Proteomics

Dataset Information

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Identification of herpes virus proteines palmitoyled in RPE-1 cells


ABSTRACT: Protein palmitoylation regulates diverse aspects of cellular function and organization and plays a key role in host immune responses to infection. Palmitoylation also modulates the function and localization of virus-encoded proteins. In Serwa et al. (doi:10.1016/j.chembiol.2015.06.024), we employed chemical proteomics tools, bio-orthogonal palmitic acid analogue (heptadec-16-ynoic acid, YnPal), and a multi-functional capture reagent (AzTB) to study palmitoylation events during infection with three strains of herpes simplex virus (HSV-1[17], HSV-1[KOS], HSV-2[186]). We found that a significant fraction of the viral proteome (twelve HSV-encoded proteins) undergoes palmitoylation; we identified a number of virus membrane glycoproteins, structural proteins, and kinases. Furthermore, we identified palmitoylation sites on five HSV-encoded proteins utilising a complementary methodology (Acyl-RAC). This paper also reports selective HSV-induced alterations to palmitoylation and myristoylation of host proteins.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Human Herpesvirus 2 (strain 186) (hhv-2) (human Herpes Simplex Virus 2) Human Herpesvirus 1 (strain 17) (hhv-1) (human Herpes Simplex Virus 1) Human Herpesvirus 1 (strain Kos) (hhv-1) (human Herpes Simplex Virus 1)

TISSUE(S): Epithelial Cell, Cell Culture

SUBMITTER: Remigiusz Serwa  

LAB HEAD: Edward W. Tate

PROVIDER: PXD002708 | Pride | 2022-03-02

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
HSV1-17_A.raw Raw
HSV1-17_B.raw Raw
HSV1-17_C.raw Raw
HSV1-KOS_A.raw Raw
HSV1-KOS_B.raw Raw
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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]

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