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DataSet Summary

  • HostingRepository: PRIDE
  • AnnounceDate: 2014-07-24
  • AnnouncementXML: Submission_2014-07-24_05:20:27.xml
  • DigitalObjectIdentifier:
  • ReviewLevel: Peer-reviewed dataset
  • DatasetOrigin: Original data
  • RepositorySupport: Unsupported dataset by repository
  • PrimarySubmitter: Marco Benevento
  • 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.
  • SpeciesList: scientific name: Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5); NCBI TaxID: ADE05;
  • ModificationList: acetylated residue
  • Instrument: LTQ Orbitrap; Q Exactive

Dataset History

VersionDatetimeStatusChangeLog Entry
02013-11-21 08:02:23ID requested
12014-06-09 02:38:44announced
22014-07-24 05:20:28announcedUpdated project metadata.

Publication List

  1. Benevento M, Di Palma S, Snijder J, Moyer CL, Reddy VS, Nemerow GR, Heck AJ, Adenovirus composition, proteolysis, and disassembly studied by in-depth qualitative and quantitative proteomics. J Biol Chem, 289(16):11421-30(2014) [pubmed]

Keyword List

  1. ProteomeXchange project tag: PRIME-XS Project
  2. curator keyword: Biomedical
  3. submitter keyword: Adenovirus, quantification, proteomics

Contact List

    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:

Full Dataset Link List

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  2. PRIDE project URI
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