Abstract
The availability of the full genomes of the malarial parasite Plasmodium falciparum and its two hosts, man and Anopheles gambiae, has dramatically increased the demand for protein display systems to study host/parasite interactions at the molecular level. Here, we explored the potential of a Saccharomyces cerevisiae expression and display system that allows proteins of interest to be targeted to the yeast surface. As proof of this principle, we used a P. falciparum erythrocyte membrane protein 1 DBL3γ domain which mediates the binding of P. falciparum-infected erythrocytes to chondroitin-4-sulfate, a host receptor involved in parasite sequestration in the placenta. Our data revealed localization of the DBL3γ domain to the yeast surface, demonstrating the value of the yeast system as a tool for displaying P. falciparum protein fragments. However, binding of the respective yeast strains to chondroitin-4-sulfate could not be demonstrated.
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Acknowledgements
This work was supported by a grant from the European Commission (BIOMALPAR). We thank Dr. Scherf for providing us with DBL3γ specific antisera and thank Elisabeth Wilken, Kathrin Steigleder and Nicole Klatt for technical support. All experiments were performed in agreement with current German laws.
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Schieck, E., Sanchez, C.P. & Lanzer, M. Targeting a DBL3γ domain of the Plasmodium falciparum erythrocyte membrane protein 1 to the surface of Saccharomyces cerevisiae . Parasitol Res 93, 318–321 (2004). https://doi.org/10.1007/s00436-004-1140-6
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DOI: https://doi.org/10.1007/s00436-004-1140-6