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Updated: Mar 17, 2026

Visualisation and Quantification of Intracellular Interactions of Neisseria meningitidis and Human α-actinin by Confocal Imaging
Published on: October 24, 2010
Neisserial Opa Protein-CEACAM Interactions: Competition for Receptors as a Means of Bacterial Invasion and
Jennifer N Martin1, Louise M Ball1, Tsega L Solomon1
1Department of Chemistry and ‡Department of Microbiology, Immunology, and Cancer Biology, University of Virginia , Charlottesville, Virginia 22903, United States.
Abstract:
Carcino-embryonic antigen-like cellular adhesion molecules (CEACAMs), members of the immunoglobulin superfamily, are responsible for cell-cell interactions and cellular signaling events. Extracellular interactions with CEACAMs have the potential to induce phagocytosis, as is the case with pathogenic Neisseria bacteria. Pathogenic Neisseria species express opacity-associated (Opa) proteins, which interact with a subset of CEACAMs on human cells, and initiate the engulfment of the bacterium. We demonstrate that recombinant Opa proteins reconstituted into liposomes retain the ability to recognize and interact with CEACAMs in vitro but do not maintain receptor specificity compared to that of Opa proteins natively expressed by Neisseria gonorrhoeae. We report that two Opa proteins interact with CEACAMs with nanomolar affinity, and we hypothesize that this high affinity is necessary to compete with the native CEACAM homo- and heterotypic interactions in the host. Understanding the mechanisms of Opa protein-receptor recognition and engulfment enhances our understanding of Neisserial pathogenesis. Additionally, these mechanisms provide insight into how human cells that are typically nonphagocytic can utilize CEACAM receptors to internalize exogenous matter, with implications for the targeted delivery of therapeutics and development of imaging agents.
Insights
Pathogenic bacteria use Opa proteins to interact with CEACAMs, triggering cell engulfment. Recombinant Opa proteins bind CEACAMs but lack native specificity, offering insights into bacterial invasion and therapeutic delivery.
Area of Science:
- Microbiology
- Cell Biology
- Immunology
Background:
- Carcino-embryonic antigen-like cellular adhesion molecules (CEACAMs) mediate cell-cell interactions and signaling.
- Pathogenic Neisseria bacteria utilize Opa proteins to engage CEACAMs, inducing host cell phagocytosis.
- Understanding this interaction is crucial for Neisserial pathogenesis and host cell manipulation.
Purpose of the Study:
- To investigate the in vitro interaction of recombinant Opa proteins with CEACAMs.
- To compare the receptor specificity of recombinant Opa proteins with native Opa proteins.
- To explore the implications of CEACAM-mediated engulfment for therapeutic applications.
Main Methods:
- Reconstitution of Opa proteins into liposomes.
- In vitro binding assays with CEACAMs.
- Affinity measurements using techniques like surface plasmon resonance (SPR).
Main Results:
- Recombinant Opa proteins recognize and bind CEACAMs in vitro.
- Receptor specificity is not fully maintained in recombinant Opa proteins compared to native forms.
- Two Opa proteins exhibit nanomolar affinity for CEACAMs, suggesting a mechanism to overcome host cell interactions.
Conclusions:
- High-affinity Opa protein-CEACAM interactions are essential for Neisserial invasion.
- CEACAMs can be exploited by pathogens to induce phagocytosis in non-professional phagocytic cells.
- These findings have potential applications in targeted drug delivery and imaging agent development.
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