• Professor Emeritus, Global Health
  • Professor Emeritus, Pediatrics - Infectious Diseases
Marilyn Parsons

Center for Infectious Disease Research
307 Westlake Ave N, Suite 500
Seattle, WA 98109
United States

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Among different disease agents, parasites are the most similar to their human hosts. This has made the search for drugs and vaccines highly challenging. Dr. Parsons' laboratory has worked to identify differences between host and parasite that could serve as targets for drug development.

The lab has studied Trypanosoma brucei (African trypanosomes), Leishmania, and Toxoplasma gondii, which cause African sleeping sickness, leishmaniasis, and toxoplasmosis, respectively. The focus of research has been on protein kinases since drugs can successfully be developed against this important class of enzymes. Although Dr. Parsons is now Emeritus, she continues to advise on these projects.
Dr. Parsons has participated in numerous workshops on parasitic diseases for graduate students in India and East Africa. She also taught biology of global diseases for undergraduates. She continues to mentor young scientists in grantwriting.

For more information on Dr. Parson's lab click here.

  • PhD (Stanford University)
  • BA (University of Kansas)
Country Affiliations 
  • French
Health Topics 
  • Education and Training
  • Infectious Diseases (other than STDs)
Pathobiology research areas 
DGH Centers, Programs and Initiatives and Affiliated Organizations 

Molecular and cellular parasitology
Parasite cell and molecular biology, with interest in drug target identification and functional analysis.


Parsons, M., Worthey, E.A., Ward, P.N., and Mottram, J.C. (2005) Comparative analysis of the kinomes of three pathogenic trypanosomatids: Leishmania major, Trypanosoma brucei, and Trypanosoma cruzi. BMC Genomics 6: 127. PMCID: PMC1266030

Worthen, C., Jensen, B.C., and Parsons, M. (2010) Diverse effects on mitochondrial and nuclear functions elicited by drugs and genetic knockdowns in bloodstream stage Trypanosoma brucei, PLoS NTDs, 4:e678. PMCID: PMC2864271.

Kayode K. Ojo, K.K., Larson, E.T., Keyloun, K.R., Castaneda, L.J., DeRocher, A.E., Inampudi, K.K., Kim, J.E., Tracy L. Arakaki, T.L., Murphy, R., Zhang, L., Napuli, A.J., Maly, D.J., Verlinde, C.M., Buckner, F.S., Parsons, M., Hol, W.J.G., Merritt, E.A., and Van Voorhis, W.C. (2010) A unique variation of the ATP binding site makes Toxoplasma gondii calcium-dependent protein kinase 1 a drug target for selective kinase inhibitors. Nat. Struct. Mol. Biol., 17: 602-507. PMCID: PMC2896873.

Jensen, B.C., Ramasamy, G., Vasconcelos, E.J.R., Ingolia, N.T., Myler, P.J., and Parsons, M. (2014) Extensive stage-regulation of translation revealed by ribosome profiling of Trypanosoma brucei. BMC Genomics 15:911. PMCID: PMC4210626.

Jensen, B.C., Booster, N., Vidadala, R.S.R., Maly, D.J., and Parsons, M. (2016) A novel protein kinase is essential in bloodstream Trypanosoma brucei. Int. J. Parasitol., 46: pp. 479-483. NIHMSID: 772127.
A membrane protease is targeted to the relict plastid of toxoplasma via an internal signal sequence. Karnataki A, Derocher AE, Coppens I, Feagin JE, Parsons M.
Traffic. 2007 Nov;8(11):1543-53. Epub 2007 Sep 6.

Conservation of PEX19-binding motifs required for protein targeting to mammalian peroxisomal and trypanosome glycosomal membranes. Saveria T, Halbach A, Erdmann R, Volkmer-Engert R, Landgraf C, Rottensteiner H, Parsons M.
Eukaryot Cell. 2007 Aug;6(8):1439-49. Epub 2007 Jun 22.

Vidadala, R.S.R, Rivas, K.L., Ojo, K.K.,Hulverson, M.A., Zambriski, J.A., Bruzual, I., Schultz, T.L., Huang, W., Zhang, Z., Scheele, S., DeRocher, A.E., Choi,R., Barrett, L.K., Siddaramaiah, L.K., Hol, W.J., Fan, E., Merritt, E.A., Parsons, M., Freiberg, G., Marsh, K., Kempf, D., Carruthers, V.B., Isoherranen, N., Doggett, J.S., Van Voorhis,W.C., and Maly, D.J. (2016). Development of an orally available and central nervous system (CNS)-penetrant Toxoplasma gondii calcium-dependent protein kinase 1 (TgCDPK1) inhibitor with minimal human Ether-à-go-go-Related Gene (hERG) activity for the treatment of Toxoplasmosis. J. Med. Chem. 59: 6531-6546. PMID:27309760. PMCID: PMC5100899

Jensen, B.C., Booster, N., Vidadala, R.S.R., Maly, D.J., and Parsons, M. (2016) A novel protein kinase is essential in bloodstream Trypanosoma brucei. Int. J. Parasitol., 46: 479-493 PMID: 27018127; PMCID:PMC4925258
Surve, S.V., Jensen, B.C., Heestand, M., Mazet, M., Smith, T.K., Bringaud, F., Parsons, M., and Schnaufer, A. (2017) Alternative NADH dehydrogenase of Trypanosoma brucei is important for efficient acetate production in bloodstream forms. Mol. Biochem. Parasitol., 211:57-61. PMID: 27717801; PMCID: PMC5225879

Biddau, M., Bouchut, A., Major, J., Saveria, T., Tottey, J., Oka, O., van-Lith, M., Jennings, K.E., Ovciarikova, J., DeRocher, A., Waller, R.F., Striepen, B., Parsons, M. and Sheiner, L. (2018) Two essential thioredoxins mediate apicoplast biogenesis, protein import, and gene expression in Toxoplasma gondii PLoS Pathogens 14: e1006836. PMID: 29470517; PMCID: PMC5823475

Scheele, S., Geiger, J.A., DeRocher, A.E., Choi, R., Smith, T.R., Hulverson, M.A., Vidadala, R.S.R., Barrett, L.K., Maly, D.J., Merritt, E.A., Ojo, K.K., Van Voorhis, W.C., and Parsons, M. (2018)Toxoplasma calcium-dependent protein kinase 1 inhibitors: probing activity and resistance using cellular thermal shift assays. Anti. Microb. Agents Chemother., 62: e00051-18. PMCID: PMC5971589.