ArticleMolecular microbiology2008
Binding of Dr adhesins of Escherichia coli to carcinoembryonic antigen triggers receptor dissociation.
Article in Molecular microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
What it found
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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.
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.
Who cites it
37 citing papers in PubMed, 62 citations in OpenAlex.
- CEA-4-1BBL: CEACAM5-Targeted 4-1BB Ligand Fusion Proteins for Cis Co-Stimulation with CEA-TCB.Antibodies (Basel, Switzerland) · 2025Article
- Artificial intelligence prediction of carcinoembryonic antigen structure and interactions relevant for colorectal cancer.Biochemistry and biophysics reports · 2025Article
- Structural aspects of CEACAM1 interactions.European journal of clinical investigation · 2024Review
- Magic-angle spinning NMR structure of Opa60 in lipid bilayers.Journal of structural biology: X · 2024Article
- Interactions of pathogenicFrontiers in immunology · 2023Review
- A Novel ssDNA Aptamer Targeting Carcinoembryonic Antigen: Selection and Characterization.Biology · 2022Article
- Structural analysis of human CEACAM1 oligomerization.Communications biology · 2022Article
- Human CEACAM1 N-domain dimerization is independent from glycan modifications.Structure (London, England : 1993) · 2022Article
- Inhibitory pattern recognition receptors.The Journal of experimental medicine · 2022Review
- The Visualization of Protein-Protein Interactions in Breast Cancer: Deployment Study in Pathological Examination.Acta histochemica et cytochemica · 2021Review
- Bacterial protein domains with a novel Ig-like fold target human CEACAM receptors.The EMBO journal · 2021Article
- Structural basis of the dynamic human CEACAM1 monomer-dimer equilibrium.Communications biology · 2021Article
- Imaging Flow Cytometry Analysis of CEACAM Binding to Opa-Expressing Neisseria gonorrhoeae.Cytometry. Part A : the journal of the International Society for Analytical Cytology · 2020Article
- MrpH, a new class of metal-binding adhesin, requires zinc to mediate biofilm formation.PLoS pathogens · 2020Article
- CEACAM1 structure and function in immunity and its therapeutic implications.Seminars in immunology · 2019Review
- Article
- A new biosensor detection system to overcome the Debye screening effect: dialysis-silicon nanowire field effect transistor.International journal of nanomedicine · 2019Article
- CEACAM3-A Prim(at)e Invention for Opsonin-Independent Phagocytosis of Bacteria.Frontiers in immunology · 2019Review
- Article
- TheThe EMBO journal · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 5 institutions in 4 countries.
Funding
Abstract
Carcinoembryonic antigen (CEA)-related cell adhesion molecules (CEACAMs) are host receptors for the Dr family of adhesins of Escherichia coli. To define the mechanism for binding of Dr adhesins to CEACAM receptors, we carried out structural studies on the N-terminal domain of CEA and its complex with the Dr adhesin. The crystal structure of CEA reveals a dimer similar to other dimers formed by receptors with IgV-like domains. The structure of the CEA/Dr adhesin complex is proposed based on NMR spectroscopy and mutagenesis data in combination with biochemical characterization. The Dr adhesin/CEA interface overlaps appreciably with the region responsible for CEA dimerization. Binding kinetics, mutational analysis and spectroscopic examination of CEA dimers suggest that Dr adhesins can dissociate CEA dimers prior to the binding of monomeric forms. Our conclusions include a plausible mechanism for how E. coli, and perhaps other bacterial and viral pathogens, exploit CEACAMs. The present structure of the complex provides a powerful tool for the design of novel inhibitory strategies to treat E. coli infections.
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What OpenQuestion holds
Registered trials
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.