Cargando…
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...
Autores principales: | , , , , , , , , , , , , , , , |
---|---|
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 |
_version_ | 1783513421303513088 |
---|---|
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. |
format | Online Article Text |
id | pubmed-7112117 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Elsevier Inc. |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT liuxia humanbornadiseasevirusinfectionimpactshostproteomeandhistonelysineacetylationinhumanoligodendrogliacells AT zhaolibo humanbornadiseasevirusinfectionimpactshostproteomeandhistonelysineacetylationinhumanoligodendrogliacells AT yangyongtao humanbornadiseasevirusinfectionimpactshostproteomeandhistonelysineacetylationinhumanoligodendrogliacells AT bodeliv humanbornadiseasevirusinfectionimpactshostproteomeandhistonelysineacetylationinhumanoligodendrogliacells AT huanghua humanbornadiseasevirusinfectionimpactshostproteomeandhistonelysineacetylationinhumanoligodendrogliacells AT liuchengyu humanbornadiseasevirusinfectionimpactshostproteomeandhistonelysineacetylationinhumanoligodendrogliacells AT huangrongzhong humanbornadiseasevirusinfectionimpactshostproteomeandhistonelysineacetylationinhumanoligodendrogliacells AT zhangliang humanbornadiseasevirusinfectionimpactshostproteomeandhistonelysineacetylationinhumanoligodendrogliacells AT wangxiao humanbornadiseasevirusinfectionimpactshostproteomeandhistonelysineacetylationinhumanoligodendrogliacells AT zhanglujun humanbornadiseasevirusinfectionimpactshostproteomeandhistonelysineacetylationinhumanoligodendrogliacells AT liusiwen humanbornadiseasevirusinfectionimpactshostproteomeandhistonelysineacetylationinhumanoligodendrogliacells AT zhoujingjing humanbornadiseasevirusinfectionimpactshostproteomeandhistonelysineacetylationinhumanoligodendrogliacells AT lixin humanbornadiseasevirusinfectionimpactshostproteomeandhistonelysineacetylationinhumanoligodendrogliacells AT hetieming humanbornadiseasevirusinfectionimpactshostproteomeandhistonelysineacetylationinhumanoligodendrogliacells AT chengzhongyi humanbornadiseasevirusinfectionimpactshostproteomeandhistonelysineacetylationinhumanoligodendrogliacells AT xiepeng humanbornadiseasevirusinfectionimpactshostproteomeandhistonelysineacetylationinhumanoligodendrogliacells |