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Cytoadherence-related homologous motifs in Plasmodium falciparum antigen Pf155/RESA and erythrocyte band 3 protein

Published online by Cambridge University Press:  06 April 2009

J. Iqbal
Affiliation:
Department of Immunology, Stockholm University, S-106 91 Stockholm, Sweden
A. B. Siddique
Affiliation:
Department of Immunology, Stockholm University, S-106 91 Stockholm, Sweden
N. Ahlborg
Affiliation:
Department of Immunology, Stockholm University, S-106 91 Stockholm, Sweden
P. Perlmann
Affiliation:
Department of Immunology, Stockholm University, S-106 91 Stockholm, Sweden
K. Berzins
Affiliation:
Department of Immunology, Stockholm University, S-106 91 Stockholm, Sweden

Summary

Cytoadherence of Plasmodium falciparum-infected erythrocytes plays an important role in the pathogenesis of cerebral malaria. The identity of cell surface molecules on parasitized erythrocytes involved in cytoadherence is of great interest to understand the molecular basis of this mechanism. Peptide sequences derived from exofacial loops of the erythrocyte antigen band 3 from parasitized erythrocytes have previously been shown to inhibit cytoadherence. We now report that a non-repeated region of Pf155/RESA (residues 213–218) contains a hexapeptide motif being highly homologous to cytoadherence inhibitory sequences from band 3. Synthetic peptides containing the hexapeptide motif of Pf155/RESA inhibited the binding of P.falciparum-infected erythrocytes to melanoma cells in vitro. Furthermore, individuals residing in malaria-endemic areas have antibodies reactive with epitopes involving these motifs in band 3 and in Pf155/RESA.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1995

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