Evidence map›Paper›PMID 40883327›Full record

ArticleNature communications2025

Structural basis of Fusobacterium nucleatum adhesin Fap2 interaction with receptors on cancer and immune cells.

Felix Schöpf, Gian L Marongiu, Klaudia Milaj, Thiemo Sprink, Judith Kikhney, Annette Moter, Daniel Roderer

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed, 1 pooled it
–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

20 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. The role of adhesins ofGut microbes · 2026
    Review
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  4. Article
  5. Article
  6. The Role of Selected Bacteria in Breast Cancer Initiation and Development.International journal of molecular sciences · 2026
    Review
  7. Review
  8. Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Review
  15. Review
  16. Review
  17. Cancers · 2025
    Review
  18. Review
  19. Structural basis for immune cell binding ofProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  20. Unraveling the Role ofCancers · 2025
    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

7 authors.

Felix SchöpfLeibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany.ORCID http://orcid.org/0000-0003-1929-6246
Gian L MarongiuLeibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Klaudia MilajLeibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Thiemo SprinkCore Facility for Cryo Electron Microscopy of the Charité-Universitätsmedizin Berlin at the Max Delbrück Center, Berlin, Germany.
Judith KikhneyInstitute of Medical Microbiology and Virology, University of Leipzig Medical Center, Leipzig, Germany.
Annette MoterInstitute of Medical Microbiology and Virology, University of Leipzig Medical Center, Leipzig, Germany.
Daniel RodererLeibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany. roderer@fmp-berlin.de.ORCID http://orcid.org/0000-0002-7276-3467

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) 548509121
6 · The paper itself

Abstract

Fusobacterium nucleatum is overrepresented in the colon microbiome of colorectal cancer patients and has been associated with tumor growth enhancement and metastasis. A pivotal pathogenic factor, the autotransporter adhesin Fap2, facilitates association to cancer and immune cells via the receptors Gal-GalNAc and TIGIT, respectively, leading to deactivation of immune cells. Mechanistic details of the Fap2/TIGIT interaction remain elusive as no structural data are available. Here, we report a system to recombinantly express functional Fap2 on the Escherichia coli surface, which interacts with Gal-GalNAc on cancer cells and with purified TIGIT with submicromolar affinity. Cryo-EM structures of Fap2, alone and in complex with TIGIT, show that the elongated ~50 nm long Fap2 extracellular region binds to TIGIT on its membrane-distal tip via an extension of a β-helix domain. Moreover, by combining structure predictions, cryo-EM, docking and molecular dynamics simulations, we identified a binding pit for Gal-GalNAc on the tip of Fap2.

Indexed as

Adhesins, BacterialFusobacterium nucleatumColorectal NeoplasmsCryoelectron MicroscopyEscherichia coliHumansMolecular Docking SimulationMolecular Dynamics SimulationProtein BindingAdhesins, Bacterial

Identifiers

PMID40883327
PMCPMC12397386

What OpenQuestion holds

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Registered trials

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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.