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School of Medicine
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The long-term goal of the Caren L. Freel Meyers Laboratory is to develop novel approaches to kill human pathogens, including bacterial pathogens and malaria parasites, with the ultimate objective of developing potential therapeutic agents.
Toward this goal, we are pursuing studies of bacterial isoprenoid biosynthetic enzymes comprising the methylerythritol phosphate (MEP) pathway essential in many human pathogens. Studies focus on understanding mechanism and regulation in the pathway toward the development of selective inhibitors of isoprenoid biosynthesis. Our strategies for creating new anti-infective agents involve interdisciplinary research in the continuum of organic, biological and medicinal chemistry. Molecular biology, protein expression and biochemistry, and synthetic chemistry are key tools for our research.
Photini Sinnis Lab
Research in the Photini Sinnis Lab explores the fundamental biology of the pre-erythrocytic stages of malaria. Our team is focused on the sporozoite stage of Plasmodium, which is the infective stage of the malaria parasite, and the liver stages into which they develop. We use classic biochemistry, mutational analysis, and in vitro and in vivo assays to better understand the molecular interactions between the parasite and its mosquito and mammalian hosts. Our goal is to translate our findings to help develop treatments and a vaccine that target the malaria parasite.
Sean T. Prigge Lab
Current research in the Sean T. Prigge Lab explores the biochemical pathways found in the apicoplast, an essential organelle found in malaria parasites, using a combination of cell biology and genetic, biophysical and biochemical techniques. We are particularly focused on the pathways used for the biosynthesis and modification of fatty acids and associated enzyme cofactors, including pantothenate, lipoic acid, biotin and iron-sulfur clusters. We want to better understand how the cofactors are acquired and used, and whether they are essential for the growth of blood-stage malaria parasites.
Biophysics and Biophysical Chemistry