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Structural basis of Fusobacterium nucleatum adhesin Fap2 interaction with receptors on cancer and immune cells
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Structural basis of Fusobacterium nucleatum adhesin Fap2 interaction with receptors on cancer and immune cells
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Journal Article
Structural basis of Fusobacterium nucleatum adhesin Fap2 interaction with receptors on cancer and immune cells
2025
Overview
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.
Fusobacterium nucleatum promotes colorectal cancer via its adhesin Fap2. Here, Schöpf et al. show the molecular basis for Fap2 interaction with its receptors TIGIT on immune cells and Gal-GalNAc on tumor cells using cryo-EM and integrative modeling.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 14/63
/ 631/57
/ 82/103
/ 82/80
/ 82/83
/ Adhesins, Bacterial - chemistry
/ Adhesins, Bacterial - genetics
/ Adhesins, Bacterial - metabolism
/ Adhesins, Bacterial - ultrastructure
/ Cancer
/ Colorectal Neoplasms - microbiology
/ E coli
/ Escherichia coli - metabolism
/ Fusobacterium nucleatum - immunology
/ Fusobacterium nucleatum - metabolism
/ Genomes
/ Humanities and Social Sciences
/ Humans
/ Molecular Docking Simulation
/ Molecular Dynamics Simulation
/ Proteins
/ Science
/ Tumors
