Journal article
Parasite-encoded Hsp40 proteins define novel mobile structures in the cytosol of the P. falciparum-infected erythrocyte
S Külzer, M Rug, K Brinkmann, P Cannon, A Cowman, K Lingelbach, GL Blatch, AG Maier, JM Przyborski
Cellular Microbiology | WILEY | Published : 2010
Abstract
Plasmodium falciparum is predicted to transport over 300 proteins to the cytosol of its chosen host cell, the mature human erythrocyte, including 19 members of the Hsp40 family. Here, we have generated transfectant lines expressing GFP- or HA-Strep-tagged versions of these proteins, and used these to investigate both localization and other properties of these Hsp40 co-chaperones. These fusion proteins labelled punctate structures within the infected erythrocyte, initially suggestive of a Maurer's clefts localization. Further experiments demonstrated that these structures were distinct from the Maurer's clefts in protein composition. Transmission electron microscopy verifies a non-cleft local..
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Awarded by DFG Graduate School
Funding Acknowledgements
G.B., K.L. and J.M.P. are supported by a DFG grant as part of the 'German-African Cooperation Projects in Infectology'. S.K. was supported by a PhD scholarship of the DFG Graduate School GK1216 (Inter- and intracellular Trafficking and Communication, IITC). A.G.M. is an ARC Australian Research Fellow, and M.R. and A.G.M. are recipients of a grant from the National Health and Medical Research Council of Australia. Part of this work was carried out by K.B. during his MSc thesis work. We wish to thank Hans-Peter Beck, Catherine Braun-Breton, Hagai Ginsburg, Peter Preiser, Ralf Jacob, the Australian Red Cross blood bank and the employees of the Marburg University Hospital blood bank for essential reagents and thoughtful discussions, and Christine Langer for technical assistance (EM). We also wish to acknowledge the huge contribution of the PlasmoDB team to functional genomics in the Plasmodium system (Aurrecoechea et al., 2009).