(BSc, PhD Victoria)
Leishmania and related trypanosomatids have a specialized organelle called a glycosome that compartmentalizes enzymes essential for a variety of enzymes essential for metabolic processes such as glycolysis, fatty acid b-oxidation, purine salvage, pyrimidine biosynthesis, lipid biosynthesis, and carbon dioxide fixation. These glycosomal proteins are synthesized in the cytosolic and imported across the glycosome membrane by a yet unknown mechanism. My lab uses a multidisciplinary approach that exploits protein chemistry, bioinformatics, molecular biology, immunocytochemistry, and genetic techniques to investigated the molecular processes involved in the targeting and import of proteins into the glycosome. An ultimate goal of this work is to identify potential protein targets that may be used to develop new antiparasitic chemotherapeutic agents.
- Dobie F, Berg A, Boitz JM, Jardim A. (2007)
- Two new cases of de novo small supernumerary marker chromosomes (sSMC) detected at prenatal diagnosis. Prenat Diagn. 2007 Apr;27(4):380-1.
- Madrid KP, Jardim A.(2005)
- Peroxin 5-peroxin 14 association in the protozoan Leishmania donovani involves a novel protein-protein interaction motif. Biochem J.391:105-14.
- Madrid, K. P., De Crescenzo, G., Wang, S., and Jardim, A. (2004)
- Modulation of the Leishmania donovani Peroxin 5 Quaternary Structure by Peroxisomal Targeting Signal 1 Ligands. Molecular and Cellular Biology, 24: 7331–7344
- Zarella-Boitz JM. Rager N. Jardim A. Ullman B. (2004)
- Subcellular localization of adenine and xanthine phosphoribosyltransferases in Leishmania donovani. Molecular & Biochemical Parasitology. 134:43-51
- Roberts SC, Scott J, Gasteier JE, Jiang Y, Brooks B et al. (2002)
- S-adenosylmethionine decarboxylase from Leishmania donovani. Molecular, genetic, and biochemical characterization of null mutants and overproducers. J Biol Chem 277: 5902-5909.
- Furuya T. Kessler P. Jardim A. Schnaufer A. Crudder C. Parsons M. (2002)
- Glucose is toxic to glycosome-deficient trypanosomes. Proceedings of the National Academy of Sciences of the United States of America. 99:14177-82