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Originally published In Press as doi:10.1074/jbc.M211446200 on January 29, 2003

J. Biol. Chem., Vol. 278, Issue 16, 14480-14486, April 18, 2003
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A Novel Erythrocyte Binding Antigen-175 Paralogue from Plasmodium falciparum Defines a New Trypsin-resistant Receptor on Human Erythrocytes*

Tim-Wolf GilbergerDagger , Jennifer K. Thompson, Tony Triglia, Robert T. Good, Manoj T. Duraisingh, and Alan F. Cowman§

From The Walter and Eliza Hall Institute of Medical Research, Melbourne 3050, Australia

The recognition and invasion of human erythrocytes by the most lethal malaria parasite Plasmodium falciparum is dependent on multiple ligand-receptor interactions. Members of the erythrocyte binding-like (ebl) family, including the erythrocyte binding antigen-175 (EBA-175), are responsible for high affinity binding to glycoproteins on the surface of the erythrocyte. Here we describe a paralogue of EBA-175 and show that this protein (EBA-181/JESEBL) binds in a sialic acid-dependent manner to erythrocytes. EBA-181 is expressed at the same time as EBA-175 and co-localizes with this protein in the microneme organelles of asexual stage parasites. The receptor binding specificity of EBA-181 to erythrocytes differs from other members of the ebl family and is trypsin-resistant and chymotrypsin-sensitive. Furthermore, using glycophorin B-deficient erythrocytes we show that binding of EBA-181 is not dependent on this sialoglycoprotein. The level of expression of EBA-181 differs among parasite lines, and the importance of this ligand for invasion appears to be strain-dependent as the EBA-181 gene can be disrupted in W2mef parasites, without affecting the invasion phenotype, but cannot be targeted in 3D7 parasites.


* This work was supported by the National Health and Medical Research Council of Australia.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Funded by a Deutsche Forschunggemeinschaft Emmy Noether Fellowship.

§ A Howard Hughes International Scholar. To whom correspondence should be addressed: The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Melbourne, 3050, Australia. Tel.: 61-9345-2555; E-mail: cowman@wehi.edu.au.


Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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