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Notwithstanding the variety of administrative/service responsibilities held, I have maintained an active research program funded by the Natural Sciences and Engineering Research Council of Canada (NSERC), the Canadian Institutes of Health Research (CIHR) and the Canadian National Centres of Excellence (Glycomics Network) that investigates the mechanism of action of enzymes that function on carbohydrates to identify new targets for antibacterial therapy and to functionalize carbohydrate-based nanoparticles. Such studies entail determining the structure and function relationship of the enzymes involved in the biosynthesis and degradation of peptidoglycan, in antibiotic resistance, and in glycogen hydrolysis.

• Listed in the Canadian Who’s Who
• Editor of the Canadian Journal of Microbiology
• Associate editor of Antibiotics and The Cell Wall
• Editorial Board member of the Internation Journal of Biochemistry & Cell Biology
• Member of the College of Reviewers - Canadian Institutes for Health Research
• Member of provincial and national research granting agencies
• President’s Distinguished Professor Award
• 2001 College of Biological Science Teaching Excellence Award

Please contact me about undergraduate and graduate research opportunities in the areas of enzymology and bacterial cell wall physiology.

Clarke Lab Members

*underlining denotes trainees from my lab

• Anderson, A.C., Stangherlin, S., Pimentel, K., Weadge, J.T. & Clarke, A.J. (2022) The SGNH hydrolase family: a template for carbohydrate diversity. Glycobiology 32, 826-848.
• Jones, C.S., Anderson, A.C. and Clarke, A.J. (2021) Mechanism of Staphylococcus aureus peptidoglycan O-acetyltransferase A (OatA) as an O-acyltransferase. Proc. Natl. Acad. Sci. 118 (36) e2103602118
• Jones, C.S., Sychantha, D., Howell, P.L. and Clarke, A.J. (2020) Structural basis for the O-acetyltransferase activity of the extracytoplasmic domain of OatA from Staphylococcus aureus. J. Biol. Chem. 295, 8204-8213.
• Brott A.S., Jones, A.S., and Clarke, A.J. (2019) Development of a high throughput screen for the identification of inhibitors of peptidoglycan O-acetyltransferases, new potential antibacterial targets. Antibiotics 8, 65.
• Sychantha, D., Brott, A.S., Jones, A.S., and Clarke, A.J. (2018) Mechanistic pathways for peptidoglycan O-acetylation and de-O-acetylation. Fronteirs Microbiol. 9, 2332. (Invited review)
• Sychantha, D., Little, D.J., Chapman, R.N. Boons, G.-J., Robinson, H., Howell, P.L. and Clarke, A.J. (2018) PatB1 is an O-acetyltransferase that decorates secondary cell wall polysaccharides. Nature Chemical Biology 14, 79-85.
• Sychantha, D., and Clarke, A.J. (2018) Peptidoglycan modification by the catalytic domain of Streptococcus pneumoniae OatA follows a ping-pong bi-bi mechanism of action. Biochemistry 57(16): 2394-2401.
• Sychantha, D., Jones, C., Little, D.J., Moynihan, P.J., Robinson, H., Galley, N.F., Roper, D.I. Dowson, C.G., Howell, P.L. and Clarke, A.J. (2017) In vitro characterization of the antivirulence target of Gram-positive pathogens, peptidoglycan O-acetyltransferase A (OatA). PloS Pathogens 13(10), e1006667.
• Herlihey, F.A., Osorio-Valeriano, M., Dreyfus, G. and Clarke, A.J. (2016) Modulation of the lytic activity of the dedicated autolysin for flagellum formation Sltf by flagellar rod proteins FlgB and FlgF. J. Bacteriol. 198, 1847–1856.
• Herlihey, F.A., Moynihan, P.J. and Clarke, A.J. (2014) The essential protein for bacterial flagella formation FlgJ functions as a β-N-acetylglucosaminidase. J. Biol. Chem. 289, 31029–31042.
• Moynihan, P.J. and Clarke, A.J. (2014) The mechanism of peptidoglycan O-acetyltransferase involves an Asp-His-Ser catalytic triad. Biochemistry 53, 6243–6251.
• Moynihan, P.J. and Clarke, A.J. (2014) Substrate specificity and kinetic characterization of peptidoglycan O-acetyltransferase B from Neisseria gonorrhoeae. J. Biol. Chem. 289: 16748-16760.