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Hervé LeMoual

herve [dot] le-moual [at] mcgill [dot] ca (Email)
Tel:(514) 398-6235

Dr. Herve LemoualMy research interests are in molecular microbiology. We are currently working on two-component regulatory systems, which are prevalent signaling pathways in bacteria.They allow bacterial cells to sense and respond to environmental stimuli by modulating the transcription of specific genes. They consist of a histidine protein kinase (first component, which is usually a transmembrane protein), and a cytoplasmic response regulator (second component). Recognition of the external signal triggers an intracellular phosphorylation cascade that, in turn, elicits a specific output response. Using tools of both molecular biology and biochemistry, we study the molecular mechanisms by which the receptor transduces extracellular signals across the membrane and elicits appropriate cellular responses. Better understanding the structural basis for information transfer across the membrane will lead to the development of small molecules able to interfere with receptor signaling and, in turn, act as antimicrobial agents.

Ongoing Projects

Signal transduction by the PhoP/PhoQ two-component system of Salmonella typhimurium

Signal transduction by the Ser/Thr kinases and phosphatases of Salmonella typhi.

Regulation of virulence gene expression in Actinobacillus actinomycetemcomitans.

SELECTED PUBLICATIONS

Perron-Savard, P., De Crescenzo G., and Le Moual, H. (2005) Dimerization and DNA binding of the Salmonella enterica PhoP response regulator are phosphorylation independent. Microbiology, 151(12), 3979-3987.

Bader, M. W., Sanowar, S., Delay, M., Cho, U., Schneider, A., Klevit, R., Xu, W., Le Moual, H., and Miller, S.I. (2005) Recognition of antimicrobial peptides by a bacterial sensor kinase. Cell 122, 461-472.

Sanowar, S., and Le Moual, H. (2005) Functional reconstitution of the Salmonella typhimurium PhoQ histidine kinase sensor in proteoliposomes. Biochem. J., 390, 769-776.

Lai, S. M., and Le Moual, H. (2005) PrpZ, a Salmonella enterica serovar Typhi serine/threonine protein phosphatase 2C with dual substrate specificity. Microbiology, 151(4), pp. 1159-1167.

Sanowar, S., and Le Moual, H. (2003) Mutational analysis of the residue at position 48 in the Salmonella enterica serovar Typhimurium PhoQ sensor kinase. Journal of Bacteriology, 185(6), pp. 1935-1941.

Montagne, M., Martel, A., and Le Moual, H. (2001) Characterization of the catalytic activities of the PhoQ histidine protein kinase of Salmonella enterica serovar Typhimurium. Journal of Bacteriology, 183(5), pp. 1787-1791.

Le Moual, H., Quang, T., and Koshland D. E. Jr. (1998) Conformational changes in the cytoplasmic domain of the Escherichia coli aspartate receptor upon adaptive methylation. Biochemistry, 37(42), pp.14852-14859.

Le Moual, H., Quang, T., and Koshland D. E. Jr. (1997) Methylation of the Escherichia coli chemotaxis receptors: Intra and interdimer mechanisms. Biochemistry, 36(43), pp. 13441-13448.

Le Moual, H., and Koshland D. E. Jr. (1996) Molecular evolution of the C-terminal cytoplasmic domain of a superfamily of bacterial receptors involved in taxis. Journal of Molecular Biology, 261(4), pp. 568-585.