The ubiquitin-proteasome system is required for the early stages of porcine circovirus type 2 replication

Virology

Volumn 456-457, Issue 1, 2014, Pages 198-204

  Cheng, Shuang ^a   Yan, Weidong ^a   Gu, Wei ^a   He, Qigai ^a  

^a HUAZHONG AGRICULTURAL UNIVERSITY   (China)

Author keywords

Lactacystin; MG132; PCV2; PK15 cells; UPS; Viral replication

Indexed keywords

LACTACYSTIN; MG132; PCV2; PK15 CELLS; UPS; VIRAL REPLICATION;

ANIMALS; CELL LINE; CIRCOVIRUS; HOST-PATHOGEN INTERACTIONS; PROTEASOME ENDOPEPTIDASE COMPLEX; SWINE; UBIQUITIN; VIRAL LOAD; VIRUS REPLICATION;

EID: 84898626930     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2014.03.028     Document Type: Article

References (47)

1. Allan G.M., Kennedy S., McNeilly F., Foster J.C., Ellis J.A., Krakowka S.J., Meehan B.M., Adair B.M. Experimental reproduction of severe wasting disease by co-infection of pigs with porcine circovirus and porcine parvovirus. J. Comp. Pathol. 1999, 121(1):1-11.
2. Bres V., Kiernan R.E., Linares L.K., Chable-Bessia C., Plechakova O., Tréand C., Emiliani S., Peloponese J.-M., Jeang K.-T., Coux O. A non-proteolytic role for ubiquitin in Tat-mediated transactivation of the HIV-1 promoter. Nat. Cell Biol. 2003, 5(8):754-761.
3. Chae C. A review of porcine circovirus 2-associated syndromes and diseases. Vet. J. 2005, 169(3):326-336.
4. Chen Z., Hagler J., Palombella V.J., Melandri F., Scherer D., Ballard D., Maniatis T. Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway. Genes Dev. 1995, 9(13):1586-1597.
5. Cheng S., Zhang M., Li W., Wang Y., Liu Y., He Q. Proteomic analysis of porcine alveolar macrophages infected with porcine circovirus type 2. J. Proteomics 2012, 75(11):3258-3269.
6. Ciechanover A. The ubiquitin-proteasome proteolytic pathway. Cell 1994, 79(1):13-21.
7. Ciechanover A., Iwai K. The ubiquitin system: from basic mechanisms to the patient bed. IUBMB Life 2004, 56(4):193-201.
8. Cino-Ozuna A.G., Henry S., Hesse R., Nietfeld J.C., Bai J., Scott H.M., Rowland R.R. Characterization of a new disease syndrome associated with porcine circovirus type 2 in previously vaccinated herds. J. Clin. Microbiol. 2011, 49(5):2012-2016.
9. Ehlers M.D. Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system. Nat. Neurosci. 2003, 6(3):231-242.
10. Faurez F., Dory D., Grasland B., Jestin A. Replication of porcine circoviruses. Virol. J. 2009, 6:60.
11. Fernandez-Garcia M.D., Meertens L., Bonazzi M., Cossart P., Arenzana-Seisdedos F., Amara A. Appraising the roles of CBLL1 and the ubiquitin/proteasome system for flavivirus entry and replication. J. Virol. 2011, 85(6):2980-2989.
12. Gao G., Luo H. The ubiquitin-proteasome pathway in viral infections. Can. J. Physiol. Pharmacol. 2006, 84(1):5-14.
13. Glotzer M., Murray A.W., Kirschner M.W. Cyclin is degraded by the ubiquitin pathway. Nature 1991, 349(6305):132-138.
14. Han Y.H., Moon H.J., You B.R., Park W.H. The effect of MG132, a proteasome inhibitor on HeLa cells in relation to cell growth, reactive oxygen species and GSH. Oncol. Rep. 2009, 22(1):215-221.
