Prof. Dr.

Joris MESSENS

Group leader Oxidative Stress Signaling
Brussels Center for Redox Biology
VIB Center for Structural Biology
Room E4.16
Pleinlaan 2
B-1050 Brussels
Vrije Universiteit Brussel

redox.vub.ac.be

Phone: 
+32-2-6291992

Joris Messens is since 2012 group leader of the Oxidative Stress Signaling research group within the VIB Center for Structural Biology and professor at the Vrije Universiteit Brussel. After several years in Biotech-industry as an Engineer in Biochemistry, he became an expert in protein purification. He obtained his PhD from the John Moores University of Liverpool (UK, 2003) with structural and functional work on arsenate reductase from Staphyloccocus aureus. In 2006, he created together with Jean-Francois Collet (de Duve Institute, UCL) the Brussels Center for Redox Biology (http://redox.vub.ac.be/) as a platform to stimulate redox and oxidative protein folding research. He is author or co-author of more than 80 peer-reviewed publications (h-index = 28), most of which focus on thiol-disulfide exchange and oxidative stress defense mechanisms. Joris Messens is also frequently askes as invited speaker, session leader, chair and co-chair on international meetings, like GRC, ESF, EMBO, and he is member of the reviewing board for the DFG priority program ‘Dynamics of thiol-based switches in cellular physiology’.

The mission of the Messens lab is to decipher redox-regulated protein-protein interactions in macromolecular complexes, with the ultimate goal to improve oxidative stress resistance in plants and to identify novel therapeutic targets in redox diseases.

How proteins sense oxidation and transduce reactive oxygen stimuli into downstream biological effects is one of the major challenges in redox biology. Knowledge of the mechanisms by which these redox sensors and transducers function is invaluable in understanding how these pathways can be manipulated, thus opening up new possibilities for the discovery of new targets or treatments. We aim to pinpoint crucial protein switches and to understand the mechanistic on-and-off-processes in communication.

The Achilles’ heel of oxidative stress survival of pathogenic Actinomycetes

Persistent human Actinomycete pathogens, like Mycobacterium tuberculosis, are dynamically being reprogrammed to survive H2O2 and HOCl (bleach) stress of our immune system. They engage various enzymatic strategies to fight off ROS and keep their intracellular redox state in homeostasis to prevent damage. A specific redox defense system in these bacteria is mycothiol (MSH), a low molecular weight (LMW) thiol molecule which serves as a glutathione (GSH) surrogate. MSH is critical for the oxidative stress defense of Actinomycetes, and we are unraveling the detailed mode of action of mycothiol electron transfer pathways of oxidative stress defense enzymes.

 
Oxidative stress tolerance in plants

Biotic and abiotic stresses cause significant agricultural yield losses worldwide, and accumulation of reactive oxygen species (ROS) can both cause damage on cellular components, inducing cell death, and act as signal molecules. Knowledge of the redox checkpoints in its signaling network will be invaluable in understanding how these pathways can be manipulated. The objective is to analyze the dynamics in the thiol-proteome under oxidative stress and in function of time by identifying the proteins that are modified by ROS on their cysteines, and to understand the structure/function of sensor proteins in complex with their target proteins.

 

Cancer: a redox disease

In cancer cells, high peroxide levels are dynamically outbalanced by up-regulated anti-oxidant systems, among which peroxiredoxins (Prx) play an important role. Prx are abundant and maintain the peroxide levels low, and Prx can act in redox relay complexes with other proteins. The transcription factor STAT3 is such an interacting protein, and it is aberrantly activated in numerous cancer cells, and promotes tumorigenesis. To bring the cancer cell out of balance, we will target specific regions involved in catalytic conformational change that trap Prx transducers in complex with their partner.

  • Practical course ‘Redox Biology’ in the Interuniversity Programme in Molecular Biology (IPMB): From 2012 till now
  • Practical course on ‘Redox Biochemistry’ within the course “Proteïnechemie & Structuurbepaling”, 1st master year bio-engineering sciences: From 2003 till now.
  • ‘Advanced course of Protein Purification’ - 1st master year of Master of Science in Biomolecular Sciences: 2010-2011 and 2011-2012.
  • General Chemistry and Protein Chemistry - 1st master year Interuniversity Programme in Molecular Biology (IPMB): From 2012-2013 till now.