Journal article
Interactions between Plasmodium falciparum skeleton-binding protein 1 and the membrane skeleton of malaria-infected red blood cells
LM Kats, NI Proellocks, DW Buckingham, L Blanc, J Hale, X Guo, X Pei, S Herrmann, EG Hanssen, RL Coppel, N Mohandas, X An, BM Cooke
Biochimica Et Biophysica Acta Biomembranes | Published : 2015
Abstract
Abstract During development inside red blood cells (RBCs), Plasmodium falciparum malaria parasites export proteins that associate with the RBC membrane skeleton. These interactions cause profound changes to the biophysical properties of RBCs that underpin the often severe and fatal clinical manifestations of falciparum malaria. P. falciparum erythrocyte membrane protein 1 (PfEMP1) is one such exported parasite protein that plays a major role in malaria pathogenesis since its exposure on the parasitised RBC surface mediates their adhesion to vascular endothelium and placental syncytioblasts. En route to the RBC membrane skeleton, PfEMP1 transiently associates with Maurer's clefts (MCs), paras..
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Awarded by National Institutes of Health
Funding Acknowledgements
This work was supported by grants from the National Health and Medical Research Council of Australia (NHMRC) (Project Grant 606447 to BMC and Fellowships 545831 to BMC and 606734 to LMK) and by the National Institutes of Health (DK 26263 and DK 32094 and DK 100810). We thank the Australian Red Cross Blood Service for generously providing human red blood cells for in vitro malaria culture.