Mutational analysis of the functional sites in porcine reproductive and respiratory syndrome virus non-structural protein 10

References

1. Bautista E. M., Faaberg K. S., Mickelson D., McGruder E. D. 2002; Functional properties of the predicted helicase of porcine reproductive and respiratory syndrome virus. Virology 298:258–270 [View Article][PubMed]
   [Google Scholar]
2. Cao W., Coman M. M., Ding S., Henn A., Middleton E. R., Bradley M. J., Rhoades E., Hackney D. D., Pyle A. M., De La Cruz E. M. 2011; Mechanism of Mss116 ATPase reveals functional diversity of DEAD-box proteins. J Mol Biol 409:399–414 [View Article][PubMed]
   [Google Scholar]
3. Deng Z., Lehmann K. C., Li X., Feng C., Wang G., Zhang Q., Qi X., Yu L., Zhang X.other authors 2014; Structural basis for the regulatory function of a complex zinc-binding domain in a replicative arterivirus helicase resembling a nonsense-mediated mRNA decay helicase. Nucleic Acids Res 42:3464–3477 [View Article][PubMed]
   [Google Scholar]
4. Fang Y., Snijder E. J. 2010; The PRRSV replicase: exploring the multifunctionality of an intriguing set of nonstructural proteins. Virus Res 154:61–76 [View Article][PubMed]
   [Google Scholar]
5. Fang J., Li H., Peng G., Cao S., Zhen F. F., Chen H., Song Y. 2013; Methods for detecting ATP hydrolysis and nucleic acid unwinding of Japanese encephalitis virus NS3 helicase. J Virol Methods 194:33–38 [View Article][PubMed]
   [Google Scholar]
6. Gilhooly N. S., Gwynn E. J., Dillingham M. S. 2013; Superfamily 1 helicases. Front Biosci (Schol Ed) 5:206–216[PubMed]
   [Google Scholar]
7. Henn A., Cao W., Hackney D. D., De La Cruz E. M. 2008; The ATPase cycle mechanism of the DEAD-box rRNA helicase, DbpA. J Mol Biol 377:193–205 [View Article][PubMed]
   [Google Scholar]
8. Henn A., Cao W., Licciardello N., Heitkamp S. E., Hackney D. D., De La Cruz E. M. 2010; Pathway of ATP utilization and duplex rRNA unwinding by the DEAD-box helicase, DbpA. Proc Natl Acad Sci U S A 107:4046–4050 [View Article][PubMed]
   [Google Scholar]
9. Henn A., Bradley M. J., De La Cruz E. M. 2012; ATP utilization and RNA conformational rearrangement by DEAD-box proteins. Annu Rev Biophys 41:247–267 [View Article][PubMed]
   [Google Scholar]
10. Ho S. N., Hunt H. D., Horton R. M., Pullen J. K., Pease L. R. 1989; Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51–59 [View Article][PubMed]
    [Google Scholar]
11. Jankowsky E. 2011; RNA helicases at work: binding and rearranging. Trends Biochem Sci 36:19–29 [View Article][PubMed]
    [Google Scholar]
12. Leng X., Li Z., Xia M., Li X., Wang F., Wang W., Zhang X., Wu H. 2012; Mutations in the genome of the highly pathogenic porcine reproductive and respiratory syndrome virus potentially related to attenuation. Vet Microbiol 157:50–60 [View Article][PubMed]
    [Google Scholar]
13. Li Y., Xue C., Wang L., Chen X., Chen F., Cao Y. 2010; Genomic analysis of two Chinese strains of porcine reproductive and respiratory syndrome viruses with different virulence. Virus Genes 40:374–381 [View Article][PubMed]
    [Google Scholar]
14. Li Y., Zhou L., Zhang J., Ge X., Zhou R., Zheng H., Geng G., Guo X., Yang H. 2014; Nsp9 and Nsp10 contribute to the fatal virulence of highly pathogenic porcine reproductive and respiratory syndrome virus emerging in China. PLoS Pathog 10:e1004216 [View Article][PubMed]
    [Google Scholar]
15. Music N., Gagnon C. A. 2010; The role of porcine reproductive and respiratory syndrome (PRRS) virus structural and non-structural proteins in virus pathogenesis. Anim Health Res Rev 11:135–163 [View Article][PubMed]
    [Google Scholar]
16. Seybert A., van Dinten L. C., Snijder E. J., Ziebuhr J. 2000; Biochemical characterization of the equine arteritis virus helicase suggests a close functional relationship between arterivirus and coronavirus helicases. J Virol 74:9586–9593 [View Article][PubMed]
    [Google Scholar]
17. Seybert A., Posthuma C. C., van Dinten L. C., Snijder E. J., Gorbalenya A. E., Ziebuhr J. 2005; A complex zinc finger controls the enzymatic activities of nidovirus helicases. J Virol 79:696–704 [View Article][PubMed]
    [Google Scholar]
18. Snijder E. J., Kikkert M., Fang Y. 2013; Arterivirus molecular biology and pathogenesis. J Gen Virol 94:2141–2163 [View Article][PubMed]
    [Google Scholar]
19. Tian K., Yu X., Zhao T., Feng Y., Cao Z., Wang C., Hu Y., Chen X., Hu D.other authors 2007; Emergence of fatal PRRSV variants: unparalleled outbreaks of atypical PRRS in China and molecular dissection of the unique hallmark. PLoS ONE 2:e526 [View Article][PubMed]
    [Google Scholar]
20. van Dinten L. C., den Boon J. A., Wassenaar A. L., Spaan W. J., Snijder E. J. 1997; An infectious arterivirus cDNA clone: identification of a replicase point mutation that abolishes discontinuous mRNA transcription. Proc Natl Acad Sci U S A 94:991–996 [View Article][PubMed]
    [Google Scholar]
21. van Dinten L. C., van Tol H., Gorbalenya A. E., Snijder E. J. 2000; The predicted metal-binding region of the arterivirus helicase protein is involved in subgenomic mRNA synthesis, genome replication, and virion biogenesis. J Virol 74:5213–5223 [View Article][PubMed]
    [Google Scholar]
22. van Marle G., van Dinten L. C., Spaan W. J., Luytjes W., Snijder E. J. 1999; Characterization of an equine arteritis virus replicase mutant defective in subgenomic mRNA synthesis. J Virol 73:5274–5281[PubMed]
    [Google Scholar]
23. Yu M. S., Lee J., Lee J. M., Kim Y., Chin Y. W., Jee J. G., Keum Y. S., Jeong Y. J. 2012; Identification of myricetin and scutellarein as novel chemical inhibitors of the SARS coronavirus helicase, nsP13. Bioorg Med Chem Lett 22:4049–4054 [View Article][PubMed]
    [Google Scholar]
24. Zhou L., Zhang J., Zeng J., Yin S., Li Y., Zheng L., Guo X., Ge X., Yang H. 2009; The 30-amino-acid deletion in the Nsp2 of highly pathogenic porcine reproductive and respiratory syndrome virus emerging in China is not related to its virulence. J Virol 83:5156–5167 [View Article][PubMed]
    [Google Scholar]