Journal article
Tracking glideosome-associated protein 50 reveals the development and organization of the inner membrane complex of Plasmodium falciparum
JA Yeoman, E Hanssen, AG Maier, N Klonis, B Maco, J Baum, L Turnbull, CB Whitchurch, MWA Dixon, L Tilley
Eukaryotic Cell | Published : 2011
DOI: 10.1128/EC.00244-10
Abstract
The most deadly of the human malaria parasites, Plasmodium falciparum, has different stages specialized for invasion of hepatocytes, erythrocytes, and the mosquito gut wall. In each case, host cell invasion is powered by an actin-myosin motor complex that is linked to an inner membrane complex (IMC) via a membrane anchor called the glideosome-associated protein 50 (PfGAP50). We generated P. falciparum transfectants expressing green fluorescent protein (GFP) chimeras of PfGAP50 (PfGAP50-GFP). Using immunoprecipitation and fluorescence photobleaching, we show that C-terminally tagged PfGAP50-GFP can form a complex with endogenous copies of the linker protein PfGAP45 and the myosin A tail domai..
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Funding Acknowledgements
We acknowledge support from the Australian Research Council and the Australian National Health and Medical Research Council. C. B. W. is an Australian National Health and Medical Research Council Senior Research Fellow. M. W. A. D. is an Australian National Health and Medical Research Council Training Fellow. A. G. M. is an ARC Australian Research Fellow.