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Chem Biol. 2015 Aug 20;22(8):1008-17. doi: 10.1016/j.chembiol.2015.06.024. Epub 2015 Aug 6.

Systems Analysis of Protein Fatty Acylation in Herpes Simplex Virus-Infected Cells Using Chemical Proteomics.

Author information

1
Department of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ, UK.
2
Section of Virology, Faculty of Medicine, Imperial College London, Norfolk Place, London W2 1QN, UK.
3
Leibniz-Institut für Molekulare Pharmakologie (FMP), Robert-Rössle Street 10, 13125 Berlin, Germany.
4
Department of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ, UK. Electronic address: e.tate@imperial.ac.uk.
5
Section of Virology, Faculty of Medicine, Imperial College London, Norfolk Place, London W2 1QN, UK. Electronic address: pohare@imperial.ac.uk.

Abstract

Protein fatty acylation regulates diverse aspects of cellular function and organization and plays a key role in host immune responses to infection. Acylation also modulates the function and localization of virus-encoded proteins. Here, we employ chemical proteomics tools, bio-orthogonal probes, and capture reagents to study myristoylation and palmitoylation during infection with herpes simplex virus (HSV). Using in-gel fluorescence imaging and quantitative mass spectrometry, we demonstrate a generalized reduction in myristoylation of host proteins, whereas palmitoylation of host proteins, including regulators of interferon and tetraspanin family proteins, was selectively repressed. Furthermore, we found that a significant fraction of the viral proteome undergoes palmitoylation; we identified a number of virus membrane glycoproteins, structural proteins, and kinases. Taken together, our results provide broad oversight of protein acylation during HSV infection, a roadmap for similar analysis in other systems, and a resource with which to pursue specific analysis of systems and functions.

PMID:
26256475
PMCID:
PMC4543063
DOI:
10.1016/j.chembiol.2015.06.024
[Indexed for MEDLINE]
Free PMC Article

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