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Title: Region of Nipah virus C protein responsible for shuttling between the cytoplasm and nucleus

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. -- Highlights: •Nipah virus (NiV) infection resulted in high mortality, but effective treatment has not been established. •Several reports revealed that NiV nonstructural C protein (NiV-C) was essential for NiV pathogenicity, however, whole of NiV-C function is still unknown. •Although nonstructural C proteins of other Paramyxoviruses are expressed in similar mechanism and exert similar activity, subcellular localization and cellular targets aremore » different. In this study, we evaluated the subcellular localization of NiV-C. •To our knowledge, this is the first report showing that NiV-C shuttles between the nucleus and cytoplasm. We also clarified that NiV-C has nuclear export signal and nuclear localization signal using NiV-C deleted, alanine substitution mutants and enhanced green fluorescent protein (EGFP) fused proteins. •And we also showed that interferon (IFN) antagonist activity of NiV-C related to its subcellular localization. Our results indicate that NiV-C exert IFN antagonist activity in the cytoplasm.« less

Authors:
;
Publication Date:
OSTI Identifier:
22692220
Resource Type:
Journal Article
Resource Relation:
Journal Name: Virology; Journal Volume: 497; Other Information: Copyright (c) 2016 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ALANINES; CELL NUCLEI; CYTOPLASM; ENCEPHALITIS; FLUORESCENCE; INTERFERON; MORTALITY; MUTANTS; RABBIT TUBES; VIRUSES

Citation Formats

Horie, Ryo, and Yoneda, Misako, E-mail: yone@ims.u-tok. Region of Nipah virus C protein responsible for shuttling between the cytoplasm and nucleus. United States: N. p., 2016. Web. doi:10.1016/J.VIROL.2016.07.013.
Horie, Ryo, & Yoneda, Misako, E-mail: yone@ims.u-tok. Region of Nipah virus C protein responsible for shuttling between the cytoplasm and nucleus. United States. doi:10.1016/J.VIROL.2016.07.013.
Horie, Ryo, and Yoneda, Misako, E-mail: yone@ims.u-tok. Sat . "Region of Nipah virus C protein responsible for shuttling between the cytoplasm and nucleus". United States. doi:10.1016/J.VIROL.2016.07.013.
@article{osti_22692220,
title = {Region of Nipah virus C protein responsible for shuttling between the cytoplasm and nucleus},
author = {Horie, Ryo and Yoneda, Misako, E-mail: yone@ims.u-tok},
abstractNote = {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. -- Highlights: •Nipah virus (NiV) infection resulted in high mortality, but effective treatment has not been established. •Several reports revealed that NiV nonstructural C protein (NiV-C) was essential for NiV pathogenicity, however, whole of NiV-C function is still unknown. •Although nonstructural C proteins of other Paramyxoviruses are expressed in similar mechanism and exert similar activity, subcellular localization and cellular targets are different. In this study, we evaluated the subcellular localization of NiV-C. •To our knowledge, this is the first report showing that NiV-C shuttles between the nucleus and cytoplasm. We also clarified that NiV-C has nuclear export signal and nuclear localization signal using NiV-C deleted, alanine substitution mutants and enhanced green fluorescent protein (EGFP) fused proteins. •And we also showed that interferon (IFN) antagonist activity of NiV-C related to its subcellular localization. Our results indicate that NiV-C exert IFN antagonist activity in the cytoplasm.},
doi = {10.1016/J.VIROL.2016.07.013},
journal = {Virology},
number = ,
volume = 497,
place = {United States},
year = {Sat Oct 15 00:00:00 EDT 2016},
month = {Sat Oct 15 00:00:00 EDT 2016}
}