Dr. Allan Rod Merrill

I was raised on a farm in the foothills of the Rocky Mountains in Southern Alberta where I learned how to work and also how to solve problems, and to fix just about anything. I have loved science since my days as a grade school student, when I realized that I would rather be a scientist than a farmer. I obtained my undergraduate degree at the University of Lethbridge in Organic Chemistry and then I pursued graduate work at the University of Ottawa/National Research Council with Professor Arthur G. Szabo, where I developed a keen interest in the application of optical spectroscopy to study protein structure and function. I subsequently tendered an NSERC PDF award to conduct Postdoctoral research work at Purdue University (Indiana) where I furthered my training in Biophysics and I learned protein crystallography and membrane biochemistry. I get my euphoric highs and hence my motivation to continue through the research garden of life from the seemingly small, but important discoveries that are the privilege of scientific researchers. I am addicted to science. I love to talk, walk, and live scientific research. I draw kinetic energy from seeing the “light” turned on within the souls of students, both undergraduate and graduate, who catch a moonbeam of pure knowledge as I share my experience, wisdom and insight with them.

The philosophy of my research program is to use biophysical and biochemical techniques to study the structure and dynamic properties of both membrane and soluble proteins. The systems that we have chosen for study involve bacterial diseases and our approach is to elucidate the molecular mechanisms whereby virulence factors facilitate the disease process.

B.Sc. Lethbridge
Ph.D. Ottawa

My research is in the general area of protein structure and dynamics and is specifically focused on the biochemistry of bacterial toxins involved in disease and consists of the following projects:

• Membrane structure of the colicin E1 ion channel
• Data mining and bioinformatics of bacterial virulence factors
• Optical spectroscopic approaches to study protein structure and dynamics
• Enzyme reaction mechanism of the bacterial mono-ADP-ribosyltransferase family
• Inhibition mechanisms and structural complexes of toxins with inhibitors
• X-ray structures of protein-protein complexes involving toxins

1. Turner, M., Tremblay, O., Heney, K. A., Lugo, M. R., Ebeling, J., Genersch, E., and Merrill, A. R. (2020) Characterization of C3larvinA, a novel RhoA-targeting ADP-ribosyltransferase toxin produced by the honey bee pathogen, Paenibacillus larvae. Biosci Rep 40, BSR20193405.
2. Lugo, M. R., and Merrill, A. R. (2019) An In-Silico Sequence-Structure-Function Analysis of the N-Terminal Lobe in CT Group Bacterial ADP-Ribosyltransferase Toxins. Toxins (Basel) 11, pii:E365.
3. Su, Z., Ho, D., Merrill, A. R., and Lipkowski, J. (2019) In Situ Electrochemical and PM-IRRAS Studies of Colicin E1 Ion Channels in the Floating Bilayer Lipid Membrane. Langmuir 35, 8452-8459.
4. Lugo, M. R., Lyons, B.L., Lento, C., Wilson, D.J., Merrill, A.R. (2018) Dynamics of Scabin toxin. A proposal for the binding mode of the DNA substrate. Plos One 13, e0194425.
5. Lyons, B., Lugo, MR, Carlin, S, Lidster, T, and Merrill, AR. (2018) Characterization of the catalytic signature of Scabin toxin, a DNA-targeting ADP-ribosyltransferase. Biochemical Journal 475, 225-245.
6. Ebeling, J., Funfhaus, A., Knispel, H., Krska, D., Ravulapalli, R., Heney, K. A., Lugo, M. R., Merrill, A. R., and Genersch, E. (2017) Characterization of the toxin Plx2A, a RhoA-targeting ADP-ribosyltransferase produced by Paenibacillus larvae. Environ Microbiol 19, 5100-5116.
7. Lugo, M. R., Ho, D., and Merrill, A. R. (2016) Resolving the 3D spatial orientation of helix I in the closed state of the colicin E1 channel domain by FRET. Insights into the integration mechanism. Arch Biochem Biophys 608, 52-73.
8. Lugo, M. R., Ravulapalli, R., Dutta, D., and Merrill, A. R. (2016) Structural variability of C3larvin toxin. Intrinsic dynamics of the alpha/beta fold of the C3-like group of mono-ADP-ribosyltransferase toxins. J. Biomol. Struct. Dyn 34, 2537-2560.
9. Lyons, B., Ravulapalli, R., Lanoue, J., Lugo, M. R., Dutta, D., Carlin, S., and Merrill, A. R. (2016) Scabin, a Novel DNA-acting ADP-ribosyltransferase from Streptomyces scabies. J. Biol. Chem 291, 11198-11215.

• BIOC*4540 Enzymology
• BIOC*3560 Structure and Function in Biochemistry