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

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About: Human borna disease virus infection impacts host proteome and histone lysine acetylation in human oligodendroglia cells Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Human borna disease virus infection impacts host proteome and histone lysine acetylation in human oligodendroglia cells
Creator	Li, Xin Wang, Xiao Zhang, Liang Xie, Peng Zhang, Lujun Liu, Xia Huang, Hua Bode, Liv Cheng, Zhongyi He, Tieming Huang, Rongzhong Liu, Chengyu Liu, Siwen Yang, Yongtao Zhao, Libo Zhou, Jingjing
source	Elsevier; Medline; PMC
abstract	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.
has issue date	2014-08-01(xsd:dateTime)
bibo:doi	10.1016/j.virol.2014.06.040
bibo:pmid	25086498
has license	no-cc
sha1sum (hex)	615035c3a4f19bbda72d84a04ba5596d0b7c56a8
schema:url	https://doi.org/10.1016/j.virol.2014.06.040
resource representing a document's title	Human borna disease virus infection impacts host proteome and histone lysine acetylation in human oligodendroglia cells
has PubMed Central identifier	PMC7112117
has PubMed identifier	25086498
schema:publication	Virology
resource representing a document's body	covid:615035c3a4f19bbda72d84a04ba5596d0b7c56a8#body_text
is schema:about of	named entity 'HOST' named entity 'oligodendroglial' named entity 'isotope' named entity 'lysine' named entity 'DNA repair' named entity 'Methods' named entity 'impacts' named entity 'PROTEINS' named entity 'LYSINE' named entity 'HISTONES' named entity 'STABLE ISOTOPE' named entity 'STRAIN' named entity 'IDENTIFIED' named entity 'INFECTION' named entity 'QUANTIFIABLE' named entity 'BDV' named entity '4383' named entity 'CORE' named entity 'VALIDATED' named entity 'BORNA DISEASE VIRUS' named entity 'UNDERSTANDING' named entity 'ADDRESS' named entity 'HISTONE' named entity 'REPLICATES' named entity 'CELLS' named entity 'TIME' named entity 'SITES' named entity 'PATHWAYS' named entity 'USING' named entity 'IMPACTED' named entity 'HISTONE' named entity 'ALTERED' named entity 'QUANTITATIVE PROTEOMICS' named entity 'ACETYLATION' named entity 'KAC' named entity 'INFECTIONS' named entity 'OLIGODENDROGLIA' named entity 'PROTEOME' named entity 'IMPACTS' named entity 'CELLS' named entity 'BORNA DISEASE VIRUS' named entity 'VIRUS INFECTION' named entity 'ACETYLATION' named entity 'HUMAN' named entity 'ALLOWING' named entity 'ANNOTATED' named entity 'USED' named entity 'PROTEOME' named entity 'LYSINE' named entity 'POST' named entity 'IMMUNE RESPONSE' named entity 'BACKGROUND' named entity 'HUMAN' named entity 'PERSISTENT' named entity 'BASED' named entity 'THIRTY' named entity 'DRIVEN' named entity 'BIOCHEMISTRY' named entity 'HISTONE ACETYLATION' named entity 'PATHOPHYSIOLOGY' named entity 'CONCLUSIONS' named entity 'TRANSCRIPTIONAL REGULATION' named entity 'HOW' named entity 'RESULTS' named entity 'IN VITRO' named entity 'DNA REPAIR'

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