PXD000591-3

PXD000591 is an original dataset announced via ProteomeXchange.

Title	Human Adenovirus 5 (HAdV5), LC-MSMS
Description	Using high-resolution mass spectrometry (MS)-based proteomics in combination with multiple protease digestion, we profiled, with on average 90% sequence coverage, all 13 viral proteins present in an human adenovirus (HAdV) vector. This in-depth profile provided multiple peptide-based evidence on intrinsic protease activity affecting several HAdV proteins. Next, the generated peptide library was used to develop a targeted proteomics method using selected reaction monitoring (SRM) aimed at quantitative profiling of the stoichiometry of all 13 proteins present in the HAdV. We also used this method to probe the release of specific virus proteins initiated by thermal stimulation, mimicking the early stage of HAdV disassembly during entry into host cells. We confirmed the copy numbers of the most well characterized viral capsid components and established the copy numbers for proteins whose stoichiometry has so far not been accurately defined. We also found that heating HAdV induces the complete release of the penton base and fiber proteins as well as a substantial release of protein VIII and VI. For these latter proteins, maturational proteolysis by the adenoviral protease (AVP) leads to the differential release of fragments with certain peptides being fully released and others largely retained in the AdV particles. This information is likely to be beneficial for the ongoing interpretation of high resolution cryoEM and X-ray electron density maps.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:20:57.767.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Marco Benevento
SpeciesList	scientific name: Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5); NCBI TaxID: 28285;
ModificationList	acetylated residue
Instrument	Q Exactive; LTQ Orbitrap

Revision	Datetime	Status	ChangeLog Entry
0	2013-11-21 08:02:23	ID requested
1	2014-06-09 02:38:44	announced
2	2014-07-24 05:20:28	announced	Updated project metadata.
⏵ 3	2024-10-22 04:21:05	announced	2024-10-22: Updated project metadata.

10.1074/jbc.M113.537498;

Benevento M, Di Palma S, Snijder J, Moyer CL, Reddy VS, Nemerow GR, Heck AJR, Adenovirus composition, proteolysis, and disassembly studied by in-depth qualitative and quantitative proteomics. J Biol Chem, 289(16):11421-11430(2014) [pubmed]

ProteomeXchange project tag: PRIME-XS Project

curator keyword: Biomedical

submitter keyword: proteomics,Adenovirus, quantification

Albert J.R. Heck
contact affiliation	Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Science, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands; Netherlands Proteomics Centre, Padualaan 8, 3584 CH Utrecht, The Netherlands
contact email	a.j.r.heck@uu.nl
lab head
Marco Benevento
contact affiliation	Faculty of Sciences
contact email	m.benevento@uu.nl
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/2014/06/PXD000591

PRIDE project URI

• PRIDE
  1. PXD000591
     1. Label: PRIDE project
     2. Name: Human Adenovirus 5 (HAdV5), LC-MSMS