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Host factor SMYD3 is recruited by Ebola virus nucleoprotein to facilitate viral mRNA transcription
The polymerase complex of Ebola virus (EBOV) is the functional unit for transcription and replication of viral genome. Nucleoprotein (NP) is a multifunctional protein with high RNA binding affinity and recruits other viral proteins to form functional polymerase complex. In our study, we investigated...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6758638/ https://www.ncbi.nlm.nih.gov/pubmed/31516086 http://dx.doi.org/10.1080/22221751.2019.1662736 |
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author | Chen, Jingliang He, Zhangping Yuan, Yaochang Huang, Feng Luo, Baohong Zhang, Jianhua Pan, Ting Zhang, Hui Zhang, Junsong |
author_facet | Chen, Jingliang He, Zhangping Yuan, Yaochang Huang, Feng Luo, Baohong Zhang, Jianhua Pan, Ting Zhang, Hui Zhang, Junsong |
author_sort | Chen, Jingliang |
collection | PubMed |
description | The polymerase complex of Ebola virus (EBOV) is the functional unit for transcription and replication of viral genome. Nucleoprotein (NP) is a multifunctional protein with high RNA binding affinity and recruits other viral proteins to form functional polymerase complex. In our study, we investigated host proteins associated with EBOV polymerase complex using NP as bait in a transcription and replication competent minigenome system by mass spectrometry analysis and identified SET and MYND domain-containing protein 3 (SMYD3) as a novel host protein which was required for the replication of EBOV. SMYD3 specifically interacted with NP and was recruited to EBOV inclusion bodies through NP. The depletion of SMYD3 dramatically suppressed EBOV mRNA production. A mimic of non-phosphorylated VP30, which is a transcription activator, could partially rescue the viral mRNA production downregulated by the depletion of SMYD3. In addition, SMYD3 promoted NP-VP30 interaction in a dose-dependent manner. These results revealed that SMYD3 was a novel host factor recruited by NP to supporting EBOV mRNA transcription through increasing the binding of VP30 to NP. Thus, our study provided a new understanding of mechanism underlying the transcription of EBOV genome, and a novel anti-EBOV drug design strategy by targeting SMYD3. |
format | Online Article Text |
id | pubmed-6758638 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Taylor & Francis |
record_format | MEDLINE/PubMed |
spelling | pubmed-67586382019-10-09 Host factor SMYD3 is recruited by Ebola virus nucleoprotein to facilitate viral mRNA transcription Chen, Jingliang He, Zhangping Yuan, Yaochang Huang, Feng Luo, Baohong Zhang, Jianhua Pan, Ting Zhang, Hui Zhang, Junsong Emerg Microbes Infect Original Articles The polymerase complex of Ebola virus (EBOV) is the functional unit for transcription and replication of viral genome. Nucleoprotein (NP) is a multifunctional protein with high RNA binding affinity and recruits other viral proteins to form functional polymerase complex. In our study, we investigated host proteins associated with EBOV polymerase complex using NP as bait in a transcription and replication competent minigenome system by mass spectrometry analysis and identified SET and MYND domain-containing protein 3 (SMYD3) as a novel host protein which was required for the replication of EBOV. SMYD3 specifically interacted with NP and was recruited to EBOV inclusion bodies through NP. The depletion of SMYD3 dramatically suppressed EBOV mRNA production. A mimic of non-phosphorylated VP30, which is a transcription activator, could partially rescue the viral mRNA production downregulated by the depletion of SMYD3. In addition, SMYD3 promoted NP-VP30 interaction in a dose-dependent manner. These results revealed that SMYD3 was a novel host factor recruited by NP to supporting EBOV mRNA transcription through increasing the binding of VP30 to NP. Thus, our study provided a new understanding of mechanism underlying the transcription of EBOV genome, and a novel anti-EBOV drug design strategy by targeting SMYD3. Taylor & Francis 2019-09-13 /pmc/articles/PMC6758638/ /pubmed/31516086 http://dx.doi.org/10.1080/22221751.2019.1662736 Text en © 2019 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group, on behalf of Shanghai Shangyixun Cultural Communication Co., Ltd https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Articles Chen, Jingliang He, Zhangping Yuan, Yaochang Huang, Feng Luo, Baohong Zhang, Jianhua Pan, Ting Zhang, Hui Zhang, Junsong Host factor SMYD3 is recruited by Ebola virus nucleoprotein to facilitate viral mRNA transcription |
title | Host factor SMYD3 is recruited by Ebola virus nucleoprotein to facilitate viral mRNA transcription |
title_full | Host factor SMYD3 is recruited by Ebola virus nucleoprotein to facilitate viral mRNA transcription |
title_fullStr | Host factor SMYD3 is recruited by Ebola virus nucleoprotein to facilitate viral mRNA transcription |
title_full_unstemmed | Host factor SMYD3 is recruited by Ebola virus nucleoprotein to facilitate viral mRNA transcription |
title_short | Host factor SMYD3 is recruited by Ebola virus nucleoprotein to facilitate viral mRNA transcription |
title_sort | host factor smyd3 is recruited by ebola virus nucleoprotein to facilitate viral mrna transcription |
topic | Original Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6758638/ https://www.ncbi.nlm.nih.gov/pubmed/31516086 http://dx.doi.org/10.1080/22221751.2019.1662736 |
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