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CHD3 facilitates vRNP nuclear export by interacting with NES1 of influenza A virus NS2
NS2 from influenza A virus mediates Crm1-dependent vRNP nuclear export through interaction with Crm1. However, even though the nuclear export signal 1 (NES1) of NS2 does not play a requisite role in NS2–Crm1 interaction, there is no doubt that NES1 is crucial for vRNP nuclear export. While the mecha...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Basel
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4323543/ https://www.ncbi.nlm.nih.gov/pubmed/25213355 http://dx.doi.org/10.1007/s00018-014-1726-9 |
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author | Hu, Yong Liu, Xiaokun Zhang, Anding Zhou, Hongbo Liu, Ziduo Chen, Huanchun Jin, Meilin |
author_facet | Hu, Yong Liu, Xiaokun Zhang, Anding Zhou, Hongbo Liu, Ziduo Chen, Huanchun Jin, Meilin |
author_sort | Hu, Yong |
collection | PubMed |
description | NS2 from influenza A virus mediates Crm1-dependent vRNP nuclear export through interaction with Crm1. However, even though the nuclear export signal 1 (NES1) of NS2 does not play a requisite role in NS2–Crm1 interaction, there is no doubt that NES1 is crucial for vRNP nuclear export. While the mechanism of the NES1 is still unclear, it is speculated that certain host partners might mediate the NES1 function through their interaction with NES1. In the present study, chromodomain-helicase-DNA-binding protein 3 (CHD3) was identified as a novel host nuclear protein for locating NS2 and Crm1 on dense chromatin for NS2 and Crm1-dependent vRNP nuclear export. CHD3 was confirmed to interact with NES1 in NS2, and a disruption to this interaction by mutation in NES1 significantly delayed viral vRNPs export and viral propagation. Further, the knockdown of CHD3 would affect the propagation of the wild-type virus but not the mutant with the weakened NS2–CHD3 interaction. Therefore, this study demonstrates that NES1 is required for maximal binding of NS2 to CHD3, and that the NS2–CHD3 interaction on the dense chromatin contributed to the NS2-mediated vRNP nuclear export. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s00018-014-1726-9) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-4323543 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Springer Basel |
record_format | MEDLINE/PubMed |
spelling | pubmed-43235432015-02-18 CHD3 facilitates vRNP nuclear export by interacting with NES1 of influenza A virus NS2 Hu, Yong Liu, Xiaokun Zhang, Anding Zhou, Hongbo Liu, Ziduo Chen, Huanchun Jin, Meilin Cell Mol Life Sci Research Article NS2 from influenza A virus mediates Crm1-dependent vRNP nuclear export through interaction with Crm1. However, even though the nuclear export signal 1 (NES1) of NS2 does not play a requisite role in NS2–Crm1 interaction, there is no doubt that NES1 is crucial for vRNP nuclear export. While the mechanism of the NES1 is still unclear, it is speculated that certain host partners might mediate the NES1 function through their interaction with NES1. In the present study, chromodomain-helicase-DNA-binding protein 3 (CHD3) was identified as a novel host nuclear protein for locating NS2 and Crm1 on dense chromatin for NS2 and Crm1-dependent vRNP nuclear export. CHD3 was confirmed to interact with NES1 in NS2, and a disruption to this interaction by mutation in NES1 significantly delayed viral vRNPs export and viral propagation. Further, the knockdown of CHD3 would affect the propagation of the wild-type virus but not the mutant with the weakened NS2–CHD3 interaction. Therefore, this study demonstrates that NES1 is required for maximal binding of NS2 to CHD3, and that the NS2–CHD3 interaction on the dense chromatin contributed to the NS2-mediated vRNP nuclear export. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s00018-014-1726-9) contains supplementary material, which is available to authorized users. Springer Basel 2014-09-12 2015 /pmc/articles/PMC4323543/ /pubmed/25213355 http://dx.doi.org/10.1007/s00018-014-1726-9 Text en © The Author(s) 2014 https://creativecommons.org/licenses/by/4.0/ Open AccessThis article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited. |
spellingShingle | Research Article Hu, Yong Liu, Xiaokun Zhang, Anding Zhou, Hongbo Liu, Ziduo Chen, Huanchun Jin, Meilin CHD3 facilitates vRNP nuclear export by interacting with NES1 of influenza A virus NS2 |
title | CHD3 facilitates vRNP nuclear export by interacting with NES1 of influenza A virus NS2 |
title_full | CHD3 facilitates vRNP nuclear export by interacting with NES1 of influenza A virus NS2 |
title_fullStr | CHD3 facilitates vRNP nuclear export by interacting with NES1 of influenza A virus NS2 |
title_full_unstemmed | CHD3 facilitates vRNP nuclear export by interacting with NES1 of influenza A virus NS2 |
title_short | CHD3 facilitates vRNP nuclear export by interacting with NES1 of influenza A virus NS2 |
title_sort | chd3 facilitates vrnp nuclear export by interacting with nes1 of influenza a virus ns2 |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4323543/ https://www.ncbi.nlm.nih.gov/pubmed/25213355 http://dx.doi.org/10.1007/s00018-014-1726-9 |
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