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@article{Serwa:2015:10.1016/j.chembiol.2015.06.024,
author = {Serwa, R and Krause, E and Abaitua, F and Tate, EW and O'Hare, PF},
doi = {10.1016/j.chembiol.2015.06.024},
journal = {Chemistry & Biology},
pages = {1008--1017},
title = {Systems analysis of protein fatty acylation in herpes simplex virus infected cells using chemical proteomics.},
url = {http://dx.doi.org/10.1016/j.chembiol.2015.06.024},
volume = {22},
year = {2015}
}
TY - JOUR
AB - 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.
AU - Serwa,R
AU - Krause,E
AU - Abaitua,F
AU - Tate,EW
AU - O'Hare,PF
DO - 10.1016/j.chembiol.2015.06.024
EP - 1017
PY - 2015///
SN - 1074-5521
SP - 1008
TI - Systems analysis of protein fatty acylation in herpes simplex virus infected cells using chemical proteomics.
T2 - Chemistry & Biology
UR - http://dx.doi.org/10.1016/j.chembiol.2015.06.024
UR - http://hdl.handle.net/10044/1/25083
VL - 22
ER -