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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
A Novel Erythrocyte Binding Antigen-175 Paralogue from
Plasmodium falciparum Defines a New Trypsin-resistant
Receptor on Human Erythrocytes*
Tim-Wolf
Gilberger ,
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.
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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Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.
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