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A more recent version of this article appeared on December 20, 2002
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M207985200v1
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Papers In Press, published online ahead of print October 14, 2002
J. Biol. Chem, 10.1074/jbc.M207985200
Submitted on August 6, 2002
Revised on October 14, 2002
Accepted on October 14, 2002

Phage display peptides bind to the malarial protein apical membrane antigen-1 and inhibit the invasion of merozoites into host erythrocytes

Felomena Li, Anton Dluzewski, Andrew M. Coley, Alan W. Thomas, Leann Tilley, Robin F. Anders, and Michael Foley

Biochemistry, La Trobe University, Melbourne, Victoria 3083

Corresponding Author: acoley{at}bioserve.latrobe.edu.au

AMA1 is a transmembrane protein present on the surface of merozoites that is thought to be involved in the process of parasite invasion into the 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 could facilitate 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 a characterisation 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. It is proposed that this peptide blocks an interaction between AMA1 and a ligand on the erythrocyte surface that is involved in a critical step in malaria invasion. The identification and characterisation of these peptide inhibitors now permit an evaluation of the essential requirements that are necessary for efficient neutralisation of merozoite invasion by blocking AMA1 function.


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