Journal article
Polymorphisms in erythrocyte binding antigens 140 and 181 affect function and binding but not receptor specificity in Plasmodium falciparum
AG Maier, J Baum, B Smith, DJ Conway, AF Cowman
Infection and Immunity | Published : 2009
DOI: 10.1128/IAI.01331-08
Abstract
Invasion of human erythrocytes by the malaria parasite Plasmodium falciparum utilizes multiple ligand- receptor interactions involving erythrocyte receptors and parasite erythrocyte binding proteins of the Duffy binding-like family. Erythrocyte binding antigen 175 (EBA-175) binds to glycophorin A, the most abundant protein on the human erythrocyte surface and EBA-140 (also known as BAEBL) binds to glycophorin C, while the receptor for EBA-181 (also known as JESEBL) remains unknown. EBA binding is mediated via region II, a highly structured extracellular domain that shows a degree of sequence variability between different laboratory strains/isolates. Here, we determined the influence of regio..
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Awarded by Medical Research Council
Funding Acknowledgements
[ "We thank the Red Cross Blood Service (Melbourne, Australia) for the supply of erythrocytes and serum. Our thanks go to M. Cravino, M. O'Neill, M. Brown, M. Duraisingh, J. Thompson, and T. Triglia for their support. We thank Melanie Rug, Brendan Crabb, and Matthias Marti for critical comments. We are grateful to Joyce Poole and David Anstee from the Red Cell Reference Department of IBGRL (United Kingdom), Peter Zimmerman, Sheral Patel (Case Western University), and John Reeder (PNG Institute of Medical Research) for the mutant erythrocytes and the blood donors for their participation.", "A. G. M. is an ARC Australian Research Fellow, J. B. is recipient of an NHMRC Career Development Award and A. F. C. is a Howard Hughes International Scholar. This work was supported by the National Health and Medical Research Council of Australia and the Wellcome Trust." ]