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A furoviral replicase recruits host HSP70 to membranes for viral RNA replication
Many host factors have been identified to be involved in viral infection. However, although furoviruses cause important diseases of cereals worldwide, no host factors have yet been identified that interact with furoviral genes or participate in the viral infection cycle. In this study, both TaHSP70...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5377427/ https://www.ncbi.nlm.nih.gov/pubmed/28367995 http://dx.doi.org/10.1038/srep45590 |
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author | Yang, Jian Zhang, Fen Cai, Nian-Jun Wu, Ne Chen, Xuan Li, Jing Meng, Xiang-Feng Zhu, Tong-Quan Chen, Jian-Ping Zhang, Heng-Mu |
author_facet | Yang, Jian Zhang, Fen Cai, Nian-Jun Wu, Ne Chen, Xuan Li, Jing Meng, Xiang-Feng Zhu, Tong-Quan Chen, Jian-Ping Zhang, Heng-Mu |
author_sort | Yang, Jian |
collection | PubMed |
description | Many host factors have been identified to be involved in viral infection. However, although furoviruses cause important diseases of cereals worldwide, no host factors have yet been identified that interact with furoviral genes or participate in the viral infection cycle. In this study, both TaHSP70 and NbHSP70 were up-regulated in Chinese wheat mosaic furovirus (CWMV)-infected plants. Their overexpression and inhibition were correlated with the accumulation of viral genomic RNAs, suggesting that the HSP70 genes could be necessary for CWMV infection. The subcellular distributions of TaHSP70 and NbHSP70 were significantly affected by CWMV infection or by infiltration of RNA1 alone. Further assays showed that the viral replicase encoded by CWMV RNA1 interacts with both TaHSP70 and NbHSP70 in vivo and vitro and that its region aa167–333 was responsible for the interaction. Subcellular assays showed that the viral replicase could recruit both TaHSP70 and NbHSP70 from the cytoplasm or nucleus to the granular aggregations or inclusion-like structures on the intracellular membrane system, suggesting that both HSP70s may be recruited into the viral replication complex (VRC) to promote furoviral replication. This is the first host factor identified to be involved in furoviral infection, which extends the list and functional scope of HSP70 chaperones. |
format | Online Article Text |
id | pubmed-5377427 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-53774272017-04-10 A furoviral replicase recruits host HSP70 to membranes for viral RNA replication Yang, Jian Zhang, Fen Cai, Nian-Jun Wu, Ne Chen, Xuan Li, Jing Meng, Xiang-Feng Zhu, Tong-Quan Chen, Jian-Ping Zhang, Heng-Mu Sci Rep Article Many host factors have been identified to be involved in viral infection. However, although furoviruses cause important diseases of cereals worldwide, no host factors have yet been identified that interact with furoviral genes or participate in the viral infection cycle. In this study, both TaHSP70 and NbHSP70 were up-regulated in Chinese wheat mosaic furovirus (CWMV)-infected plants. Their overexpression and inhibition were correlated with the accumulation of viral genomic RNAs, suggesting that the HSP70 genes could be necessary for CWMV infection. The subcellular distributions of TaHSP70 and NbHSP70 were significantly affected by CWMV infection or by infiltration of RNA1 alone. Further assays showed that the viral replicase encoded by CWMV RNA1 interacts with both TaHSP70 and NbHSP70 in vivo and vitro and that its region aa167–333 was responsible for the interaction. Subcellular assays showed that the viral replicase could recruit both TaHSP70 and NbHSP70 from the cytoplasm or nucleus to the granular aggregations or inclusion-like structures on the intracellular membrane system, suggesting that both HSP70s may be recruited into the viral replication complex (VRC) to promote furoviral replication. This is the first host factor identified to be involved in furoviral infection, which extends the list and functional scope of HSP70 chaperones. Nature Publishing Group 2017-04-03 /pmc/articles/PMC5377427/ /pubmed/28367995 http://dx.doi.org/10.1038/srep45590 Text en Copyright © 2017, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Yang, Jian Zhang, Fen Cai, Nian-Jun Wu, Ne Chen, Xuan Li, Jing Meng, Xiang-Feng Zhu, Tong-Quan Chen, Jian-Ping Zhang, Heng-Mu A furoviral replicase recruits host HSP70 to membranes for viral RNA replication |
title | A furoviral replicase recruits host HSP70 to membranes for viral RNA replication |
title_full | A furoviral replicase recruits host HSP70 to membranes for viral RNA replication |
title_fullStr | A furoviral replicase recruits host HSP70 to membranes for viral RNA replication |
title_full_unstemmed | A furoviral replicase recruits host HSP70 to membranes for viral RNA replication |
title_short | A furoviral replicase recruits host HSP70 to membranes for viral RNA replication |
title_sort | furoviral replicase recruits host hsp70 to membranes for viral rna replication |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5377427/ https://www.ncbi.nlm.nih.gov/pubmed/28367995 http://dx.doi.org/10.1038/srep45590 |
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