Related Experiment Video
Updated: Apr 16, 2026

Biomimetic Materials to Characterize Bacteria-host Interactions
Published on: November 16, 2015
The apicomplexan glideosome and adhesins - Structures and function
Lauren E Boucher1, Jürgen Bosch1
1Department of Biochemistry and Molecular Biology, Johns Hopkins Bloomberg School of Public Health, 615 N Wolfe St, Baltimore, MD 21205, USA; Johns Hopkins Malaria Research Institute, Johns Hopkins Bloomberg School of Public Health, 615 N Wolfe St, Baltimore, MD 21205, USA.
Abstract:
The apicomplexan family of pathogens, which includes Plasmodium spp. and Toxoplasma gondii, are primarily obligate intracellular parasites and invade multiple cell types. These parasites express extracellular membrane protein receptors, adhesins, to form specific pathogen-host cell interaction complexes. Various adhesins are used to invade a variety of cell types. The receptors are linked to an actomyosin motor, which is part of a complex comprised of many proteins known as the invasion machinery or glideosome. To date, reviews on invasion have focused primarily on the molecular pathways and signals of invasion, with little or no structural information presented. Over 75 structures of parasite receptors and glideosome proteins have been deposited with the Protein Data Bank. These structures include adhesins, motor proteins, bridging proteins, inner membrane complex and cytoskeletal proteins, as well as co-crystal structures with peptides and antibodies. These structures provide information regarding key interactions necessary for target receptor engagement, machinery complex formation, how force is transmitted, and the basis of inhibitory antibodies. Additionally, these structures can provide starting points for the development of antibodies and inhibitory molecules targeting protein-protein interactions, with the aim to inhibit invasion. This review provides an overview of the parasite adhesin protein families, the glideosome components, glideosome architecture, and discuss recent work regarding alternative models.
Insights
Apicomplexan parasites like Plasmodium use adhesins and the glideosome invasion machinery to enter host cells. Structural data reveals key interactions for developing new anti-invasion therapies.
Area of Science:
- Parasitology
- Structural Biology
- Molecular Cell Biology
Background:
- Apicomplexan parasites (e.g., Plasmodium, Toxoplasma) are obligate intracellular pathogens.
- They utilize adhesins and a protein complex called the glideosome for host cell invasion.
- Previous invasion reviews lacked detailed structural insights.
Purpose of the Study:
- To review the structural basis of apicomplexan parasite invasion.
- To highlight the role of adhesins and glideosome components.
- To discuss the potential for structure-based therapeutic development.
Main Methods:
- Analysis of over 75 Protein Data Bank structures of parasite invasion proteins.
- Review of existing literature on apicomplexan invasion mechanisms.
- Discussion of recent findings on glideosome architecture and function.
Main Results:
- Structural data is available for key adhesins, motor proteins, and cytoskeletal components of the invasion machinery.
- Structures elucidate critical protein-protein interactions in receptor engagement and force transmission.
- Co-crystal structures reveal potential targets for inhibitory antibodies and small molecules.
Conclusions:
- Structural biology provides crucial insights into apicomplexan parasite invasion mechanisms.
- Understanding these structures can guide the development of novel anti-parasitic strategies.
- Further research into glideosome architecture and alternative invasion models is warranted.
Related Concept Videos
Glycocalyx and its Functions
Surface Appendages of Archaea
Immunoglobulin-like Cell Adhesion Molecules
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Adherens Junctions
Adherens Junctions are Dynamic
Cancer Cell Migration through Invadopodia
Clathrin Coated Vesicles

