Journal
FEMS MICROBIOLOGY REVIEWS
Volume 37, Issue 4, Pages 607-631Publisher
OXFORD UNIV PRESS
DOI: 10.1111/1574-6976.12013
Keywords
rhoptry organelle; parasitophorous vacuole; secreted kinases; effector molecules; Toxoplasma gondii; immune evasion
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Funding
- FP7 [215281]
- Swiss National Science Foundation [FN3100A0-116722]
- Japanese-Swiss Science and Technology Program
- Ministry of Education, Culture, Sports, Science and Technology
- Kato Memorial Bioscience Foundation
- Mochida Memorial Foundation for Medical and Pharmaceutical Research
- Waksman Foundation of Japan INC
- Tokyo Biochemical Research Foundation
- Research Foundation for Microbial Diseases of Osaka University
- Nakajima Foundation
- Asahi Glass Foundation
- Osaka Foundation for Promotion of Clinical Immunology
- Senri Life Science Foundation
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Rhoptries are club-shaped secretory organelles located at the anterior pole of species belonging to the phylum of Apicomplexa. Parasites of this phylum are responsible for a huge burden of disease in humans and animals and a loss of economic productivity. Members of this elite group of obligate intracellular parasites include Plasmodium spp. that cause malaria and Cryptosporidium spp. that cause diarrhoeal disease. Although rhoptries are almost ubiquitous throughout the phylum, the relevance and role of the proteins contained within the rhoptries varies. Rhoptry contents separate into two intra-organellar compartments, the neck and the bulb. A number of rhoptry neck proteins are conserved between species and are involved in functions such as host cell invasion. The bulb proteins are less well-conserved and probably evolved for a particular lifestyle. In the majority of species studied to date, rhoptry content is involved in formation and maintenance of the parasitophorous vacuole; however some species live free within the host cytoplasm. In this review, we will summarise the knowledge available regarding rhoptry proteins. Specifically, we will discuss the role of the rhoptry kinases that are used by Toxoplasma gondii and other coccidian parasites to subvert the host cellular functions and prevent parasite death.
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