The mission of the Oxidative Stress Signaling 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.
Protein Methionine Sulfoxide Dynamics in Arabidopsis thaliana under Oxidative StressJacques S, Ghesquière B, De Bock P, Demol H, Wahni K, Willems P, Messens J, Van Breusegem F, Gevaert KMOLECULAR & CELLULAR PROTEOMICS, 14, 1217-29, 2015 DYn-2 Based Identification of Arabidopsis SulfenomesAkter S, Huang J, Bodra N, De Smet B, Wahni K, Rombaut D, Pauwels J, Gevaert K, Carroll K, Van Breusegem F, Messens JMOLECULAR & CELLULAR PROTEOMICS, 14, 1183-200, 2015 The Corynebacterium glutamicum mycothiol peroxidase is a reactive oxygen species-scavenging enzyme that shows promiscuity in thiol redox controlPedre B, Van Molle I, Villadangos A, Wahni K, Vertommen D, Turell L, Erdogan H, Mateos L, Messens JMOLECULAR MICROBIOLOGY, 96, 1176-91, 2015 Sulfenome mining in Arabidopsis thalianaWaszczak C, Akter S, Eeckhout D, Persiau G, Wahni K, Bodra N, Van Molle I, De Smet B, Vertommen D, Gevaert K, De Jaeger G, Van Montagu M, Messens J, Van Breusegem FPROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 111, 11545-50, 2014 Protein S-Mycothiolation Functions as Redox-Switch and Thiol Protection Mechanism in Corynebacterium glutamicum Under Hypochlorite StressChi B, Busche T, Van Laer K, Bäsell K, Becher D, Clermont L, Seibold G, Persicke M, Kalinowski J, Messens J, Antelmann HANTIOXIDANTS & REDOX SIGNALING, 20, 589-605, 2014
14/11/2012 - Flemish biologists lead by Joris Messens have discovered that Mycobacterium tuberculosis – the bacterium that causes tuberculosis – has an ingenious defence mechanism against oxygen.
19/11/2009 - Bacteria possess an ingenious mechanism for preventing oxygen from harming the building blocks of the cell. This is the new finding of a team of biologists.
PhD: John Moores University of Liverpool, UK, 2003
VIB Group Leader: since 2012