Michael Klemba

Associate Professor


Ph.D., Molecular Biophysics and Biochemistry, Yale University, 1996

B.S., Biology and Chemistry, University of Waterloo, 1990


  • 2011 – present: Associate Professor, Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg
  • 2005 – 2011: Assistant Professor, Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg

Courses Taught

  • BCHM 3114 - Biochemistry for Biotechnology and Life Sciences
  • BCHM 5304 - Enzymology
  • BCHM 5224 - Protein Structure and Function

Other Teaching and Advising

  • Undergraduate advising
  • Mentor for undergraduate research (e.g., BCHM 4994)
  • Mentor for doctoral students in the Biochemistry graduate program

Program Focus

Malaria is one of the most devastating infectious diseases in the world today. The objective of my research is to understand how the human malaria parasite Plasmodium falciparum thrives in its host red blood cell. We employ biochemical and cell biological approaches to study:

  • endocytosis and catabolism of erythrocyte hemoglobin by the parasite
  • lipid catabolism and utilization of host lipid species for fatty acid scavenging
  • protein sorting and trafficking to the parasite’s vacuole and specialized apical secretory organelles
  • mechanisms of action of anti-malarial compounds

Current Projects

Discovery of anti-malarial compounds that target the cytostomal endocytic pathway”- funded by the Bill and Melinda Gates Foundation. The objective of this project is to screen 400 validated anti-malarial compounds (the “Malaria Box”) to identify novel inhibitors of host hemoglobin uptake through the ctyostomal endocytic pathway.

“Roles of Two Aminopeptidases in Peptide Catabolism in the Malaria Parasite”- funded by the National Institutes of Health. The goals of this project are to define the biochemical and structural properties of two vacuolar aminopeptidases that participate in hemoglobin catabolism in the human malaria parasite Plasmodium falciparum.

  • Denloye, T., S. Dalal, and M. Klemba. 2012. Characterization of a glycerophosphodiesterase with an unusual tripartite distribution and an important role in the asexual blood stages of Plasmodium falciparum. Mol. Biochem. Parasitol. 186:29-37. Publication Link (PDF)
  • Dalal, S., D.R. Ragheb, and M. Klemba. 2012. Engagement of the S1, S1’ and S2’ subsites drives efficient catalysis of peptide bond hydrolysis by the M1-family aminopeptidase from Plasmodium falciparum. Mol. Biochem. Parasitol. 183:70-7. Publication Link (PDF)
  • Ragheb, D., S. Dalal, K.M. Bompiani, W.K. Ray, and M. Klemba. 2011. Distribution and biochemical properties of an M1-family aminopeptidase in Plasmodium falciparum indicate a role in vacuolar hemoglobin catabolism. J. Biol. Chem. 286:27255-65. Publication Link (PDF)
  • Harbut, M.B., G. Velmourougane, S. Dalal, G. Reiss, J.C. Whisstock, O. Onder, D. Brisson, S. McGowan, M. Klemba, and D.C. Greenbaum. 2011. Bestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidases. Proc. Natl. Acad. Sci. USA 108:E526-34. Publication Link (PDF)
  • Velmourougane, G., M. Harbut, S. Dalal, S. McGowan, C.A. Oellig, J.C. Whisstock, M. Klemba, and D.C. Greenbaum. 2011. Synthesis of new (-)-Bestatin-based inhibitor libraries reveals a novel binding mode in the S1 pocket of the essential malaria M1 metalloaminopeptidase. J. Med. Chem. 54:1655-66. Publication Link (PDF)
  • Wang, F., P. Krai, E. Deu, B. Bibb, C. Lauritzen, J. Pedersen, M. Bogyo and M. Klemba. 2011. Biochemical characterization of Plasmodium falciparum dipeptidyl aminopeptidase I. Mol. Biochem. Parasitol. 175:10-20. Publication Link (PDF)
  • Ragheb, D., K. Bompiani, S. Dalal, and M. Klemba. 2009. Evidence for catalytic roles for Plasmodium falciparum aminopeptidase P in the food vacuole and cytosol. J. Biol. Chem. 284:24806-15. Publication Link (PDF)
  • Dalal, S. and M. Klemba. 2007. Roles for two aminopeptidases in vacuolar hemoglobin catabolism in Plasmodium falciparum. J. Biol. Chem. 282:35978-87. Publication Link (PDF)
Michael Klemba