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Virology. 2015 Nov;485:58-78. doi: 10.1016/j.virol.2015.06.024. Epub 2015 Jul 23.

Persistent human Borna disease virus infection modifies the acetylome of human oligodendroglia cells towards higher energy and transporter levels.

Author information

1
Shanghai Key Laboratory of Forensic Medicine, Institute of Forensic Science, Ministry of Justice, Shanghai 200063, China.
2
Institute of Neuroscience and the Collaborative Innovation Center for Brain Science, Chongqing Medical University, Chongqing 400016, China; Chongqing Key Laboratory of Neurobiology, Chongqing Medical University, Chongqing 400016, China.
3
Institute of Neuroscience and the Collaborative Innovation Center for Brain Science, Chongqing Medical University, Chongqing 400016, China.
4
Institute of Neuroscience and the Collaborative Innovation Center for Brain Science, Chongqing Medical University, Chongqing 400016, China; Chongqing Key Laboratory of Neurobiology, Chongqing Medical University, Chongqing 400016, China; Department of Neurology, The First Affiliated Hospital of Chongqing Medical University, Chongqing 400016, China.
5
Department of Pathology, Faculty of Basic Medicine, Chongqing Medical University, Chongqing 400016, China.
6
Department of Internal Medicine, University-Town Hospital of Chongqing Medical University, Chongqing 400016, China.
7
Jingjie PTM BioLab (Hangzhou) Co. Ltd, Hangzhou 310018, China.
8
Advanced Institute of Translational Medicine, Tongji University, Shanghai 200092, China.
9
Institute of Neuroscience and the Collaborative Innovation Center for Brain Science, Chongqing Medical University, Chongqing 400016, China; Chongqing Key Laboratory of Neurobiology, Chongqing Medical University, Chongqing 400016, China; Department of Neurology, The First Affiliated Hospital of Chongqing Medical University, Chongqing 400016, China. Electronic address: xiepeng@cqmu.edu.cn.

Abstract

BACKGROUND:

Borna disease virus (BDV) is a neurotropic RNA virus persistently infecting mammalian hosts including humans. Lysine acetylation (Kac) is a key protein post-translational modification (PTM). The unexpectedly broad regulatory scope of Kac let us to profile the entire acetylome upon BDV infection.

METHODS:

The acetylome was profiled through stable isotope labeling for cell culture (SILAC)-based quantitative proteomics. The quantifiable proteome was annotated using bioinformatics.

RESULTS:

We identified and quantified 791 Kac sites in 473 Kac proteins in human BDV Hu-H1-infected and non-infected oligodendroglial (OL) cells. Bioinformatic analysis revealed that BDV infection alters the acetylation of metabolic proteins, membrane-associated proteins and transmembrane transporter activity, and affects the acetylation of several lysine acetyltransferases (KAT).

CONCLUSIONS:

Upon BDV persistence the OL acetylome is manipulated towards higher energy and transporter levels necessary for shuttling BDV proteins to and from nuclear replication sites.

KEYWORDS:

Acetylation; BDV; Borna disease virus; Kac; Oligodendroglia; Proteomic

PMID:
26210075
DOI:
10.1016/j.virol.2015.06.024
[Indexed for MEDLINE]
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