15. Harms P.A., Sorden S.D., Halbur P.G., Bolin S.R., Lager K.M., Morozov I., Paul P.S. Experimental reproduction of severe disease in CD/CD pigs concurrently infected with type 2 porcine circovirus and porcine reproductive and respiratory syndrome virus. Vet. Pathol. 2001, 38(5):528-539.
16. Hershko A., Ciechanover A. The ubiquitin system for protein degradation. Annu. Rev. Biochem. 1992, 61:761-807.
17. Jentsch S., McGrath J.P., Varshavsky A. The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme. Nature 1987, 329(6135):131-134.
18. Karpe Y.A., Meng X.J. Hepatitis E virus replication requires an active ubiquitin-proteasome system. J. Virol. 2012, 86(10):5948-5952.
19. Klinger P.P., Schubert U. The ubiquitin-proteasome system in HIV replication: potential targets for antiretroviral therapy. Expert Rev. Anti-infect. Ther. 2005, 3(1):61-79.
20. Li, Z., Xu, X., Huang, Y., Ding, L., Wang, Z., Yu, G., Xu, D., Li, W., Tong, D., 2012. Swainsonine activates mitochondria-mediated apoptotic pathway in human lung cancer A549 cells and retards the growth of lung cancer xenografts. Int. J. Biol. Sci. 8 (3), 394-405.
21. Liu J., Zhu Y., Chen I., Lau J., He F., Lau A., Wang Z., Karuppannan A.K., Kwang J. The ORF3 protein of porcine circovirus type 2 interacts with porcine ubiquitin E3 ligase Pirh2 and facilitates p53 expression in viral infection. J. Virol. 2007, 81(17):9560-9567.
22. Lopez T., Silva-Ayala D., Lopez S., Arias C.F. Replication of the rotavirus genome requires an active ubiquitin-proteasome system. J. Virol. 2011, 85(22):11964-11971.
23. Luo H., Zhang J., Cheung C., Suarez A., McManus B.M., Yang D. Proteasome inhibition reduces coxsackievirus B3 replication in murine cardiomyocytes. Am. J. Pathol. 2003, 163(2):381-385.
24. Michalek M.T., Grant E.P., Gramm C., Goldberg A.L., Rock K.L. A role for the ubiquitin-dependent proteolytic pathway in MHC class I-restricted antigen presentation. Nature 1993, 363(6429):552-554.
25. Mukhopadhyay D., Riezman H. Proteasome-independent functions of ubiquitin in endocytosis and signaling. Science 2007, 315(5809):201-205.
26. Opriessnig T., Thacker E.L., Yu S., Fenaux M., Meng X.J., Halbur P.G. Experimental reproduction of postweaning multisystemic wasting syndrome in pigs by dual infection with Mycoplasma hyopneumoniae and porcine circovirus type 2. Vet. Pathol. 2004, 41(6):624-640.
27. Pagano M., Tam S.W., Theodoras A.M., Beer-Romero P., Del Sal G., Chau V., Yew P.R., Draetta G.F., Rolfe M. Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27. Science 1995, 269(5224):682-685.
28. Palombella V.J., Rando O.J., Goldberg A.L., Maniatis T. The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B. Cell 1994, 78(5):773-785.
29. Patrick G.N., Zhou P., Kwon Y.T., Howley P.M., Tsai L.-H. p35, the neuronal-specific activator of cyclin-dependent kinase 5 (Cdk5) is degraded by the ubiquitin-proteasome pathway. J. Biol. Chem. 1998, 273(37):24057-24064.
30. Raaben M., Posthuma C.C., Verheije M.H.,Lintelo E.G., Kikkert M., Drijfhout J.W., Snijder E.J., Rottier P.J., de Haan C.A. The ubiquitin-proteasome system plays an important role during various stages of the coronavirus infection cycle. J. Virology 2010, 84(15):7869-7879.
31. Ramos-Vara J.A., Duran O., Render J.A., Craft D. Porcine dermatitis and nephropathy syndrome in the USA. Vet. Rec. 1997, 141(18):479-480.
