Rift Valley fever virus NSs protein functions and the similarity to other bunyavirus NSs proteins

Hoai J. Ly, Tetsuro Ikegami

Research output: Contribution to journalArticlepeer-review

42 Scopus citations


Rift Valley fever is a mosquito-borne zoonotic disease that affects both ruminants and humans. The nonstructural (NS) protein, which is a major virulence factor for Rift Valley fever virus (RVFV), is encoded on the S-segment. Through the cullin 1-Skp1-Fbox E3 ligase complex, the NSs protein promotes the degradation of at least two host proteins, the TFIIH p62 and the PKR proteins. NSs protein bridges the Fbox protein with subsequent substrates, and facilitates the transfer of ubiquitin. The SAP30-YY1 complex also bridges the NSs protein with chromatin DNA, affecting cohesion and segregation of chromatin DNA as well as the activation of interferon-β promoter. The presence of NSs filaments in the nucleus induces DNA damage responses and causes cell-cycle arrest, p53 activation, and apoptosis. Despite the fact that NSs proteins have poor amino acid similarity among bunyaviruses, the strategy utilized to hijack host cells are similar. This review will provide and summarize an update of recent findings pertaining to the biological functions of the NSs protein of RVFV as well as the differences from those of other bunyaviruses.

Original languageEnglish (US)
Article number118
JournalVirology journal
Issue number1
StatePublished - Jul 2 2016


  • Bunyavirus
  • E3 ligase
  • Interferon
  • NSs
  • PKR
  • Phlebovirus
  • Rift Valley fever virus
  • Ubiquitin
  • p53
  • p62

ASJC Scopus subject areas

  • Virology
  • Infectious Diseases


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