PXD002708

PXD002708 is an original dataset announced via ProteomeXchange.

Title	Identification of herpes virus proteines palmitoyled in RPE-1 cells
Description	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.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:34:56.030.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Remigiusz Serwa
SpeciesList	scientific name: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1); NCBI TaxID: 10299; scientific name: Human herpesvirus 2 (strain 186) (HHV-2) (Human herpes simplex virus 2); NCBI TaxID: 10312; scientific name: Human herpesvirus 1 (strain KOS) (HHV-1) (Human herpes simplex virus 1); NCBI TaxID: 10306;
ModificationList	palmitoylated residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2015-08-12 07:43:09	ID requested
1	2022-03-02 03:01:13	announced
⏵ 2	2024-10-22 05:34:56	announced	2024-10-22: Updated project metadata.

10.1016/j.chembiol.2015.06.024;

Serwa RA, Abaitua F, Krause E, Tate EW, O'Hare P, Systems Analysis of Protein Fatty Acylation in Herpes Simplex Virus-Infected Cells Using Chemical Proteomics. Chem Biol, 22(8):1008-17(2015) [pubmed]

curator keyword: Biomedical

submitter keyword: Palmitoylation, chemical proteomics, tagging by substrate, Acyl-RAC, herpes virus

Edward W. Tate
contact affiliation	Department of Chemistry, Imperial College London
contact email	e.tate@imperial.ac.uk
lab head
Remigiusz Serwa
contact affiliation	Imperial College London
contact email	r.serwa@imperial.ac.uk
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD002708
     1. Label: PRIDE project
     2. Name: Identification of herpes virus proteines palmitoyled in RPE-1 cells