An inhibitory function of WW domain-containing host proteins in RNA virus replication

Jun Qin, Daniel Barajas, Peter D. Nagy

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

To identify new genes affecting Tomato bushy stunt virus (TBSV) replication in yeast model host, we are studying protein families, whose members have been identified during previous high throughput screening. In this paper, we have characterized the WW domain-containing protein family from yeast and plants. We find that, in addition to Rsp5 E3 ubiquitin ligase, yeast Wwm1 and Prp40 and three Arabidopsis WW domain-containing proteins are strong inhibitors of TBSV replication. The tombusvirus replicase complex isolated from yeast with down-regulated Wwm1 protein level was more active. Accumulation of viral p92pol was reduced when Wwm1 was over-expressed, suggesting that the stability of p92pol might be reduced, as observed with Rsp5. Moreover, replication of two insect RNA viruses is also inhibited by Wwm1 and Rsp5, suggesting that WW domain-containing proteins might have broad regulatory effects on RNA viruses. Thus, artificial antiviral proteins with WW domains could be useful antiviral strategy.

Original languageEnglish
Pages (from-to)106-119
Number of pages14
JournalVirology
Volume426
Issue number2
DOIs
StatePublished - May 10 2012

Bibliographical note

Funding Information:
The authors thank Dr. Judit Pogany for valuable comments. In addition, technical suggestions with FHV and NoV from Dr. J. Pogany are appreciated. This work was supported by the National Science Foundation ( IOB-0517218 ), NIH-NIAID ( 5R21AI079457-02 ) and the Kentucky Tobacco Research and Development Center to PDN.

Keywords

  • Antiviral factor
  • E3 ubiquitin ligase
  • FHV
  • Host-virus interaction
  • NoV
  • Replication
  • Rsp5
  • Tomato bushy stunt virus
  • Viral replicase
  • WW domain
  • Yeast

ASJC Scopus subject areas

  • Virology

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