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Originally published In Press as doi:10.1074/jbc.M207985200 on October 14, 2002

J. Biol. Chem., Vol. 277, Issue 52, 50303-50310, December 27, 2002
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Phage-displayed Peptides Bind to the Malarial Protein Apical Membrane Antigen-1 and Inhibit the Merozoite Invasion of Host Erythrocytes*

Felomena LiDagger §, Anton Dluzewski, Andrew M. ColeyDagger §||, Alan Thomas**, Leann TilleyDagger §, Robin F. AndersDagger ||, and Michael FoleyDagger §||Dagger Dagger

From the Dagger  Department of Biochemistry, La Trobe University, Bundoora, 3083 Victoria, Australia, the Cooperative Research Centres for § Diagnostics and || Vaccine Technologies and  the Department of Immunobiology, New Guy's House, King's College, London SE1 9RT, United Kingdom, and the ** Department of Parasitology, Biomedical Primate Research Centre, 2280 GH Rijswijk, The Netherlands

Apical membrane antigen-1 (AMA1) is a transmembrane protein present on the surface of merozoites that is thought to be involved in the process of parasite invasion of host erythrocytes. Although it is the target of a natural immune response that can inhibit invasion, little is known about the molecular mechanisms by which AMA1 facilitates the invasion process. In an attempt to identify peptides that specifically interact with and block the function of AMA1, a random peptide library displayed on the surface of filamentous phage was panned on recombinant AMA1 from Plasmodium falciparum. Three peptides with affinity for AMA1 were isolated, and characterization of their fine binding specificities indicated that they bind to a similar region on the surface of AMA1. One of these peptides was found to be a potent inhibitor of the invasion of P. falciparum merozoites into human erythrocytes. We propose that this peptide blocks interaction between AMA1 and a ligand on the erythrocyte surface that is involved in a critical step in malarial invasion. The identification and characterization of these peptide inhibitors now permit an evaluation of the essential requirements that are necessary for efficient neutralization of merozoite invasion by blocking AMA1 function.

* This work was supported in part by the Australian Research Council and the National Health and Medical Research Council of Australia, and by travel awards from the Australian Society of Parasitology, the Royal Society, and the Wellcome Trust (United Kingdom) (to A. D.).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 Dagger To whom correspondence should be addressed: Dept. of Biochemistry, La Trobe University, Bundoora, 3083 Victoria, Australia. Tel.: 61-3-9479-2158; Fax: 61-3-9479-2467; E-mail: m.foley@latrobe.edu.au.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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