PXD055230-2

PXD055230 is an original dataset announced via ProteomeXchange.

Title	Global Lysine Lactylation Dynamics during HCMV and HSV-1 Infections
Description	Aerobic glycolysis is a hallmark of virus-infected cells, leading to substantial accumulation and secretion of lactate. However, the regulatory roles of lactate during viral infections are still poorly understood. Here, we report that human cytomegalovirus (HCMV) infection leverages lactate to induce widespread protein lactylation and promote viral spread. Lactyllysine decorates intrinsically disordered regions (IDRs) of proteins, regulating viral protein condensates and immune signaling transduction. Dynamic lactylation of immune response pathways, a feature shared during infection with herpes simplex virus 1 (HSV-1), suppresses immunity through regulation of HEXIM1, RBM14, and IFI16. K90 lactylation of the viral DNA sensor IFI16 blocks recruitment of the DNA-damage response master kinase DNA-PK, preventing IFI16-driven gene repression and cytokine responses. Together, we characterize global protein lactylation dynamics during virus infection, finding virus-induced lactate contributes to its immune evasion through direct inhibition of immune signaling pathways.
HostingRepository	PRIDE
AnnounceDate	2025-01-13
AnnouncementXML	Submission_2025-01-13_03:59:52.878.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Matthew Tyl
SpeciesList	scientific name: Human cytomegalovirus (HHV-5) (Human herpesvirus 5); NCBI TaxID: 10359; scientific name: Homo sapiens (Human); NCBI TaxID: 9606; scientific name: Human alphaherpesvirus 1; NCBI TaxID: 10298;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive HF; timsTOF Ultra

Revision	Datetime	Status	ChangeLog Entry
0	2024-08-27 03:41:21	ID requested
1	2024-11-23 13:03:23	announced
⏵ 2	2025-01-13 03:59:53	announced	2025-01-13: Updated project metadata.

Tyl MD, Merengwa VU, Cristea IM, Infection-induced lysine lactylation enables herpesvirus immune evasion. Sci Adv, 11(2):eads6215(2025) [pubmed]

10.1126/sciadv.ads6215;

submitter keyword: HCMV, HSV-1, Lactyllysine, Fibroblast,Lactylation

Ileana Cristea
contact affiliation	Department of Molecular Biology, Princeton University
contact email	icristea@princeton.edu
lab head
Matthew Tyl
contact affiliation	Princeton University
contact email	mtyl@princeton.edu
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/2024/11/PXD055230

PRIDE project URI

• PRIDE
  1. PXD055230
     1. Label: PRIDE project
     2. Name: Global Lysine Lactylation Dynamics during HCMV and HSV-1 Infections