期刊
VIROLOGY JOURNAL
卷 13, 期 -, 页码 -出版社
BMC
DOI: 10.1186/s12985-016-0573-8
关键词
Rift Valley fever virus; Phlebovirus; Bunyavirus; NSs; PKR; TFIIH; p62; p53; Ubiquitin; Interferon; E3 ligase
类别
资金
- National Institute of Health [R01 AI087643-01A1]
- Sealy Center for Vaccine Development at The University of Texas Medical Branch at Galveston (UTMB)
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-beta 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.
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