Alveolins are intermediate filament proteins that are exclusively found in apicomplexan parasites (causative agents of for example malaria, toxoplasmosis, cryptosporidiosis), dinoflagellate algea and ciliates. Alveolins are defined by possessing 12 amino-acid tandem repeat structures in their functional domains, which resemble those of other protozoan cytoskeletal proteins like articulins. In malaria parasites, alveolins are essential for cell development across the life cycle and as such form attractive targets for disease control. This project aims to determine the core architecture and atomic structure of the alveolins, as well as the underlying mechanisms for their assembly into the cortical cytoskeleton of malaria parasites.
Al-Khattaf FS, Tremp AZ, Dessens JT (2015). Plasmodium alveolins possess distinct, but functionally and structurally related multi-repeat domains. Parasitology Research 114:631-39.
Tremp AZ, Al-Khattaf FS, Dessens JT (2014). Distinct temporal recruitment of Plasmodium alveolins to the subpellicular network. Parasitology Research 113:4177-88.
Tremp AZ and Dessens JT (2011). Malaria IMC1 membrane skeleton proteins operate autonomously and participate in motility independently of cell shape. Journal of Biological Chemistry 286:5383-91.
Tremp AZ, Khater EI and Dessens JT (2008). IMC1b is a membrane skeleton protein involved in cell shape, mechanical strength, motility and infectivity of malaria ookinetes. Journal of Biological Chemistry 283:27604-11.
Khater EI, Sinden RE and Dessens JT (2004). A malaria membrane skeletal protein is essential for normal morphogenesis, motility and infectivity of sporozoites. Journal of Cell Biology 167:425-32.