Degree Type
Creative Component
Semester of Graduation
Spring 2019
Department
Biomedical Sciences
First Major Professor
Joshua Beck
Degree(s)
Master of Science (MS)
Major(s)
Biomedical Sciences
Abstract
PTEX is the Plasmodium translocon of exported proteins of the malaria parasite (Plasmodium sp.) and functions to export proteins out of the parasite vacuolar membrane, remodeling the host erythrocyte. Remodeling enables the parasite to access vital nutrients and avoid immune defense of the host, enabling parasite survival and leading to malaria disease. A key protein interaction in PTEX involves 12 residues of component EXP2, which form an augmented β-sheet with component HSP101. Theoretically, interrupting this essential interaction by introducing a peptide corresponding to these 12 residues of EXP2 to compete with endogenous EXP2 would fatally damage the protein transport mechanism. If utilized therapeutically, this peptide could inhibit function of PTEX, thereby protecting host erythrocyte from parasitic use of nutrients and proteins, ultimately leading to parasite death.
Copyright Owner
Elena Bartemes
Copyright Year
2019
File Format
application/pdf
Recommended Citation
Bartemes, (Maria) Elena Y., "Can key protein interactions be disrupted in PTEX to inhibit its function?" (2019). Creative Components. 134.
https://lib.dr.iastate.edu/creativecomponents/134
