Armando Jardim

Armando Jardim

Associate Professor

 

T: 514-398-7727  |  armando [dot] jardim [at] mcgill [dot] ca (Email)  | Parasitology Building P-105

Degrees

BSc, PhD (Victoria)

Short Bio

Armando Jardim is an Associate Professor of Biochemistry at Institute of Parasitology and an Associate Member of the Department of Microbiology and Immunology at McGill University. He has more than 25 years of experience in the field of protein/peptide biochemistry, chromatographic separation techniques and molecular biology. His research program focuses on structural and functional dissection the molecular machinery required for the biogenesis of the glycosome, a subcellular organelle that is critical for the viability of the medically important protozoan parasite Leishmania. This work has led to the identification of novel proteins that are being exploited as potential drug targets. His team, in collaboration with colleagues, is investigating a spectrum of proteins and small molecule metabolites secreted by the helminth parasite Trichuris suis with the aim to identifying immunomodulatory molecules for the treatment of autoimmune disorders such as inflammatory bowel disease.  He has authored 64 publications in leading edge journals and filed a number of patents which have stemmed from his research efforts. Dr. Jardim has served as the Director of the Centre for Host-Parasite Interactions, an expert reviewer for national and international funding agencies, and as an Associate Editor for the journals PLOS Neglected and Tropical Diseases and Molecular and Biochemical Parasitology.

Research Interests

The Jardim laboratory is investigating the medically important infectious organisms Leishmania and E. coli which cause leishmaniasis and gastrointestinal diseases, respectively. 

Current Research

  1. Leishmania parasites have a specialized organelle called a glycosome 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. Target of these proteins is vital for parasite viability. My lab uses a multidisciplinary approach to investigate 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.
  2. Helminths (parasitic worms), are known to down modulate the mammalian host immune response which to promote worm survival. Recent studies have demonstrated that infection with these parasite can lead to an improvement in the clinical pathologies associated with autoimmune disease such as inflammatory bowel disease, multiple sclerosis, asthma. These affects are likely mediated through the secreted-excreted factors (ESF) release by the worms. The objective of this research is to identify and characterize the proteins or metabolites in the ESF that down modulate the pro-inflammatory immune response which are implicated in the promotion of autoimmune disorder.
  3. Enteropathogenic and enterohemorrhagic E. coli are a major cause of food and water borne infections. These bacteria E. coli express a molecular machine known as the type III secretion system that permits the direct injection of virulence factors into the cytosolic compartment of the host gut epithelial cells. The process is dependent on the formation of a pore structure on the host plasma membrane. Work in our laboratory is exploiting model membrane to understand the mechanism associated with protein-membrane interaction and the subsequent assembly of  pore structure containing the bacterial proteins EspB and EspD.

Courses

LSCI 211 Biochemistry 1 3 Credits
    Offered in the:
  • Fall
  • Winter
  • Summer


BTEC 619 Biotechnology Laboratory 2 4 Credits
    Offered in the:
  • Fall
  • Winter
  • Summer

Publications

View a list of current publications.

Publications

Selected Publications

van Bergen B, Cyr N, Strasser R, Blanchette M, Sheppard JD, Jardim A. (2016) α,β-Dicarbonyl reduction is mediated by the Saccharomyces Old Yellow Enzyme. FEMS Yeast Res. (in press)

Smith S, Boitz J, Chidambaram ES, Chatterjee A, Ait-Tihyaty M, Ullman B, Jardim A. (2015) The cystathionine-β-synthase domains on the guanosine 5''-monophosphate reductase and inosine 5'-monophosphate dehydrogenase enzymes from Leishmania regulate enzymatic activity in response to guanylate and adenylate nucleotide levels. Mol Microbiol. 100:824-40

 Chatterjee A, Caballero-Franco C, Bakker D, Totten S, Jardim A. (2015) Pore-forming Activity of the Escherichia coli Type III Secretion System Protein EspD.. J Biol Chem. 290:25579-94

Valanparambil RM, Segura M, Tam M, Jardim A, Geary TG and Stevenson MM (2014) Production and analysis of immunomodulatory excretory-secretory products from the mouse gastrointestinal nematode Heligmosomoides polygyrus bakeri. Nat Protoc 9: 2740-54.