ArticleInfection and immunity2002
Carcinoembryonic antigen family receptor recognition by gonococcal Opa proteins requires distinct combinations of hypervariable Opa protein domains.
Article in Infection and immunity, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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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.
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Who cites it
28 citing papers in PubMed, 47 citations in OpenAlex.
- Diversity and evolution of a phase-variable multi-locus antigen in Neisseria gonorrhoeae.PLoS pathogens · 2026Article
- Diversity and evolution of a phase-variable multi-locus antigen inbioRxiv : the preprint server for biology · 2026Article
- Neutrophil CEACAMs and the Inflammatory Response toJournal of innate immunity · 2026Review
- Magic-angle spinning NMR structure of Opa60 in lipid bilayers.Journal of structural biology: X · 2024Article
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- Article
- Variable Expression of Opa Proteins by Neisseria gonorrhoeae Influences Bacterial Association and Phagocytic Killing by Human Neutrophils.Journal of bacteriology · 2022Article
- Proton Detected Solid-State NMR of Membrane Proteins at 28 Tesla (1.2 GHz) and 100 kHz Magic-Angle Spinning.Biomolecules · 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
- Quantifying Carcinoembryonic Antigen-like Cell Adhesion Molecule-Targeted Liposome Delivery Using Imaging Flow Cytometry.Molecular pharmaceutics · 2019Article
- CEACAM1 structure and function in immunity and its therapeutic implications.Seminars in immunology · 2019Review
- Neisseria gonorrhoeae MlaA influences gonococcal virulence and membrane vesicle production.PLoS pathogens · 2019Article
- Refinement of Highly Flexible Protein Structures using Simulation-Guided Spectroscopy.Angewandte Chemie (International ed. in English) · 2018Article
- Gonococcal Defenses against Antimicrobial Activities of Neutrophils.Trends in microbiology · 2018Review
- Neisserial Opa Protein-CEACAM Interactions: Competition for Receptors as a Means of Bacterial Invasion and Pathogenesis.Biochemistry · 2016Article
- Expression of Opacity Proteins Interferes with the Transmigration of Neisseria gonorrhoeae across Polarized Epithelial Cells.PloS one · 2015Article
- Structure of the Neisserial outer membrane protein Opa₆₀: loop flexibility essential to receptor recognition and bacterial engulfment.Journal of the American Chemical Society · 2014Article
- The biology of Neisseria adhesins.Biology · 2013Article
- Innate recognition by neutrophil granulocytes differs between Neisseria gonorrhoeae strains causing local or disseminating infections.Infection and immunity · 2013Article
- Neisseria meningitidis has two independent modes of recognizing its human receptor CEACAM1.PloS one · 2011Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Neisserial Opa proteins function as a family of adhesins that bind heparan sulfate proteoglycan (HSPG) or carcinoembryonic antigen family (CEACAM) receptors on human host cells. In order to define the CEACAM binding domain on Opa proteins, we tested the binding properties of a series of gonococcal (strain MS11) recombinants producing mutant and chimeric Opa proteins with alterations in one or more of the four surface-exposed loops. Mutagenesis demonstrated that the semivariable domain, present in the first loop, was completely dispensable for CEACAM binding. In contrast, the two hypervariable (HV) regions present in the second and third loops were essential for binding; deletion of either domain resulted in loss of receptor recognition. Deletion of the fourth loop resulted in a severe decrease in Opa expression at the cell surface and could therefore not be tested for CEACAM binding. Chimeric Opa variants, containing combinations of HV regions derived from different CEACAM binding Opa proteins, lost most of their receptor binding activity. Some chimeric variants gained HSPG binding activity. Together, our results indicate that full recognition of CEACAM receptors by Opa proteins requires a highly coordinate interplay between both HV regions. Furthermore, shuffling of HV regions may result in novel HSPG receptor binding activity.
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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.