<<< Full experiment listing

PXD021756

PXD021756 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleThe Serpin-like Loop-insertion of Ovalbumin Increases Stability and Reduces OVA 323-339 Epitope Immunogenicity
DescriptionChicken ovalbumin (cOVA) has been studied for decades primarily due to the robust genetic and molecular resources that are available for experimental investigations. cOVA is a member of the serpin superfamily of proteins that function as protease inhibitors, although cOVA does not exhibit this activity. As a serpin, cOVA possesses a protease-sensitive reactive-center loop that lies adjacent to the OVA 323-339 CD4+ T-cell epitope. We took advantage of the previously described single-substitution-variant, OVA R339T, which can undergo the dramatic structural transition observed in serpins to study how changes in loop size and protein stability influences CD4+ T-cell priming in vivo. We observed that the OVA R339T loop-insertion increases stability and protease resistance, resulting in reduced CD4+ T-cell priming of the OVA 323-339 epitope in SJL mice. These findings have implications for the design of more effective vaccines for the treatment of infectious diseases and cancer as well as the development of more robust CD4+ T-cell-epitope prediction tools.
HostingRepositoryPRIDE
AnnounceDate2023-11-14
AnnouncementXMLSubmission_2023-11-14_08:51:38.405.xml
DigitalObjectIdentifierhttps://dx.doi.org/10.6019/PXD021756
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterDaniel Moss
SpeciesList scientific name: Gallus gallus (Chicken); NCBI TaxID: 9031;
ModificationListmonohydroxylated residue; iodoacetamide derivatized residue
InstrumentOrbitrap Fusion
Dataset History
RevisionDatetimeStatusChangeLog Entry
02020-09-30 01:01:19ID requested
12021-05-07 09:20:33announced
22023-11-14 08:51:38announced2023-11-14: Updated project metadata.
Publication List
10.6019/PXD021756;
Keyword List
submitter keyword: LC-MS, Antigen Processing, Limited Proteolysis
Contact List
Samuel J. Landy
contact affiliationDepartment of Biochemistry and Molecular Biology, School of Medicine, Tulane University, New Orleans, Louisiana 70112
contact emaillandry@tulane.edu
lab head
Daniel Moss
contact affiliationTulane University
contact emaildmoss2@tulane.edu
dataset submitter
Full Dataset Link List
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/2021/05/PXD021756
PRIDE project URI
Repository Record List
[ + ]