The Messens Lab

JORIS MESSENS

Microbiology, Structural Biology, Plant Biology

The mission of the Messens lab is to establish a detailed functional and structural view on the mode of action of the proteins involved in surviving oxidative stress by exploring the electron transfer redox pathways that tightly control sulfur oxygen signaling through reversible switch mechanisms on cysteines and methionines in pathogenic Actinomycetes and plants. Several oxidoreductase proteins, which successively pass on electrons via complex intra- and intermolecular cascades using thiol-disulfide chemistry, are involved. We want to understand how redox-regulated checkpoints are embedded into a variety of metabolic pathways and how cells rapidly switch between distinct catabolic or anabolic processes, protect particularly vulnerable intermediates, and activate survival pathways in response to oxidative stress. Ultimately, we want to translate our knowledge back to the cell or the crop, so that we can cure infectious diseases or design crops that survive extreme conditions.

The coming years we want to exploit our biochemical, structural and quantum chemical expertise in thiol/redox-chemistry through the following projects:

‘New redox pathways to fight pathogenic Actinomycetes’. The major low-molecular-weight thiol of Actinomycetes is ‘mycothiol’. Our main aim is to reveal new redox pathways involved in the oxidative stress defence of mycothiol-producing bacterial pathogens during persistence in human macrophages.

‘Oxidative stress signalling in plants’. One of the warning messages used by living cells under stress is the production of specific 'Reactive Oxygen Species (ROS)’. To understand the complex networks of interactions induced under cellular redox stress, we aim to identify and characterize the proteome of sulfenylated cysteine residues (sulfenome) in Arabidopsis thaliana.

Visit also the Brussels Center for Redox Biology website at http://redox.vub.ac.be.

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Thiol-Disulfide Exchange in Signaling:Disulfide Bonds As a Switch   The mechanism of reversible protein S-mycothiolation in Mycobacteria unraveled 2012, ©Wiley-Blackwell