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