat.1002303.
44. Zhai Y, et al. 2008. Coordinated changes in mRNA turnover, translation, and RNA processing bodies in bronchial epithelial cells following inflammatory stimulation. Mol. Cell. Biol. 28:7414-7426.
45. Zhong J, et al. 2006. Persistent hepatitis C virus infection in vitro: coevolution of virus and host. J. Virol. 80:11082-11093.