Degree Type

Creative Component

Semester of Graduation

Spring 2019

Department

Biomedical Sciences

First Major Professor

Joshua R Beck

Degree(s)

Master of Science (MS)

Major(s)

Biomedical Sciences

Abstract

Malaria has been devastating major civilizations worldwide and is still a major concern for large population of people. It is responsible for more than 215 million cases and 445,000 deaths each year (CDC n.d.). This infectious disease is caused by Plasmodium parasites, which invade and reproduce within human erythrocytes, inducing the clinical symptoms of malaria. These symptoms result from the hundreds of effector proteins the parasite exports into the host erythrocytes cytoplasm. These effector proteins remodel the erythrocyte to become more suitable for the parasite survival. During the erythrocytic stage of malaria, protein export mechanisms are critical and require many signaling sequencing and transport proteins to deliver the effector proteins. The only protein translocon that has been identified thus far is PTEX (Ho, et al. 2018). PTEX is a membrane protein complex over 1.2MDa in size consisting of three core proteins HSP101 ATPase, PTEX150, and EXP2 (Ho, et al. 2018). In order to study the mechanism of translocation that PTEX utilizes, first a fluorescence tag (m-NG) was fused to the SBP-1 into plasmids that contain Dihydrofolate reductase-based destabilizing domain fused to HSP101 which will serve as a conditional knockdown system of PTEX when the small molecule Trimethoprim is removed from growth media. These plasmids were transfected into parasite lines. The mechanism by which PTEX translocate the SBP-1 membrane protein will be determined based on the location at which it is held relative to PTEX after the conditional knockdown system has been activated. Due to the time constraints, no results have been obtained at the time of this report.

Copyright Owner

isaac, Benjamin

File Format

Word

Included in

Diseases Commons

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