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Porcine DNAJB6 promotes PCV2 replication via enhancing the formation of autophagy in host cells

Hsp40/DnaJ family proteins play important roles in the infection process of various viruses. Porcine DNAJB6 (pDNAJB6) is a major member of this family, but its role in modulating the replication of porcine circovirus type 2 (PCV2) is still unclear. In the present study, pDNAJB6 was found to be signi...

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Autores principales: Han, Cong, Du, Qian, Zhu, Lei, Chen, Nannan, Luo, Le, Chen, Qiao, Yin, Jiatong, Wu, Xingchen, Tong, Dewen, Huang, Yong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7203849/
https://www.ncbi.nlm.nih.gov/pubmed/32381067
http://dx.doi.org/10.1186/s13567-020-00783-z
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author Han, Cong
Du, Qian
Zhu, Lei
Chen, Nannan
Luo, Le
Chen, Qiao
Yin, Jiatong
Wu, Xingchen
Tong, Dewen
Huang, Yong
author_facet Han, Cong
Du, Qian
Zhu, Lei
Chen, Nannan
Luo, Le
Chen, Qiao
Yin, Jiatong
Wu, Xingchen
Tong, Dewen
Huang, Yong
author_sort Han, Cong
collection PubMed
description Hsp40/DnaJ family proteins play important roles in the infection process of various viruses. Porcine DNAJB6 (pDNAJB6) is a major member of this family, but its role in modulating the replication of porcine circovirus type 2 (PCV2) is still unclear. In the present study, pDNAJB6 was found to be significantly upregulated by PCV2 infection, and confirmed to be interacted with PCV2 capsid (Cap) protein and co-localized at both cytoplasm and nucleus in the PCV2-infected cells. Knockout of pDNAJB6 significantly reduced the formation of autophagosomes in PCV2-infected cells or in the cells expressing Cap protein, whereas overexpression of pDNAJB6 showed an opposite effect. In addition, the domain mapping assay showed that the J domain of pDNAJB6 (amino acids (aa) 1–99) and the C terminus of Cap (162-234 aa) were required for the interaction of pDNAJB6 with Cap. Notably, the interaction of pDNAJB6 with Cap was very important to promoting the formation of autophagosomes induced by PCV2 infection or Cap expression and enhancing the replication of PCV2. Taken together, the results presented here show a novel function of pDNAJB6 in regulation of porcine circovirus replication that pDNAJB6 enhances the formation of autophagy to promote viral replication through interacting with viral capsid protein during PCV2 infection.
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spelling pubmed-72038492020-05-09 Porcine DNAJB6 promotes PCV2 replication via enhancing the formation of autophagy in host cells Han, Cong Du, Qian Zhu, Lei Chen, Nannan Luo, Le Chen, Qiao Yin, Jiatong Wu, Xingchen Tong, Dewen Huang, Yong Vet Res Research Article Hsp40/DnaJ family proteins play important roles in the infection process of various viruses. Porcine DNAJB6 (pDNAJB6) is a major member of this family, but its role in modulating the replication of porcine circovirus type 2 (PCV2) is still unclear. In the present study, pDNAJB6 was found to be significantly upregulated by PCV2 infection, and confirmed to be interacted with PCV2 capsid (Cap) protein and co-localized at both cytoplasm and nucleus in the PCV2-infected cells. Knockout of pDNAJB6 significantly reduced the formation of autophagosomes in PCV2-infected cells or in the cells expressing Cap protein, whereas overexpression of pDNAJB6 showed an opposite effect. In addition, the domain mapping assay showed that the J domain of pDNAJB6 (amino acids (aa) 1–99) and the C terminus of Cap (162-234 aa) were required for the interaction of pDNAJB6 with Cap. Notably, the interaction of pDNAJB6 with Cap was very important to promoting the formation of autophagosomes induced by PCV2 infection or Cap expression and enhancing the replication of PCV2. Taken together, the results presented here show a novel function of pDNAJB6 in regulation of porcine circovirus replication that pDNAJB6 enhances the formation of autophagy to promote viral replication through interacting with viral capsid protein during PCV2 infection. BioMed Central 2020-05-07 2020 /pmc/articles/PMC7203849/ /pubmed/32381067 http://dx.doi.org/10.1186/s13567-020-00783-z Text en © The Author(s) 2020 Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.
spellingShingle Research Article
Han, Cong
Du, Qian
Zhu, Lei
Chen, Nannan
Luo, Le
Chen, Qiao
Yin, Jiatong
Wu, Xingchen
Tong, Dewen
Huang, Yong
Porcine DNAJB6 promotes PCV2 replication via enhancing the formation of autophagy in host cells
title Porcine DNAJB6 promotes PCV2 replication via enhancing the formation of autophagy in host cells
title_full Porcine DNAJB6 promotes PCV2 replication via enhancing the formation of autophagy in host cells
title_fullStr Porcine DNAJB6 promotes PCV2 replication via enhancing the formation of autophagy in host cells
title_full_unstemmed Porcine DNAJB6 promotes PCV2 replication via enhancing the formation of autophagy in host cells
title_short Porcine DNAJB6 promotes PCV2 replication via enhancing the formation of autophagy in host cells
title_sort porcine dnajb6 promotes pcv2 replication via enhancing the formation of autophagy in host cells
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7203849/
https://www.ncbi.nlm.nih.gov/pubmed/32381067
http://dx.doi.org/10.1186/s13567-020-00783-z
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