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Human borna disease virus infection impacts host proteome and histone lysine acetylation in human oligodendroglia cells

BACKGROUND: Borna disease virus (BDV) replicates in the nucleus and establishes persistent infections in mammalian hosts. A human BDV strain was used to address the first time, how BDV infection impacts the proteome and histone lysine acetylation (Kac) of human oligodendroglial (OL) cells, thus allo...

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Autores principales: Liu, Xia, Zhao, Libo, Yang, Yongtao, Bode, Liv, Huang, Hua, Liu, Chengyu, Huang, Rongzhong, Zhang, Liang, Wang, Xiao, Zhang, Lujun, Liu, Siwen, Zhou, Jingjing, Li, Xin, He, Tieming, Cheng, Zhongyi, Xie, Peng
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Inc. 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7112117/
https://www.ncbi.nlm.nih.gov/pubmed/25086498
http://dx.doi.org/10.1016/j.virol.2014.06.040
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author Liu, Xia
Zhao, Libo
Yang, Yongtao
Bode, Liv
Huang, Hua
Liu, Chengyu
Huang, Rongzhong
Zhang, Liang
Wang, Xiao
Zhang, Lujun
Liu, Siwen
Zhou, Jingjing
Li, Xin
He, Tieming
Cheng, Zhongyi
Xie, Peng
author_facet Liu, Xia
Zhao, Libo
Yang, Yongtao
Bode, Liv
Huang, Hua
Liu, Chengyu
Huang, Rongzhong
Zhang, Liang
Wang, Xiao
Zhang, Lujun
Liu, Siwen
Zhou, Jingjing
Li, Xin
He, Tieming
Cheng, Zhongyi
Xie, Peng
author_sort Liu, Xia
collection PubMed
description BACKGROUND: Borna disease virus (BDV) replicates in the nucleus and establishes persistent infections in mammalian hosts. A human BDV strain was used to address the first time, how BDV infection impacts the proteome and histone lysine acetylation (Kac) of human oligodendroglial (OL) cells, thus allowing a better understanding of infection-driven pathophysiology in vitro. METHODS: Proteome and histone lysine acetylation were profiled through stable isotope labeling for cell culture (SILAC)-based quantitative proteomics. The quantifiable proteome was annotated using bioinformatics. Histone acetylation changes were validated by biochemistry assays. RESULTS: Post BDV infection, 4383 quantifiable differential proteins were identified and functionally annotated to metabolism pathways, immune response, DNA replication, DNA repair, and transcriptional regulation. Sixteen of the thirty identified Kac sites in core histones presented altered acetylation levels post infection. CONCLUSIONS: BDV infection using a human strain impacted the whole proteome and histone lysine acetylation in OL cells.
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spelling pubmed-71121172020-04-02 Human borna disease virus infection impacts host proteome and histone lysine acetylation in human oligodendroglia cells Liu, Xia Zhao, Libo Yang, Yongtao Bode, Liv Huang, Hua Liu, Chengyu Huang, Rongzhong Zhang, Liang Wang, Xiao Zhang, Lujun Liu, Siwen Zhou, Jingjing Li, Xin He, Tieming Cheng, Zhongyi Xie, Peng Virology Article BACKGROUND: Borna disease virus (BDV) replicates in the nucleus and establishes persistent infections in mammalian hosts. A human BDV strain was used to address the first time, how BDV infection impacts the proteome and histone lysine acetylation (Kac) of human oligodendroglial (OL) cells, thus allowing a better understanding of infection-driven pathophysiology in vitro. METHODS: Proteome and histone lysine acetylation were profiled through stable isotope labeling for cell culture (SILAC)-based quantitative proteomics. The quantifiable proteome was annotated using bioinformatics. Histone acetylation changes were validated by biochemistry assays. RESULTS: Post BDV infection, 4383 quantifiable differential proteins were identified and functionally annotated to metabolism pathways, immune response, DNA replication, DNA repair, and transcriptional regulation. Sixteen of the thirty identified Kac sites in core histones presented altered acetylation levels post infection. CONCLUSIONS: BDV infection using a human strain impacted the whole proteome and histone lysine acetylation in OL cells. Elsevier Inc. 2014-09 2014-08-01 /pmc/articles/PMC7112117/ /pubmed/25086498 http://dx.doi.org/10.1016/j.virol.2014.06.040 Text en Copyright © 2014 Elsevier Inc. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Liu, Xia
Zhao, Libo
Yang, Yongtao
Bode, Liv
Huang, Hua
Liu, Chengyu
Huang, Rongzhong
Zhang, Liang
Wang, Xiao
Zhang, Lujun
Liu, Siwen
Zhou, Jingjing
Li, Xin
He, Tieming
Cheng, Zhongyi
Xie, Peng
Human borna disease virus infection impacts host proteome and histone lysine acetylation in human oligodendroglia cells
title Human borna disease virus infection impacts host proteome and histone lysine acetylation in human oligodendroglia cells
title_full Human borna disease virus infection impacts host proteome and histone lysine acetylation in human oligodendroglia cells
title_fullStr Human borna disease virus infection impacts host proteome and histone lysine acetylation in human oligodendroglia cells
title_full_unstemmed Human borna disease virus infection impacts host proteome and histone lysine acetylation in human oligodendroglia cells
title_short Human borna disease virus infection impacts host proteome and histone lysine acetylation in human oligodendroglia cells
title_sort human borna disease virus infection impacts host proteome and histone lysine acetylation in human oligodendroglia cells
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7112117/
https://www.ncbi.nlm.nih.gov/pubmed/25086498
http://dx.doi.org/10.1016/j.virol.2014.06.040
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