Abstract:
:Nipah virus (NiV) causes severe encephalitis in humans, with high mortality. NiV nonstructural C protein (NiV-C) is essential for its pathogenicity, but its functions are unclear. In this study, we focused on NiV-C trafficking in cells and found that it localizes predominantly in the cytoplasm but partly in the nucleus. An analysis of NiV-C mutants showed that amino acids 2, 21-24 and 110-139 of NiV-C are important for its localization in the cytoplasm. Inhibitor treatment indicates that the nuclear export determinant is not a classical CRM1-dependent nuclear export signal. We also determined that amino acids 60-75 and 72-75 were important for nuclear localization of NiV-C. Furthermore, NiV-C mutants that had lost their capacity for nuclear localization inhibited the interferon (IFN) response more strongly than complete NiV-C. These results indicate that the IFN-antagonist activity of NiV-C occurs in the cytoplasm.
journal_name
Virologyjournal_title
Virologyauthors
Horie R,Yoneda M,Uchida S,Sato H,Kai Cdoi
10.1016/j.virol.2016.07.013subject
Has Abstractpub_date
2016-10-01 00:00:00pages
294-304eissn
0042-6822issn
1096-0341pii
S0042-6822(16)30180-5journal_volume
497pub_type
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