| Summary: | <p>Abstract</p> <p>Background</p> <p>The development of <it>Plasmodium falciparum </it>within human erythrocytes induces a wide array of changes in the ultrastructure, function and antigenic properties of the host cell. Numerous proteins encoded by the parasite have been shown to interact with the erythrocyte membrane. The identification of new interactions between human erythrocyte and <it>P. falciparum </it>proteins has formed a key area of malaria research. To circumvent the difficulties provided by conventional protein techniques, a novel application of the phage display technology was utilised.</p> <p>Methods</p> <p><it>P. falciparum </it>phage display libraries were created and biopanned against purified erythrocyte membrane proteins. The identification of interacting and in-frame amino acid sequences was achieved by sequencing parasite cDNA inserts and performing bioinformatic analyses in the PlasmoDB database.</p> <p>Results</p> <p>Following four rounds of biopanning, sequencing and bioinformatic investigations, seven <it>P. falciparum </it>proteins with significant binding specificity toward human erythrocyte spectrin and protein 4.1 were identified. The specificity of these <it>P. falciparum </it>proteins were demonstrated by the marked enrichment of the respective in-frame binding sequences from a fourth round phage display library.</p> <p>Conclusion</p> <p>The construction and biopanning of <it>P. falciparum </it>phage display expression libraries provide a novel approach for the identification of new interactions between the parasite and the erythrocyte membrane.</p>
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