PXD010494 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | LC-MS/MS EThcD of MERS-CoV and SARS-CoV S N-linked glycopeptides from recombinant spike ectodomains and whole MERS virions |
Description | Recent outbreaks of severe acute respiratory syndrome and Middle-East respiratory syndrome along with the threat of a future coronavirus pandemic underscore the importance of finding ways to neutralize these viruses. The trimeric spike transmembrane glycoprotein S mediates entry into host cells and is the major target of neutralizing antibodies. To understand the humoral immune response elicited upon natural infections with coronaviruses, we structurally characterized the SARS-CoV and MERS-CoV S glycoproteins in complex with neutralizing antibodies isolated from human survivors using cryo electron microscopy and characterized the site-specific N-linked glycan profile of the recombinant S proteins with LC-MS/MS using EThcD fragmentation. Although the two antibodies studied blocked attachment to the host cell receptor, only the anti-SARS-CoV S antibody triggered premature fusogenic conformational changes via receptor functional mimicry. These results provide a structural framework for understanding coronavirus neutralization by human antibodies and shed light on the coronavirus fusion activation pathway which appears to take place through a receptor-driven ratcheting mechanism. |
HostingRepository | PRIDE |
AnnounceDate | 2019-05-01 |
AnnouncementXML | Submission_2019-05-02_07:07:18.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Joost Snijder |
SpeciesList | scientific name: Severe acute respiratory syndrome-related coronavirus; NCBI TaxID: 694009; scientific name: Middle East respiratory syndrome-related coronavirus; NCBI TaxID: 1335626; |
ModificationList | complex glycosylation |
Instrument | Orbitrap Fusion ETD |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2018-07-19 01:53:19 | ID requested | |
1 | 2019-05-01 10:01:45 | announced | |
⏵ 2 | 2019-05-02 07:08:30 | announced | Updated publication reference for PubMed record(s): 30712865. |
3 | 2024-10-22 04:51:46 | announced | 2024-10-22: Updated project metadata. |
Publication List
Walls AC, Xiong X, Park YJ, Tortorici MA, Snijder J, Quispe J, Cameroni E, Gopal R, Dai M, Lanzavecchia A, Zambon M, Rey FA, Corti D, Veesler D, Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion. Cell, 176(5):1026-1039.e15(2019) [pubmed] |
Keyword List
submitter keyword: MERS, SARS, N-linked glycosylation, EThcD |
Contact List
David Veesler |
contact affiliation | Department of Biochemistry, University of Washington, Seattle WA USA |
contact email | dveesler@uw.edu |
lab head | |
Joost Snijder |
contact affiliation | University of Washington |
contact email | joost.snijder@gmail.com |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD010494
- Label: PRIDE project
- Name: LC-MS/MS EThcD of MERS-CoV and SARS-CoV S N-linked glycopeptides from recombinant spike ectodomains and whole MERS virions