Systems analysis of protein fatty acylation in herpes simplex virus infected cells using chemical proteomics.
File(s)
Published version
Author(s)
Serwa, R
Krause, E
Abaitua, F
Tate, EW
O'Hare, PF
Type
Journal Article
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.
Date Issued
2015-08-06
Date Acceptance
2015-07-13
Citation
Chemistry & Biology, 2015, 22 (8), pp.1008-1017
ISSN
1074-5521
Publisher
Elsevier
Start Page
1008
End Page
1017
Journal / Book Title
Chemistry & Biology
Volume
22
Issue
8
Copyright Statement
© 2015 The Authors. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
License URL
Publication Status
Published