PXD050139 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Implications of O-glycan modifications in the hinge region of a plant-produced SARS-CoV-2-IgA antibody on functionality |
Description | In this study, we carried out host engineering to generate a therapeutic glycoprotein largely devoid of plant-endogenous O-glycans for functional characterization. We generated four variants of a potentSARS-CoV-2 neutralizing antibody, COVA2-15 IgA1. The variants that differed in the number of modified proline residues and O-glycan compositions of their hinge region were assessed regarding their physicochemical properties and functionality. |
HostingRepository | PRIDE |
AnnounceDate | 2024-02-27 |
AnnouncementXML | Submission_2024-02-27_07:29:52.888.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Richard Strasser |
SpeciesList | scientific name: Nicotiana benthamiana; NCBI TaxID: 4100; |
ModificationList | complex glycosylation |
Instrument | Orbitrap Exploris 480 |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2024-02-26 02:34:35 | ID requested | |
⏵ 1 | 2024-02-27 07:29:53 | announced | |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: glycosylation, antibody,glycoprotein, Nicotiana benthamiana,virus |
Contact List
Richard Strasser |
contact affiliation | Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria |
contact email | richard.strasser@boku.ac.at |
lab head | |
Richard Strasser |
contact affiliation | University of Natural Resources and Life Sciences Vienna |
contact email | richard.strasser@boku.ac.at |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD050139
- Label: PRIDE project
- Name: Implications of O-glycan modifications in the hinge region of a plant-produced SARS-CoV-2-IgA antibody on functionality