Clinical Associate Professor, Microbial Infection and Immunity
Director of Graduate and Post-Graduate Education, Microbial Infection and Immunity

730 Biomedical Research Tower (BRT)
460 W 12th Ave, Columbus OH 43210

Research Interests

Dr. Drew's research focuses on the study of Plasmodium falciparum, the protozoan parasite that causes the most pathogenic form of human malaria. His efforts for discovery and development of novel therapeutics to treat infections with P. falciparum are divided into two strategies:

In an aim to identify novel structures and/or scaffolds for potential development of therapeutic leads, the Drew lab is screening chemical compounds for their ability to kill malaria parasites. Toxicity screens are being performed on in vitro cell cultures of P. falciparum in 96 or 384-well plate formats using a new FACSCantoII flow cytometer housed in the lab. Promising compounds are prioritized based on a scoring matrix using criteria such as potency, death-phenotype, and selectivity. Compounds are further characterized through structure-activity analysis and target identification. This work is done in close collaboration with members of the Division of Medicinal Chemistry and Pharmacognosy in the OSU College of Pharmacy.

In a target-based approach, the Drew lab is also evaluating a number of parasite-expressed proteases as viable drug targets. Studies involve the characterization of these enzymes through biochemical, genetic, and cell biological methods. In this effort, the lab has completed a screen of a library of mechanism-based cysteine protease inhibitors against P. falciparum. Through these studies the lab has identified compounds that kill parasites at low micromolar concentrations. This approach has allowed for the elucidation of the mechanism of activation of the aspartic protease plasmepsins and has uncovered a protease homologous to the yeast autophagy protein, ATG4, which appears to be involved in regulating nutrient acquisition via autophagy in this parasite. Current efforts are underway to assess the essentiality and cellular function of this putative protease.

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