Identification of genes involved in signalling during host cell invasion by the apicomplexan parasite Toxoplasma gondii
Zusammenfassung der Projektergebnisse
Firstly the methodology to identify parasite phosphorylation sites on a large scale is now established and can be used for directed differential phosphoproteome studies. Secondly, knowledge about phosphorylation sites in the parasites will in the future enable stringent kinase phosphorylation network analysis when we better understand the motifs that a specific kinase can phosphorylate. Methods to test kinase phosphorylation motifs have recently been developed and their use in parasite research will complement phosphoproteome studies. Thirdly, the identification of unusual phosphorylation motifs that might be accompanied by structural changes in the kinase’s active center might lead to development of novel therapeutic strategies when structural information of such kinases becomes available. Finally, the identification of a substantial number of parasite proteins that are phosphorylated after being infected into the host cell, presumably by parasite kinases (and to some extend also host kinases) revealed that apicomplexan parasites likely regulate their own proteins after secretion into the parasitophorous vacuole (which is thought to be devoid of host proteins) and into the host cell. This is an exciting field of study as both parasites dramatically remodel their respective host-cells for their specific needs. It is also likely to be a regulatory mechanism for organisms living within a cell to interact with their hosts symbiotically or parasitically.
Projektbezogene Publikationen (Auswahl)
- Cell Host & Microbe, October 2011:The Phosphoproteomes of Plasmodium falciparum and Toxoplasma gondii Reveal Unusual Adaptations Within and Beyond the Parasite’s Boundaries
Treeck M, Sanders JL, Elias JE & Boothroyd JC
- Trends in Parasitology, September 2011: Focus on the ringleader: the role of the AMA1 in apicomplexan host cell invasion and replication
Tyler JS, Treeck M, & Boothroyd JC
