Calmettes Charles
Biochemistry, Crystallography of proteins
Institut national de la recherche scientifique
Canada
Biography
Dr. Charles Calmettes obtained his B.Sc. in Biochemistry from Paul Sabatier University (Toulouse, France, 2002), then completed his M.Sc. in Biochemistry (2004) and Ph.D. in Nanobiology and Structural Biology (2008) at the Joseph Fourier University (Grenoble, France). He completed his first postdoctoral stay at the Beatson Institute for Cancer Research with Prof. Frank Kozielski (2009, Glasgow, UK) before joining Prof. Trevor Moraes' lab at the University of Toronto (2010-2016) to perform a second postdoctoral training in crystallography of membrane proteins. Dr. Charles Calmettes joined the faculty of the INRS Institut Armand-Frappier in 2016.
Research Interest
The bacterial envelope constitutes a highly functionalized interface separating the cytoplasm from the extracellular medium. In prokaryotes, the envelope presents itself under two distinct architectures determining the group membership of Gram-positive or Gram-negative bacteria. The first are defined by a single lipid membrane while the Gram-negative bacteria have a double lipid membrane that forms the contours of the periplasmic compartment. The proteins constituting the envelope play a predominant role in bacterial physiology, serving many essential functions such as cellular motility, transport of metabolites and macromolecules through membranes, communication with the host and the microbiome, and cell division. In the pathogenic microorganisms, the proteins of the envelope also contribute to the establishment of virulence via their primordial roles in secretion and injection of toxins, recognition and adhesion to host cells, and escape to the immune system.
Publications
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Michalik M, Orwick-Rydmark M, Habeck M, Alva V, Arnold T, Linke D. An evolutionarily conserved glycine-tyrosine motif forms a folding core in outer membrane proteins. PloS one. 2017 Aug 3;12(8):e0182016.
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McCallum M, Tammam S, Little DJ, Robinson H, Koo J, Shah M, Calmettes C, Moraes TF, Burrows LL, Howell PL. PilN binding modulates the structure and binding partners of the Pseudomonas aeruginosa type IVa pilus protein PilM. Journal of Biological Chemistry. 2016 May 20;291(21):11003-15.