Evidence map›Paper›PMID 39772686›Full record

ArticleScience advances2025

Infection-induced lysine lactylation enables herpesvirus immune evasion.

Matthew D Tyl, Victoria U Merengwa, Ileana M Cristea

Registry-linked trialAbstract read
In one paragraph

Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT07450833 (Assessing the Safety, Tolerability and Pharmacokinetics of Benfo-Oxythiamine), which is not on this map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

NCT07450833 phase1completednot on this map

Assessing the Safety, Tolerability and Pharmacokinetics of Benfo-Oxythiamine (B-OT) in Healthy Volunteers - An Open Label, Phase I Study

TypeinterventionalSponsorBenfovir AGRan2022 to 2022Enrolled48ConditionsHealthy VolunteersArmsBenfo-oxythiamine
3 · Its place in the literature

Who cites it

22 citing papers in PubMed.

  1. Review
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  3. Article
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  7. Article
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  11. Article
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  14. Frontiers in cellular and infection microbiology · 2026
    Article
  15. Article
  16. Review
  17. Review
  18. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Matthew D TylDepartment of Molecular Biology, Princeton University, Lewis Thomas Laboratory, Washington Road, Princeton, NJ 08544, USA.ORCID 0000-0002-6543-9028
Victoria U MerengwaDepartment of Molecular Biology, Princeton University, Lewis Thomas Laboratory, Washington Road, Princeton, NJ 08544, USA.ORCID 0009-0001-7102-7898
Ileana M CristeaDepartment of Molecular Biology, Princeton University, Lewis Thomas Laboratory, Washington Road, Princeton, NJ 08544, USA.ORCID 0000-0002-6533-2458

Funding

Mechanisms mediating immune response upon sensing of nuclear viral DNAR01GM114141 · NIGMS · PRINCETON UNIVERSITY · PI CRISTEA, ILEANA M. · 2015 to 2023
$2.6M
Dynamic virus-driven remodeling of ER-mitochondria contactsR01AI174515 · NIAID · PRINCETON UNIVERSITY · PI CRISTEA, ILEANA M. · 2022 to 2025
$2.2M
NIAID NIH HHS R01 AI174515NIGMS NIH HHS R01 GM114141
6 · The paper itself

Abstract

Aerobic glycolysis is a hallmark of many viral infections, leading to substantial accumulation of lactate. However, the regulatory roles of lactate during viral infections remain poorly understood. Here, we report that human cytomegalovirus (HCMV) infection leverages lactate to induce widespread protein lactylation and promote viral spread. We establish that lactyllysine is enriched in intrinsically disordered regions, regulating viral protein condensates and immune signaling transduction. Dynamic lactylation of immune factors suppresses immunity, a feature we show to be shared for HCMV and herpes simplex virus 1 infections, through regulation of RNA binding protein 14 and interferon-γ-inducible protein 16 (IFI16). K90 lactylation of the viral DNA sensor IFI16 inhibits recruitment of the DNA damage response kinase DNA-PK, preventing IFI16-driven virus gene repression and cytokine induction. Together, we characterize global protein lactylation dynamics during virus infection, finding that virus-induced lactate contributes to its immune evasion through direct inhibition of immune signaling pathways.

Indexed as

Immune EvasionLysineCytomegalovirusCytomegalovirus InfectionsHerpesvirus 1, HumanHumansLactic AcidNuclear ProteinsPhosphoproteinsSignal TransductionViral ProteinsIFI16 protein, humanLactic AcidLysineNuclear ProteinsPhosphoproteinsViral Proteins

Identifiers

PMID39772686
PMCPMC11708889

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.