Antibiotic resistance has been observed with trimethoprim, a synthetic antibiotic used clinically to inhibit the chromosomal dihydrofolate reductase enzyme (cDfr) found in bacteria. Resistance to trimethoprim has been associated with type A and type B dihydrofolate reductases (DfrAs and DfrBs). Where DfrAs are mutants of cDfr, DfrBs are not related to cDfr, genetically and structurally. Using metagenomic data, five non-characterized proteins have been identified as distant homologs to DfrBs (DfrBHs), were they all have a predicted structural homology with the DfrBs. The goal of the project is to characterize the DfrBHs; can they confer resistance to trimethoprim? Do they have dihydrofolate reductase activity? Finally, to verify the possible homology between the DfrBHs and the DfrBs, inhibition of the DfrBHs with DfrBs inhibitors will indicate a structural homology.

•    B. Sc. 2020 (Biochemistry and molecular medicine), Université de Montréal

•    09/2020 – Present: Graduate student, Joelle Pelletier Laboratory , Department of biochemistry,                               Université de Montréal

•    05/2020 – 08/2020: Research intern on COVID-19 antibody detection assay project - Joelle Pelletier                               Laboratory

•    2020-2022 – APRENTICE Scholarship Trainee Program - uOttawa (NSERC)

•    Summer 2019 – Center in Green Chemistry and Catalysis Scholarship (CGCC), Université de Montréal

•    Deweid, L.*, H.-Parisien, A.*, Lafontaine, K., Rochet, L.N.C., Kolmar, H. and Pelletier, J.N. (2020) Glutamine-walking: creating reactive substrates for transglutaminase-mediated protein labelling. Met. Enzymol., 644:121-148. (*equal contribution)