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TitleStructural basis of Fusobacterium nucleatum adhesin Fap2 interaction with receptors on cancer and immune cells.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 8104, Year 2025
Publish dateAug 29, 2025
AuthorsFelix Schöpf / Gian L Marongiu / Klaudia Milaj / Thiemo Sprink / Judith Kikhney / Annette Moter / Daniel Roderer /
PubMed AbstractFusobacterium 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 ...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.
External linksNat Commun / PubMed:40883327 / PubMed Central
MethodsEM (single particle)
Resolution4.4 - 6.0 Å
Structure data

EMDB-53048: Extracellular domain of the Fap2 autotransporter adhesin from Fusobacterium nucleatum ATCC23726
Method: EM (single particle) / Resolution: 4.7 Å

53049

9qe7

EMDB-53049, PDB-9qe7:
Membrane-distal part of extracellular domain of the Fap2 autotransporter adhesin from Fusobacterium nucleatum ATCC23726
Method: EM (single particle) / Resolution: 4.4 Å

EMDB-53052: Complex of Fap2 from Fusobacterium nucleatum with human TIGIT
Method: EM (single particle) / Resolution: 6.0 Å

Source
  • fusobacterium nucleatum (bacteria)
  • Homo sapiens (human)
KeywordsCELL ADHESION / Type V secretion system / autotransporter / colorectal cancer / bacterial adhesion

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