PXD063935-1

PXD063935 is an original dataset announced via ProteomeXchange.

Title	Time-Resolved Analysis of Protein-Protein Ensembles using a Destabilizing Domain (TRAPPED) to resolve dynamic interactions of SARS-CoV-2 nsp15
Description	Cellular protein-protein interactions are dynamic and can change over time. Current interactomics methods capture steady-state information but lack the ability to differentiate when the interactions occur. This study developed a post-translational method for synchronizing protein accumulation that allows for monitoring of protein-protein interactions of the same protein population over time. The protein of interest is tagged with a destabilizing protein domain, which can be stabilized and labeled by a functionalized small molecule. This system, Time-Resolved Analysis of Protein-Protein Ensembles using a Destabilizing Domain (TRAPPED), was utilized to characterize the interactions of SARS-CoV-2 and SARS-CoV non-structural protein 15 to reveal the timing of key interactions with RNA-binding proteins. TRAPPED can be expanded to study the timing of interactions in other systems including viral infection, secretion pathways, and signal transduction.
HostingRepository	PRIDE
AnnounceDate	2025-09-29
AnnouncementXML	Submission_2025-09-28_17:22:37.185.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD063935
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Crissey Cameron
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	TMT6plex-126 reporter+balance reagent acylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Exploris 480

Revision	Datetime	Status	ChangeLog Entry
0	2025-05-14 13:05:38	ID requested
⏵ 1	2025-09-28 17:22:38	announced

10.1021/acschembio.5c00377;

10.6019/PXD063935;

Cameron C, Clark RM, Metts AM, Jiang RM, Scaggs TD, Kim K, Sulikowski GA, Plate L, Time-Resolved Analysis of Protein-Protein Ensembles Using a Destabilizing Domain to Map Dynamic Interactions of SARS-CoV-2 nsp15. ACS Chem Biol, 20(9):2229-2242(2025) [pubmed]

submitter keyword: dihydrofolate reductase, proteomics, affinity purification-mass spectrometry, interactomics, destabilizing domain,Virus-host protein interactions

Lars Plate
contact affiliation	Departments of Chemistry, Biological Sciences, Microbiology and Immunology, Vanderbilt University
contact email	lars.plate@vanderbilt.edu
lab head
Crissey Cameron
contact affiliation	Vanderbilt University
contact email	crissey.d.cameron@vanderbilt.edu
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2025/09/PXD063935

PRIDE project URI

• PRIDE
  1. PXD063935
     1. Label: PRIDE project
     2. Name: Time-Resolved Analysis of Protein-Protein Ensembles using a Destabilizing Domain (TRAPPED) to resolve dynamic interactions of SARS-CoV-2 nsp15