PXD011914

PXD011914 is an original dataset announced via ProteomeXchange.

Title	Interactions of human norovirus capsid P domain with histo-blood group antigens with Hydrogen-Deuterium Exchange Mass Spectrometry
Description	Attachment of human noroviruses to histo blood group antigens (HBGAs) is essential for infection, but how this binding event promotes the infection of host cells is unknown. Here, we employed protein NMR experiments supported by mass spectrometry and crystallography to study HBGA binding to the P domain of a prevalent virus strain (GII.4) in more detail . We report a highly selective transformation of N373, located in an antigenic loop adjoining the HBGA binding site, into an iso-aspartate residue. This spontaneous post-translational modification (PTM) proceeds with an estimated half-life of a few days at physiological temperatures, independent of the presence of HBGAs but dramatically affecting HBGA recognition.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:51:20.279.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Jasmin Dülfer
SpeciesList	scientific name: Norovirus Hu/GII-4/Saga4/2006/JP; NCBI TaxID: 546981; scientific name: Norovirus Hu/GII.4/MI001/2011/USA; NCBI TaxID: 1354724; scientific name: Norovirus Hu/GII/JP/2015/GII.P17_GII.17/Kawasaki308; NCBI TaxID: 1634342; scientific name: Norwalk virus; NCBI TaxID: 11983;
ModificationList	monohydroxylated residue; deamidated residue
Instrument	Orbitrap Fusion ETD

Revision	Datetime	Status	ChangeLog Entry
0	2018-12-03 01:42:11	ID requested
1	2019-03-20 06:27:47	announced
2	2019-04-03 04:36:01	announced	Updated publication reference for PubMed record(s): 30899001.
⏵ 3	2024-10-22 04:51:28	announced	2024-10-22: Updated project metadata.

Mallagaray A, Creutznacher R, D, ü, lfer J, Mayer PHO, Grimm LL, Ordu, ñ, a JM, Trabjerg E, Stehle T, Rand KD, Blaum BS, Uetrecht C, Peters T, A post-translational modification of human Norovirus capsid protein attenuates glycan binding. Nat Commun, 10(1):1320(2019) [pubmed]

10.1038/s41467-019-09251-5;

curator keyword: Biomedical

submitter keyword: HDX MS, P domain, GII.4 Saga,human norovirus, histo-blood group antigens

Charlotte Uetrecht
contact affiliation	Heinrich Pette Institute, Leibniz Institute for Experimental Virology, Martinistrasse 52, 20251 Hamburg, Germany
contact email	charlotte.uetrecht@xfel.eu
lab head
Jasmin Dülfer
contact affiliation	Heinrich Pette Institute
contact email	jasmin.duelfer@leibniz-hpi.de
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/2019/03/PXD011914

PRIDE project URI

• PRIDE
  1. PXD011914
     1. Label: PRIDE project
     2. Name: Interactions of human norovirus capsid P domain with histo-blood group antigens with Hydrogen-Deuterium Exchange Mass Spectrometry