Associate Professor;
Molecular Microbiology
Bacterial Resistance to Host Antimicrobial Peptides
Duff Medical Building
3775 University St., Room 503
Montreal, QC H3A 2B4
Tel: (514) 398-6235
Fax: (514) 398-7052
herve [dot] le-moual [at] mcgill [dot] ca (Email)
Faculty of Dentistry – Web page
Research Orientations
Research in my laboratory focuses on elucidating the mechanisms that Gram-negative bacterial pathogens evolved to resist host antimicrobial peptides (AMPs). AMPs are natural effectors of the innate immune system. By acting as endogenous antibiotics, they defend the host against microorganisms. Bacterial pathogens have developed various mechanisms to resist killing by AMPs. In Gram-negative bacteria, these resistance mechanisms include the degradation of AMPs by outer-membrane proteases, the export of AMPs by efflux pumps and the remodeling of the lipopolysaccharide layer. My laboratory studies resistance to AMPs in enteric pathogens such as Salmonella enterica, Citrobacter rodentium, enteropathogenic Escherichia coli (EPEC) and enterohemorrhagic E. coli (EHEC). The goal of this research is to validate protein targets for therapeutic intervention.
Selected Recent Publications
Viau, C., Le Sage, V., Ting, D.K., Gross, J. and Le Moual, H. (2011) "Absence of PmrAB-mediated phosphoethanolamine modifications of Citrobacter rodentium lipopolysaccharide affects outer membrane integrity". Journal of Bacteriology; 193(9), pp. 2168-2176. Le Sage, V., Zhu, L., Lepage, C., Portt, A., Viau, C., Daigle, F., Gruenheid, S. and Le Moual, H. (2009) "An outer membrane protease of the omptin family prevents activation of the Citrobacter rodentium PhoPQ two-component system by antimicrobial peptides". Molecular Microbiology; 74(1), pp. 98-111. Faucher, S.P., Viau, C., Gros, P-P., Daigle, F. and Le Moual, H. (2008) "The prpZ gene cluster encoding eukaryotic-type Ser/Thr protein kinases and phosphatases is repressed by oxidative stress and involved in Salmonella enterica serovar Typhi survival in human macrophages". FEMS Microbiology Letters; 281(2), pp. 160-166. Prost, L.R., Daley, M.E., Le Sage, V., Le Moual, H., Klevit, R.E. and Miller, S.I. (2007) "Activation of the bacterial sensor kinase PhoQ by acidic pH". Molecular Cell; 26(2), pp. 165-174. 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), pp. 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(3), pp. 461-472. Sanowar, S., and Le Moual, H. (2005) "Functional reconstitution of the Salmonella typhimurium PhoQ histidine kinase sensor in proteoliposomes". Biochemical Journal; 390(3), pp. 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., Martel, A., 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.