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User:Joel Weadge
Joel Weadge is an Associate Professor in the Biology Department at Wilfrid Laurier University Dr. Weadge graduated with his B.Sc. from the University of Guelph and then went on to do his Ph.D. in Molecular and Cell Biology at the same institution under Dr. Anthony Clarke while studying peptidoglycan acetylesterases. Dr. Weadge then undertook a research fellowship appointment with Dr. Monica Palcic in the enzymology research group at Carlsberg Laboratory in Copenhagen, Denmark, where he worked on structure-function relationships of glycosyltransferases, including those responsible for blood group determination. He then joined Dr. Lynne Howell’s lab as a postdoctoral fellow at the Hospital for Sick Children in Toronto with CIHR and NSERC fellowships. While at Sick Kids, he continued to work on glycosyltransferases, carbohydrate esterase and acetyltransferases inherent in the alginate biosynthetic complex. Dr. Weadge’s diverse research experiences in the structure-function characterization of glycolic-enzymes and protein export apparati from a variety of carbohydrate systems (peptidoglycan, alginate, blood group antigens) form the basis for his group’s current research interests on cellulose, an exopolysaccharide found in bacterial biofilms.
Carbohydrate Esterases/Acetyltransferases
Peptidoglycan esterases (Ape1a)[1, 2, 3, 4, 5] Alginate acetyltransferase AlgX[1, 2, 3, 4, 5] Alginate acetyltransferase AlgI
Glycosyltransferases
ABO blood group glycosyltransferases Glcyosphingolipid glycosyltransferases
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- Riley LM, Weadge JT, Baker P, Robinson H, Codée JD, Tipton PA, Ohman DE, and Howell PL. (2013). Structural and functional characterization of Pseudomonas aeruginosa AlgX: role of AlgX in alginate acetylation. J Biol Chem. 2013;288(31):22299-314. DOI:10.1074/jbc.M113.484931 |
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- Baker P, Ricer T, Moynihan PJ, Kitova EN, Walvoort MT, Little DJ, Whitney JC, Dawson K, Weadge JT, Robinson H, Ohman DE, Codée JD, Klassen JS, Clarke AJ, and Howell PL. (2014). P. aeruginosa SGNH hydrolase-like proteins AlgJ and AlgX have similar topology but separate and distinct roles in alginate acetylation. PLoS Pathog. 2014;10(8):e1004334. DOI:10.1371/journal.ppat.1004334 |