Evidence map›Paper›PMID 27601221›Full record

ArticleEMBO reports2016

Natural mutations in IFITM3 modulate post-translational regulation and toggle antiviral specificity.

Alex A Compton, Nicolas Roy, Françoise Porrot, Anne Billet, Nicoletta Casartelli, Jacob S Yount, Chen Liang, Olivier Schwartz

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
5.8field-weighted citation impact, top 3% of its field
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

82 citing papers in PubMed, 112 citations in OpenAlex.

  1. Review
  2. Article
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  4. Review
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  9. Article
  10. IFITM1 and IFITM3 cooperate to restrict virus entry in endolysosomes.bioRxiv : the preprint server for biology · 2025
    Article
  11. mBio · 2025
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
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22 more citing papers are in PubMed but not listed here.

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

8 authors at 4 institutions in 3 countries.

Alex A ComptonVirus & Immunity Unit, Institut Pasteur, Paris, France alex.compton@pasteur.fr schwartz@pasteur.fr.ORCID 0000-0002-7508-4953
Nicolas RoyVirus & Immunity Unit, Institut Pasteur, Paris, France.
Françoise PorrotVirus & Immunity Unit, Institut Pasteur, Paris, France.
Anne BilletVirus & Immunity Unit, Institut Pasteur, Paris, France.
Nicoletta CasartelliVirus & Immunity Unit, Institut Pasteur, Paris, France.
Jacob S YountDepartment of Microbial Infection & Immunity, The Ohio State University, Columbus, OH, USA.
Chen LiangLady Davis Institute, McGill University, Montreal, QC, Canada.
Olivier SchwartzVirus & Immunity Unit, Institut Pasteur, Paris, France alex.compton@pasteur.fr schwartz@pasteur.fr.
Institut Pasteur · FRCentre National de la Recherche Scientifique · FRMcGill University · CAThe Ohio State University · US

Funding

Translational Therapeutics Research Program (TT)P30CA016058 · NCI · OHIO STATE UNIVERSITY · PI Tasleem J Padamsee · 1985 to 2026
$132.3M
NCI NIH HHS P30 CA016058
6 · The paper itself

Abstract

The interferon-induced transmembrane (IFITM) proteins protect host cells from diverse virus infections. IFITM proteins also incorporate into HIV-1 virions and inhibit virus fusion and cell-to-cell spread, with IFITM3 showing the greatest potency. Here, we report that amino-terminal mutants of IFITM3 preventing ubiquitination and endocytosis are more abundantly incorporated into virions and exhibit enhanced inhibition of HIV-1 fusion. An analysis of primate genomes revealed that IFITM3 is the most ancient antiviral family member of the IFITM locus and has undergone a repeated duplication in independent host lineages. Some IFITM3 genes in nonhuman primates, including those that arose following gene duplication, carry amino-terminal mutations that modify protein localization and function. This suggests that "runaway" IFITM3 variants could be selected for altered antiviral activity. Furthermore, we show that adaptations in IFITM3 result in a trade-off in antiviral specificity, as variants exhibiting enhanced activity against HIV-1 poorly restrict influenza A virus. Overall, we provide the first experimental evidence that diversification of IFITM3 genes may boost the antiviral coverage of host cells and provide selective functional advantages.

Indexed as

Evolution, MolecularHost-Pathogen InteractionsImmunity, InnateAnimalsCell LineGenomeHumansInterferon InducersMembrane ProteinsMutationPrimatesProtein TransportRNA-Binding ProteinsUbiquitinationVirusesIFITM3 protein, humanInterferon InducersMembrane ProteinsRNA-Binding ProteinsevolutionHIVIFITMinnate immunityvirus

Identifiers

PMID27601221
PMCPMC5090704
OpenAlexW2517466029

What OpenQuestion holds

Textmetadata
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.