Gustavo Arrizabalaga, Ph.D.

Associate Professor
  • 1999-2004       Post-doctoral fellow, Stanford University School of Medicine, Stanford, CA
  • 1992-1999       Ph.D., Massachusetts Institute of Technology; Cambridge, MA
  • 1988-1992       B.S., Chemistry with Biology concentration, Haverford College, Haverford, PA

Description and summary of research focus of the laboratory

Toxoplasma gondii is one of the most widespread protozoan parasites of warm-blooded animals and causes devastating diseases in immun0compromised humans and during congenital infections.  Central to the survival and pathogenesis of this obligate intracellular parasite is its ability to move from cell to cell and to quickly adapt to different environments as it propagates throughaou the infected organism.  One of the goals of my research program is to elucidate the mechanisms by which the parasite exits its host cell and becomes motile as to invade new ones. In addition, we are investigating how the parasite responds to drug treatments as to uncover new ways to treat this important human pathogen.


  • Lavine, M.D., Knoll, L.J., Rooney, P.J. and Arrizabalaga, G. 2007. A Toxoplasma gondii mutant defective in responding to calcium fluxes shows reduced in vivo pathogenicity. Molecular and Biochemical Parasitology,155(2): 113-122. PMCID: PMC2034501
  • Lavine, M and Arrizabalaga, G., 2008 Exit from host cells by the pathogenic parasite Toxoplasma gondii does not require motility. Eukaryotic Cell, 7(1): 131-140. PMCID: PMC2224157
  • Lavine, M.D. and Arrizabalaga, G., 2009. Induction of mitotic S-phase of host and neighboring cells by Toxoplasma gondii enhances parasite invasion. Molecular and Biochemical Parasitology, 164(1):95-9. PMID: PMC2654716
  • Garrison, E. and Arrizabalaga, G., 2009. Disruption of a mitochondrial homolog of a MutS DNA Repair Enzyme confers drug resistance in the pathogenic parasite Toxoplasma gondii. Molecular Microbiology, 72(2):425-41. PMCID: PMC2712120
  • Lavine, M.D. and Arrizabalaga, G. 2011. The antibiotic monensin causes cell cycle disruption of Toxoplasma gondii, mediated through the DNA repair enzyme TgMSH-1. Antimicrob Agents Chemother, 55(2): 745-55. PMCID: PMC3028789
  • Francia, M.E., Wicher S., Pace D.A., Sullivan, J., Moreno, S.N.J., and Arrizabalaga, G. 2011. A Toxoplasma protein with homology to intracellular type Sodium Hydrogen Exchangers is required for osmotolerance and protein processing. Experimental Cell Research. 317(10):1384-96. PMCID: PMC3096714
  • Lavine, M.D. and Arrizabalaga, G. 2012, Analysis of Monensin Sensitivity in Toxoplasma gondii reveals autophagy as a mechanism for drug induced death. Plos One, 7(7):e42107. PMID: PMC3405052
  • Garrison, E., Treeck, M., Ehret, M., Garbuz, T., Oswald, B.P., Settles, M., Boothroyd, J., Arrizabalaga, G. 2012, A forward genetic screen reveals calcium-dependent kinase 3 is critical for calcium-induced egress in Toxoplasma. Plos Pathogen, 8(11). PMCID: PMC3510250
  • Gaji, R., Checkley, L., Reese, M., Ferdig, M.T., and Arrizabalaga, G. 2014 Expression of the essential kinase PfCDPK1 from Plasmodium falciparum in Toxoplasma gondii facilitates the discovery of novel antimalarial drugs. Antimicrob Agents Chemother, 58(5):2598-607. PMCID: PMC3993251
  • Treeck, M., Sanders, J., Gaji, R., LaFavers, K., Child, M., Arrizabalaga, G., Elias, J., Boothroyd, J., 2014 A novel role of Calcium-dependent Kinase 3 in regulating metabolism in Toxoplasma gondii in addition to ionophore induced egress. Plos Pathogen, 10(6):e1004197. PMCID: PMC4063958

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