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Remy Loris

  • PhD: Vrije Universiteit Brussel, Brussels, Belgium, '94
  • Postdoc: Univ. of Leicester, Leicester, UK, '97-'98
  • Postdoc: CERMAV, Grenoble, France, '97-'99
  • Postdoc: Free Univ. of Brussels, Brussels, Belgium
  • VIB Project Leader since 2000

Bacterial toxin -antitoxin modules

The interests of our group encompass the broad area of structure-function relationships in proteins. Although our expertise lies primarily in macromolecular crystallography, we are furthermore interested in topics that combine crystallography and biophysics.

Although we have been involved in many structural biology projects, the major emphasis of our group is on bacterial TA modules. These are operons encoding a stable toxin and a labile antidote. They play a major role in bacterial stress physiology by temporarily halting cell division when nutrients are scarce. They are proposed to be involved in multidrug resistance. We have characterized in detail the biophysical and biochemical properties of the proteins belonging to the E. coli ccdAB and mazEF TA systems. This led to the elucidation of the first crystal structure of a TA toxin (CcdB), the first structure of a toxin:target complex (CcdB bound to a relevant fragment of gyrase) and the first structure of a TA antidote (MazE). Ongoing research in this field focuses on interactions between toxins and antidotes, on interactions of the antidotes and toxin:antidote complexes with DNA and on the ribonuclease activity of the toxin MazF.

For many years, we have been active as well in the field of structural glycobiology. With the tools of X-ray crystallography and calorimetry, our group investigated structure-function relationships of leguminous lectins. This has led to a detailed picture on how carbohydrate selectivity is achieved within this lectin family. The knowledge gained on plant lectins is currently used in collaborative investigations on a number of bacterial lectins and adhesins.

Prof. Remy Loris