Protein & Cell

, Volume 1, Issue 10, pp 956–964

DEXH-Box protein DHX30 is required for optimal function of the zinc-finger antiviral protein

  • Peiying Ye
  • Shufeng Liu
  • Yiping Zhu
  • Guifang Chen
  • Guangxia Gao
Research Article

DOI: 10.1007/s13238-010-0117-8

Cite this article as:
Ye, P., Liu, S., Zhu, Y. et al. Protein Cell (2010) 1: 956. doi:10.1007/s13238-010-0117-8

Abstract

The zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses by eliminating viral mRNAs in the cytoplasm. In previous studies, we demonstrated that ZAP directly binds to the viral mRNAs and recruits the RNA exosome to degrade the target RNA. In this article, we provide evidence that a DEXH box RNA helicase, DHX30, is required for optimal antiviral activity of ZAP. Pull-down and co-immunoprecipitation assays demonstrated that DHX30 and ZAP interacted with each other via their N terminal domains. Downregulation of DHX30 with shRNAs reduced ZAP’s antiviral activity. These data implicate that DHX30 is a cellular factor involved in the antiviral function of ZAP.

Keywords

zinc-finger antiviral proteinRNA helicaseDHX30

Copyright information

© Higher Education Press and Springer-Verlag Berlin Heidelberg 2010

Authors and Affiliations

  • Peiying Ye
    • 1
    • 2
  • Shufeng Liu
    • 1
  • Yiping Zhu
    • 1
    • 2
  • Guifang Chen
    • 1
  • Guangxia Gao
    • 1
  1. 1.Center for Infection and Immunity, Institute of BiophysicsChinese Academy of SciencesBeijingChina
  2. 2.Graduate School of Chinese Academy of SciencesBeijingChina