The University of Georgia College of Veterinary Medicine

Georgia Veterinary Scholar Program

Georgia Veterinary Scholar	Faculty Mentor

Yava Jones Tuskegee University Class of 2003	Dr. David Peterson

Production and Display of Functional Plasmodium TRAP protein In Tetrahymena thermophilia

The malaria parasite Plasmodium uses several proteins to perpetuate its life cycle in both the mosquito and the vertebrate. One such protein, thrombospondin related adhesive protein (TRAP), has been shown to be expressed on the surface of the Plasmodium sporozoite. TRAP is critical for Plasmodium gliding motility and cell invasion. In this study, the TRAP gene was amplified by polymerase chain reaction (PCR), sequenced, and confirmation of its validity was made by a comparison to previously published sequences in GenBank. Tetrahymena thermophilia, a non-pathogenic free-living ciliated protozoan, was selected as the host system for surface display of the TRAP protein. It has many attributes of an ideal expression host, including: 1) short generation time, 2) growth in inexpensive media, 3) high maximal cell density, 4) ease of culturing large volumes, and 5) the availability of strains deficient in the secretion of hydrolytic enzymes. TRAP has an N-terminal signal sequence to direct to the protein to the secretory pathway, and a C-terminal hydrophobic transmembrane domain to anchor it on the cell surface. Once surface expression of TRAP on Tetrahymena has been confirmed, the protein can be studied in depth and its exact behavior and function can be fully understood. This will allow further investigation of TRAP as a potential vaccine candidate for the control of malaria.