32. Randow F., Lehner P.J. Viral avoidance and exploitation of the ubiquitin system. Nat. Cell Biol. 2009, 11(5):527-534.
33. Rock K.L., Gramm C., Rothstein L., Clark K., Stein R., Dick L., Hwang D., Goldberg A.L. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 1994, 78(5):761-771.
34. Rosell C., Segalés J., Plana-Duran J., Balasch M., Rodriguez-Arrioja G., Kennedy S., Allan G., McNeilly F., Latimer K., Domingo M. Pathological, immunohistochemical, and in-situ hybridization studies of natural cases of postweaning multisystemic wasting syndrome (PMWS) in pigs. J. Comp. Pathol. 1999, 120(1):59-78.
35. Sakurai A., Yasuda J., Takano H., Tanaka Y., Hatakeyama M., Shida H. Regulation of human T-cell leukemia virus type 1 (HTLV-1) budding by ubiquitin ligase Nedd4. Microbes Infect. 2004, 6(2):150-156.
36. Satheshkumar P.S., Anton L.C., Sanz P., Moss B. Inhibition of the ubiquitin-proteasome system prevents vaccinia virus DNA replication and expression of intermediate and late genes. J. Virol. 2009, 83(6):2469-2479.
37. Segales J., Sitjar M., Domingo M., Dee S., Del Pozo M., Noval R., Sacristan C., De las Heras A., Ferro A., Latimer K.S. First report of post-weaning multisystemic wasting syndrome in pigs in Spain. Vet. Rec. 1997, 141(23):600-601.
38. Shackelford J., Pagano J.S. Targeting of host-cell ubiquitin pathways by viruses. Essays Biochem. 2005, 41:139-156.
39. Si X., Gao G., Wong J., Wang Y., Zhang J., Luo H. Ubiquitination is required for effective replication of coxsackievirus B3. PLoS One 2008, 3(7):e2585.
40. Tischer I., Peters D., Rasch R., Pociuli S. Replication of porcine circovirus: induction by glucosamine and cell cycle dependence. Arch. Virol. 1987, 96(1-2):39-57.
41. Varshavsky A. Regulated protein degradation. Trends Biochem. Sci. 2005, 30(6):283-286.
42. Wang Z., Ni J., Li J., Shi B., Xu Y., Yuan Z. Inhibition of hepatitis B virus replication by cIAP2 involves accelerating the ubiquitin-proteasome-mediated destruction of polymerase. J. Virol. 2011, 85(21):11457-11467.
43. Widjaja I., de Vries E., Tscherne D.M., García-Sastre A., Rottier P.J., de Haan C.A. Inhibition of the ubiquitin-proteasome system affects influenza A virus infection at a postfusion step. J. Virol. 2010, 84(18):9625-9631.
44. Wong E., Cuervo A.M. Integration of clearance mechanisms: the proteasome and autophagy. Cold Spring Harb. Perspect. Biol. 2010, 2(12):a006734.
45. Yang K., Li W., Niu H., Yan W., Liu X., Wang Y., Cheng S., Ku X., He Q. Efficacy of single dose of an inactivated porcine circovirus type 2 (PCV2) whole-virus vaccine with oil adjuvant in piglets. Acta Vet. Scand. 2012, 54:67.
46. Zanotto-Filho A., Delgado-Canedo A., Schroder R., Becker M., Klamt F., Moreira J.C. The pharmacological NFkappaB inhibitors BAY117082 and MG132 induce cell arrest and apoptosis in leukemia cells through ROS-mitochondria pathway activation. Cancer Lett. 2010, 288(2):192-203.
47. Zhu Q., Yao J., Wani G., Chen J., Wang Q.-E., Wani A.A. The ubiquitin-proteasome pathway is required for the function of the viral VP16 transcriptional activation domain. FEBS Lett. 2004, 556(1):19-25.