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Subversion of host cellular functions by the apicomplexan parasites
Louise E Kemp1, Masahiro Yamamoto, Dominique Soldati-Favre
1Department of Microbiology and Molecular Medicine, Faculty of Medicine, University of Geneva, Geneva, Switzerland. louise.kemp@unige.ch
FEMS Microbiology Reviews
|November 29, 2012
Summary
Rhoptry kinases in Apicomplexa parasites, like Toxoplasma gondii, are crucial for subverting host cell functions. Understanding these rhoptry proteins aids in developing strategies against parasitic diseases.
Area of Science:
- Parasitology
- Cell Biology
- Molecular Biology
Background:
- Rhoptries are secretory organelles in Apicomplexa parasites, essential for host-pathogen interactions.
- Apicomplexa parasites cause significant human and animal diseases, including malaria and cryptosporidiosis.
- Rhoptry contents are compartmentalized into neck and bulb, with varying protein conservation and function.
Purpose of the Study:
- To review current knowledge on rhoptry proteins in Apicomplexa.
- To specifically discuss the role of rhoptry kinases in host cell subversion by coccidian parasites.
- To highlight the importance of rhoptry proteins in parasite survival and disease pathogenesis.
Main Methods:
- Literature review of studies on rhoptry proteins in Apicomplexa.
- Analysis of conserved and variable rhoptry proteins across different species.
- Focus on the function of rhoptry kinases in host cell manipulation.
Main Results:
- Rhoptry neck proteins are often conserved and involved in host cell invasion.
- Rhoptry bulb proteins are less conserved and adapted to specific parasite lifestyles.
- Rhoptry kinases in Toxoplasma gondii and related parasites actively subvert host cellular functions.
Conclusions:
- Rhoptry proteins play diverse roles, from host cell invasion to parasitophorous vacuole formation.
- Rhoptry kinases are key effectors used by coccidian parasites to manipulate host cells for survival.
- Further research into rhoptry proteins offers potential therapeutic targets for apicomplexan diseases.
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