Conférence – Dre Joelle Pelletier, jeudi 24 avril à 10h00

PROTEO a le plaisir de vous inviter jeudi 24 avril à 10h00 à la présentation de Joelle Pelletier, Ph.D., professeure à l’Université de Montréal, invitée par Daniela Quaglia, Ph.D., professeure à l’Université du Québec à Montréal. L’événement aura lieu au Pavillon de chimie et biochimie (CB), salle CB-R450, Université du Québec à Montréal.

“Antibiotic resistance: mapping the emergence of a catalytic activity and identifying molecules to inhibit it”

We investigate the prevalence and evolutionary origin of an emerging antibiotic resistance enzyme and track its modern context in multi-drug resistance contexts carried in pathogenic microbes. DfrB enzymes were first identified in the 1970’s for providing resistance to the antimicrobial trimethoprim due to their dihydrofolate reductase activity. Intriguingly, DfrB enzymes have no evolutionary homology to any characterized protein, such that their evolutionary origin is unknown. Their active site is formed upon homotetramerization of an SH3 fold, indicative of an atypical path to evolution of enzyme function. Through kinetic and biophysical characterization as well as inhibitor discovery, we demonstrate that structurally diverse, putative proteins sharing with DfrB only its fold, recreate the DfrB active site environment and provide high trimethoprim resistance. Our results contribute important insights into the evolutionary path that finds the fold of DfrB enzymes included in the modern resistome.

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