PXD012785 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Quantitative temporal proteomic analysis of vaccinia virus infection reveals regulation of histone deacetylases by an interferon antagonist |
Description | Vaccinia virus (VACV) has numerous immune evasion strategies, including multiple mechanisms of inhibition of IRF-3, NF-κB and type I interferon (IFN) signaling. Here, we used highly multiplexed proteomics to quantify >8,000 cellular proteins and ~80% of viral proteins over seven time points spanning the whole course of VACV infection. This identified multiple novel viral targets, including putative natural killer cell ligands and IFN-stimulated genes. The class II histone deacetylase HDAC5 was selectively degraded early during VACV infection. Use of cell lines in which HDAC5 was overexpressed or knocked out showed that HDAC5 restricted replication of both VACV and herpes simplex virus type 1 (HSV-1). By generating a protein-based temporal classification of VACV gene expression, we identified the early protein C6, a multifunctional IFN antagonist, as the factor that targets HDAC5 for proteasomal degradation. Our approach thus identifies both a novel restriction factor and a viral mechanism of innate immune evasion. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_04:53:57.297.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Michael Weekes |
SpeciesList | scientific name: Vaccinia virus Western Reserve; NCBI TaxID: 696871; scientific name: Vaccinia virus; NCBI TaxID: NCBITaxon:10245; scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | TMT6plex-126 reporter+balance reagent acylated residue; monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | Orbitrap Fusion Lumos |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2019-02-19 05:22:32 | ID requested | |
1 | 2019-05-07 09:03:48 | announced | |
2 | 2019-05-27 00:08:49 | announced | Updated publication reference for PubMed record(s): 31067474. |
⏵ 3 | 2024-10-22 04:53:58 | announced | 2024-10-22: Updated project metadata. |
Publication List
10.1016/j.celrep.2019.04.042; |
Soday L, Lu Y, Albarnaz JD, Davies CTR, Antrobus R, Smith GL, Weekes MP, Quantitative Temporal Proteomic Analysis of Vaccinia Virus Infection Reveals Regulation of Histone Deacetylases by an Interferon Antagonist. Cell Rep, 27(6):1920-1933.e7(2019) [pubmed] |
Keyword List
curator keyword: Biomedical |
submitter keyword: quantitative proteomics |
tandem mass tag |
systems virology |
poxvirus |
interferon |
host-pathogen interaction |
immune evasion |
innate immunity |
restriction factor |
histone deacetylase |
Contact List
Michael Weekes |
contact affiliation | Cambridge Institute for Medical Research, University of Cambridge, Hills Road, Cambridge, CB2 0XY, UK |
contact email | Mpw1001@cam.ac.uk |
lab head | |
Michael Weekes |
contact affiliation | University of Cambridge |
contact email | mpw1001@cam.ac.uk |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD012785
- Label: PRIDE project
- Name: Quantitative temporal proteomic analysis of vaccinia virus infection reveals regulation of histone deacetylases by an interferon antagonist