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Sean T. Prigge, PhD

  • Professor

Departmental Affiliations

Center & Institute Affiliations

Contact Information

615 N. Wolfe Street
Room E5132
Baltimore, Maryland 21205

(410) 955-0105

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PhD, Johns Hopkins School of Medicine, 1997
BA, Amherst College, 1991


Malaria, a disease caused by protozoan parasites, is one of the most dangerous infectious diseases, claiming millions of lives and infecting hundreds of millions of people annually. Malaria parasites contain an essential organelle called the apicoplast that is thought to have arisen through endosymbiosis of an algal cell which had previously incorporated a cyanobacterium. Due to its prokaryotic origin, the apicoplast contains a range of metabolic pathways that differ significantly from those of the human host. We are investigating biochemical pathways found in the apicoplast, particularly those required for the biosynthesis and modification of fatty acids. This metabolism should require several enzyme cofactors such as pantothenate, lipoic acid, biotin and iron-sulfur clusters. We are interested in these cofactors, how they are acquired, how they are used, and whether they are essential for the growth of blood stage malaria parasites. We approach these questions with a combination of cell biology, genetic, biophysical and biochemical techniques.

  • Molecular Microbiology and Immunology, malaria, fatty acid biosynthesis, apicoplast, x-ray crystallography, enzymology

Recent publications

  • T. A. Dellibovi-Ragheb, H. Jhun, C. D. Goodman, M. S. Walters, D. R. T. Ragheb, K. A. Matthews, K. Rajaram, S. Mishra, G. I. McFadden, P. Sinnis and S. T. Prigge, Host biotin is required for liver stage development in malaria parasites. Proc Natl Acad Sci U S A, 115, E2604-E2613 (2018).
  • G. A. Afanador, A. J. Guerra, R. P. Swift, R. E. Rodriguez, D. Bartee, K. A. Matthews, A. Schon, E. Freire, C. L. Freel Meyers and S. T. Prigge, A novel lipoate attachment enzyme is shared by Plasmodium and Chlamydia species. Mol Microbiol, 106, 439-451 (2017).
  • A. J. Guerra, G. A. Afanador and S. T. Prigge, Crystal structure of lipoate-bound lipoate ligase 1, LipL1, from Plasmodium falciparum. Proteins, 85, 1777-1783 (2017).
  • S. G. Tewari, S. T. Prigge, J. Reifman, A. Wallqvist, Using a genome-scale metabolic network model to elucidate the mechanism of chloroquine action in Plasmodium falciparum. Int J Parasitol Drugs Drug Resist, 7, 138-146 (2017).
  • G. A. Afanador, K. A. Matthews, D. Bartee, J. E. Gisselberg, M. S. Walters, C. L. Freel Meyers, and S. T. Prigge, Redox dependent lipoylation of mitochondrial proteins in Plasmodium falciparum. Mol Micro, 94, 156-171 (2014).
  • Characterization of stress responses in malaria parasites to inform a computational model of parasite metabolism.
  • Determinants of apicoplast maintenance in malaria parasites