Evidence map›Paper›PMID 42248863›Full record

ArticleNature communications2026

Integrative proteomics and lipidomics reveals dual roles for lipid droplets in the host cell antiviral response.

Ebony A Monson, Zahra Telikani, Jay L Laws, Abbey J Milligan, Irumi Amarasinghe, Sarah E Bamford, Ashley M Rozario, Monique L Smith, Vivian Tran, Quynh N Dinh and 11 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Review
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

21 authors.

Ebony A Monson *Department of Microbiology, Anatomy, Physiology and Pharmacology, La Trobe University, Melbourne, VIC, Australia. e.monson@latrobe.edu.au.ORCID http://orcid.org/0000-0001-5632-9575
Zahra Telikani *Department of Microbiology, Anatomy, Physiology and Pharmacology, La Trobe University, Melbourne, VIC, Australia.
Jay L Laws *Department of Microbiology, Anatomy, Physiology and Pharmacology, La Trobe University, Melbourne, VIC, Australia.
Abbey J MilliganLa Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC, Australia.
Irumi AmarasingheDepartment of Microbiology, Anatomy, Physiology and Pharmacology, La Trobe University, Melbourne, VIC, Australia.
Sarah E BamfordCentre for Materials and Surface Science and Department of Mathematical and Physical Sciences, La Trobe University, Melbourne, VIC, Australia.ORCID http://orcid.org/0000-0003-3539-2553
Ashley M RozarioLa Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC, Australia.
Monique L SmithDepartment of Microbiology, Anatomy, Physiology and Pharmacology, La Trobe University, Melbourne, VIC, Australia.
Vivian TranDepartment of Microbiology, Anatomy, Physiology and Pharmacology, La Trobe University, Melbourne, VIC, Australia.
Quynh N DinhDepartment of Microbiology, Anatomy, Physiology and Pharmacology, La Trobe University, Melbourne, VIC, Australia.
Nicholas WilliamsonMelbourne Mass Spectrometry and Proteomics Facility, Bio21 Molecular Science & Biotechnology Institute, The University of Melbourne, Melbourne, VIC, Australia.ORCID http://orcid.org/0000-0002-2173-3452
Adam MechlerLa Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC, Australia.ORCID http://orcid.org/0000-0002-6428-6760
Boyin LiuLa Trobe University Bioimaging Platform, Melbourne, VIC, Australia.
Chad J JohnsonLa Trobe University Bioimaging Platform, Melbourne, VIC, Australia.ORCID http://orcid.org/0000-0002-9304-5448
Paul J PigramCentre for Materials and Surface Science and Department of Mathematical and Physical Sciences, La Trobe University, Melbourne, VIC, Australia.ORCID http://orcid.org/0000-0002-7972-492X
Michael LeemingMelbourne Mass Spectrometry and Proteomics Facility, Bio21 Molecular Science & Biotechnology Institute, The University of Melbourne, Melbourne, VIC, Australia.
Shuai NieMelbourne Mass Spectrometry and Proteomics Facility, Bio21 Molecular Science & Biotechnology Institute, The University of Melbourne, Melbourne, VIC, Australia.
Jessica K HolienSchool of Science, STEM College, RMIT University, Melbourne, VIC, Australia.
Markus J HoferCharles Perkins Centre and School of Life and Environmental Sciences, The University of Sydney, Sydney, VIC, Australia.ORCID http://orcid.org/0000-0001-5111-3978
Donna R WhelanLa Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC, Australia.
Karla J HelbigDepartment of Microbiology, Anatomy, Physiology and Pharmacology, La Trobe University, Melbourne, VIC, Australia. k.helbig@latrobe.edu.au.ORCID http://orcid.org/0000-0001-6306-2821

Funding

Department of Health | National Health and Medical Research Council (NHMRC) APP1181434Department of Health | National Health and Medical Research Council (NHMRC) APP2033787Department of Health | National Health and Medical Research Council (NHMRC) APP2038548
6 · The paper itself

Abstract

Lipid droplets (LDs), once viewed as inert lipid storage sites, are now recognised as dynamic organelles central to cellular signalling and immunity. This study presents a dual-omics approach, integrating proteomics and lipidomics, to investigate LDs in the host antiviral response. In vivo and in vitro RNA viral infection models demonstrate that LDs rapidly remodel both their proteome and lipidome. The antiviral proteins RIG-I, MDA5, STAT1, STAT2, and viperin are specifically recruited to virus-induced LDs. Simultaneously, the LD lipidome shifts toward enrichment in long-chain polyunsaturated fatty acids and bioactive phospholipids, likely enhancing membrane dynamics and protein recruitment. Correlation analysis of matched proteomic and lipidomic datasets revealed extensive lipid-protein co-regulation on LDs and identified distinct correlation networks in which immune and antiviral proteins preferentially aligned with neutral lipid species. Enzymes involved in lipid metabolism and post-translational modifications are also upregulated, suggesting a mechanistic link between lipid remodeling and protein localisation. Functional assays utilizing artificial LDs revealed that arachidonic-acid and eicosapentaenoic-acid suppress viral replication and enhance type I and III interferon responses. These findings position LDs as key immunometabolic platforms in early antiviral defence.

Indexed as

Lipid DropletsLipidomicsProteomicsAnimalsHost-Pathogen InteractionsHumansLipid MetabolismMiceProteomeViperin ProteinVirus ReplicationProteomeViperin Protein

Identifiers

PMID42248863
PMCPMC13396240

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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.