Targeting a DBL3gamma domain of the Plasmodium falciparum erythrocyte membrane protein 1 to the surface of Saccharomyces cerevisiae.
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 DBL3gamma 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 DBL3gamma 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.
Schieck
Elise
E
Hygiene Institute, Department of Parasitology, University of Heidelberg, Im Neuenheimer Feld 324, Heidelberg, Germany.
Sanchez
Cecilia P
CP
Lanzer
Michael
M
D000818:Animals; D001665:Binding Sites; D020134:Catalytic Domain / Q000235:genetics*; D002809:Chondroitin Sulfates / Q000378:metabolism; D004912:Erythrocytes / Q000378:metabolism / Q000469:parasitology*; D015966:Gene Expression Regulation, Fungal; D006790:Host-Parasite Interactions; D010963:Plasmodium falciparum / Q000235:genetics* / Q000378:metabolism; D015800:Protozoan Proteins / Q000235:genetics* / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000378:metabolism
D015800:Protozoan Proteins; C085731:erythrocyte membrane protein 1, Plasmodium falciparum; D002809:Chondroitin Sulfates