The Involvement of Histone H3 Acetylation in Bovine Herpesvirus 1 Replication in MDBK Cells
During bovine herpesvirus 1 (BoHV-1) productive infection in cell cultures, partial of intranuclear viral DNA is present in nucleosomes, and viral protein VP22 associates with histones and decreases histone H4 acetylation, indicating the involvement of histone H4 acetylation in virus replication. In...
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doaj-edfebd39a5f54f069d4fb64e2fa15cc82020-11-24T20:51:44ZengMDPI AGViruses1999-49152018-09-01101052510.3390/v10100525v10100525The Involvement of Histone H3 Acetylation in Bovine Herpesvirus 1 Replication in MDBK CellsLiqian Zhu0Xinyi Jiang1Xiaotian Fu2Yanhua Qi3Guoqiang Zhu4College of Veterinary Medicine, Yangzhou University, Yangzhou 225009, ChinaCollege of Veterinary Medicine, Yangzhou University, Yangzhou 225009, ChinaCollege of Veterinary Medicine, Yangzhou University, Yangzhou 225009, ChinaCollege of Life Science, Zhengzhou University, Zhengzhou 450066, ChinaCollege of Veterinary Medicine, Yangzhou University, Yangzhou 225009, ChinaDuring bovine herpesvirus 1 (BoHV-1) productive infection in cell cultures, partial of intranuclear viral DNA is present in nucleosomes, and viral protein VP22 associates with histones and decreases histone H4 acetylation, indicating the involvement of histone H4 acetylation in virus replication. In this study, we demonstrated that BoHV-1 infection at the late stage (at 24 h after infection) dramatically decreased histone H3 acetylation [at residues K9 (H3K9ac) and K18 (H3K18ac)], which was supported by the pronounced depletion of histone acetyltransferases (HATs) including CBP/P300 (CREB binding protein and p300), GCN5L2 (general control of amino acid synthesis yeast homolog like 2) and PCAF (P300/CBP-associated factor). The depletion of GCN5L2 promoted by virus infection was partially mediated by ubiquitin-proteasome pathway. Interestingly, the viral replication was enhanced by HAT (histone acetyltransferase) activator CTPB [N-(4-Chloro-3-trifluoromethylphenyl)-2-ethoxy-6-pentadecylbenzamide], and vice versa, inhibited by HAT inhibitor Anacardic acid (AA), suggesting that BoHV-1 may take advantage of histone acetylation for efficient replication. Taken together, we proposed that the HAT-dependent histone H3 acetylation plays an important role in BoHV-1 replication in MDBK (Madin-Darby bovine kidney) cells.http://www.mdpi.com/1999-4915/10/10/525BoHV-1HATHDACproteasomehistone H3 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Liqian Zhu Xinyi Jiang Xiaotian Fu Yanhua Qi Guoqiang Zhu |
spellingShingle |
Liqian Zhu Xinyi Jiang Xiaotian Fu Yanhua Qi Guoqiang Zhu The Involvement of Histone H3 Acetylation in Bovine Herpesvirus 1 Replication in MDBK Cells Viruses BoHV-1 HAT HDAC proteasome histone H3 |
author_facet |
Liqian Zhu Xinyi Jiang Xiaotian Fu Yanhua Qi Guoqiang Zhu |
author_sort |
Liqian Zhu |
title |
The Involvement of Histone H3 Acetylation in Bovine Herpesvirus 1 Replication in MDBK Cells |
title_short |
The Involvement of Histone H3 Acetylation in Bovine Herpesvirus 1 Replication in MDBK Cells |
title_full |
The Involvement of Histone H3 Acetylation in Bovine Herpesvirus 1 Replication in MDBK Cells |
title_fullStr |
The Involvement of Histone H3 Acetylation in Bovine Herpesvirus 1 Replication in MDBK Cells |
title_full_unstemmed |
The Involvement of Histone H3 Acetylation in Bovine Herpesvirus 1 Replication in MDBK Cells |
title_sort |
involvement of histone h3 acetylation in bovine herpesvirus 1 replication in mdbk cells |
publisher |
MDPI AG |
series |
Viruses |
issn |
1999-4915 |
publishDate |
2018-09-01 |
description |
During bovine herpesvirus 1 (BoHV-1) productive infection in cell cultures, partial of intranuclear viral DNA is present in nucleosomes, and viral protein VP22 associates with histones and decreases histone H4 acetylation, indicating the involvement of histone H4 acetylation in virus replication. In this study, we demonstrated that BoHV-1 infection at the late stage (at 24 h after infection) dramatically decreased histone H3 acetylation [at residues K9 (H3K9ac) and K18 (H3K18ac)], which was supported by the pronounced depletion of histone acetyltransferases (HATs) including CBP/P300 (CREB binding protein and p300), GCN5L2 (general control of amino acid synthesis yeast homolog like 2) and PCAF (P300/CBP-associated factor). The depletion of GCN5L2 promoted by virus infection was partially mediated by ubiquitin-proteasome pathway. Interestingly, the viral replication was enhanced by HAT (histone acetyltransferase) activator CTPB [N-(4-Chloro-3-trifluoromethylphenyl)-2-ethoxy-6-pentadecylbenzamide], and vice versa, inhibited by HAT inhibitor Anacardic acid (AA), suggesting that BoHV-1 may take advantage of histone acetylation for efficient replication. Taken together, we proposed that the HAT-dependent histone H3 acetylation plays an important role in BoHV-1 replication in MDBK (Madin-Darby bovine kidney) cells. |
topic |
BoHV-1 HAT HDAC proteasome histone H3 |
url |
http://www.mdpi.com/1999-4915/10/10/525 |
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