Unknown

Dataset Information

0

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


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.

SUBMITTER: Serwa RA 

PROVIDER: S-EPMC4543063 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Serwa Remigiusz A RA   Abaitua Fernando F   Krause Eberhard E   Tate Edward W EW   O'Hare Peter P  

Chemistry & biology 20150806 8


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 gen  ...[more]

Similar Datasets

| S-EPMC7524712 | biostudies-literature
2020-05-22 | PXD013407 | Pride
| S-EPMC7851555 | biostudies-literature
2021-01-22 | GSE163952 | GEO
| S-EPMC2882321 | biostudies-literature
2010-10-16 | GSE24725 | GEO
| PRJNA338711 | ENA
| S-EPMC2783783 | biostudies-literature
| S-EPMC5137459 | biostudies-literature
| S-EPMC3497699 | biostudies-literature