⮝ Full datasets listing

PXD035305

PXD035305 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleMX2 Viral Substrate Breadth and Inhibitory Activity Are Regulated by Protein Phosphorylation
DescriptionProductive infection by human immunodeficiency virus type-1 (HIV-1) requires the import of viral replication complexes into the nuclei of infected cells. Myxovirus resistance 2 (MX2/MxB) blocks this step, halting nuclear accumulation of viral DNA and virus replication. Here, we identify positions in MX2 whose phosphorylation status reduces or enhances antiviral function (hypomorphic and hypermorphic variants, respectively). Importantly, hypermorphic mutant proteins not only increased inhibitory activity against wild-type HIV-1 but can also exhibit antiviral capabilities against HIV-1 capsid mutant viruses that are resistant to wild-type MX2. Furthermore, some of these proteins were also able to inhibit retroviruses that are insensi- tive to MX2. Therefore, we propose that phosphorylation comprises a major element of MX2 regulation and substrate determination.
HostingRepositoryPRIDE
AnnounceDate2023-11-14
AnnouncementXMLSubmission_2023-11-14_08:57:20.673.xml
DigitalObjectIdentifierhttps://dx.doi.org/10.6019/PXD035305
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterSteven Lynham
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListphosphorylated residue
InstrumentOrbitrap Fusion Lumos
Dataset History
RevisionDatetimeStatusChangeLog Entry
02022-07-13 07:57:05ID requested
12022-07-21 06:43:04announced
22023-11-14 08:57:21announced2023-11-14: Updated project metadata.
Publication List
10.6019/PXD035305;
Keyword List
submitter keyword: innate immunity,MX2, protein phosphorylation, infection, retroviruses
Contact List
Professor Michael Malim
contact affiliationProfessor of Infectious Diseases, Department of Infectious Diseases, School of Immunology & Microbial Diseases, Faculty of Life Sciences & Medicine, King's College London
contact emailmichael.malim@kcl.ac.uk
lab head
Steven Lynham
contact affiliationKing's College London
contact emailsteven.lynham@kcl.ac.uk
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/2022/07/PXD035305
PRIDE project URI
Repository Record List
[ + ]