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Updated: Oct 24, 2025
09:26
Identification of Antibacterial Immunity Proteins in Escherichia coli using MALDI-TOF-TOF-MS/MS and Top-Down Proteomic Analysis
Published on: May 23, 2021
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CEACAM1 Activation by CbpF-Expressing E. coli
Amjad Shhadeh1, Johanna Galaski2,3, Tamar Alon-Maimon1
1The Institute of Dental Sciences, The Hebrew University-Hadassah School of Dental Medicine, Jerusalem, Israel.
Frontiers in Cellular and Infection Microbiology
|August 16, 2021
Summary
Fusobacterium nucleatum, a bacterium linked to cancer, can evade immune responses. A specific bacterial protein, CbpF, activates the CEACAM1 receptor, hindering anti-tumor immunity.
Area of Science:
- Microbiology and Immunology
- Cancer Research
Background:
- Fusobacterium nucleatum, an oral bacterium, is implicated in various cancers, including colorectal, esophageal, and breast cancer.
- F. nucleatum can inhibit anti-tumor immunity by binding and activating inhibitory receptors TIGIT and CEACAM1 on T and NK cells.
- The fusobacterial trimeric autotransporter adhesin CbpF has been identified as a molecule that binds and activates CEACAM1.
Purpose of the Study:
- To investigate the role of CbpF in activating the CEACAM1 receptor.
- To generate a functional recombinant CbpF protein for further study.
Main Methods:
- Generation of a recombinant Escherichia coli strain engineered to express the full-length CbpF protein.
- Assays to confirm the binding and activation of the human CEACAM1 receptor by the recombinant CbpF.
Main Results:
- Successfully generated a recombinant E. coli expressing full-length CbpF.
- The recombinant CbpF demonstrated efficient binding to and activation of the CEACAM1 receptor.
Conclusions:
- The CbpF protein from Fusobacterium nucleatum effectively binds and activates CEACAM1.
- This interaction provides a potential mechanism for F. nucleatum to suppress anti-tumor immunity, offering a target for therapeutic strategies.
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