Kanelis, Voula

Ph.D. | Associate Professor | Chemistry | Biological and Bioanalytical Chemistry

Contact Information

905 569 4542
905 828 5425
Mailing Address: 
3359 Mississauga Road
Postal Code: 
L5L 1C6
Voula Picture

Research Areas:

Voula Research Picture

Biochemical and biophysical studies of ABC transporters and phage proteins

Research Profile:

Research in the laboratory is focused on two main areas: ABC transporters and phage proteins. We use a combination of NMR spectroscopy and other biophysical tools to obtain information about the structure, interactions, and dynamics of proteins.

ABC transporters are multi-domain, integral membrane proteins found in all species and consist of two repeats each comprised of a membrane spanning domain (MSD) and a cytoplasmic nucleotide binding domain (NBD). ATP binding and hydrolysis at the NBDs results in transport of solutes across biological membranes. ABC proteins are of vast biomedical importance. ABC protein-mediated pumping of cytotoxic molecules from cells confers multidrug resistance to bacterial and tumour cells. Furthermore, many genetic diseases are caused by mutations of specific ABC proteins.  We are studying two different ABC proteins in the lab: (1) Ycf1p, a Cd transporter in yeast; (2) sulfonylurea receptors (SUR), which form regulatory subunits in K+ channels. Studies of Ycf1p are aimed at understanding the basic mechanisms of regulation of ABC transporters. Studies of SUR proteins are aimed at understanding the molecular defects caused by disease-causing mutations in the proteins and how we can correct these defects with drugs.

Our work on phage proteins is focused on an HNH endonuclease a the lambda-like bacteriophage. The HNH protein is critical for the phage replication cycle. We are performing structural studies of the protein to understand the molecular basis for its function in phage morphogenesis. This work will ultimately lead to generation of designer phages that can be used to treat antibiotic resistant bacteria.

Courses Taught:

CHM361, CHM362, JCP463 (undergraduate), CHM1056 (graduate)



De Araujo, E.D., Alvarez, C.P., López-Alonso, J.P., Sooklal, C.R., Stagljar, M, Kanelis, V., De Araujo, E.D., Alvarez, C.P., López-Alonso, J.P., Sooklal, C.R., Stagljar, M, Kanelis, V. Phosphorylation-dependent changes in nucleotide binding, conformation, and dynamics of the first nucleotide binding domain (NBD1) of the sulphonylurea receptor 2B (SUR2B). Journal of Biological Chemistry, jbc.M114.636233 (2015). Journal of Biological Chemistry, jbc.M114.636233 (2015).

De Araujo, E. D. and Kanelis, V. Successful development and use of a thermodynamic stability screen for optimizing the yield of nucleotide binding domains, Protein Expression and Purification, 103: 38-47 (2014).

Kala, S., Cumby, N., Sadowski, P.D., Hyder, B.Z., Kanelis, V., Davidson, A.R., Maxwell, K.L. HNH proteins are a widespread component of phage DNA packaging machines, Proceedings of the National Academy of Sciences, 111(16):6022-7 (2013).

López -Alonso, J.P., De Araujo, E. D. and Kanelis, V. NMR and fluorescence studies of drug binding to the first nucleotide binding domain of SUR2A, Biochemistry, (45):9211-9222 (2012).

Moodley, S., Maxwell, K.L. and Kanelis, V. The protein gp74 from the HK97 bacteriophage functions as an HNH endonuclease. Protein Science, 21(6):809-818 (2012).

De Araujo, E.D., Ikeda, L.K., Tzvetkova, S. and Kanelis, V. The first nucleotide binding domain of the sulfonylurea receptor 2A contains regulatory elements and is folded and functions as an independent module. Biochemistry, 50(31) 6655–6666 (2011).

Kanelis, V., Chong, P.A., and Forman-Kay, J.D. NMR Spectroscopy to study the dynamics and interactions of CFTR.  Methods in Molecular Biology, 741 377-403 (2011).

Pell, L.G., Gasmi-Seabrook, G., Morais, M., Neudecker, P., Kanelis, V., Bona, D., Donaldson, L.W., Howell, P.L., Edwards, A.M., Davidson, A.R. and Maxwell, K.L. The solution structure of the C-terminal Ig-like domain of the bacteriophage tail tube protein. Journal of Molecular Biology, 403(3) 468-79 (2011).

Kanelis, V., Hudson, R.P., Thibodeau, P.H., Thomas, P.J. and Forman-Kay, J.D. NMR evidence for differential phosphorylation-dependent interactions in WT and DF508 CFTR. EMBO Journal, 29(1) 263-77 (2010).