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PhD position
in structure-function studies of redox stress signaling proteins
Position: A PhD Research position is immediately available for
structure-function studies on peroxiredoxins of pathogentic Actinomycetes that
control signaling during oxidative stress. Successful candidates will join an
exciting research environment of the Messens VIB-laboratory in the Structural
Biology Research Center in Brussels. The Messens laboratory is recognized as a
world leader in the redox field, and the lab provides an outstanding position
in protein biochemistry and structure, in a highly dynamic and team-oriented
research group. Successful candidates will work on the FWO-project ‘A Combined
Experimental and Theoretical Approach towards Sulfenylation in the
Peroxiredoxin AhpE of M. tuberculosis:
Unraveling its Redox Chemistry’ in collaboration with the Frank De Proft lab at
the VUB, specialized in quantum chemical calculations, and with the Madia
Trujillo lab at Universidad de la República Uruguay. In this cutting-edge
research environment, you will tackle essential biological problems in oxidative
stress signaling and redox regulation.
Project: Every 20 seconds a person dies from
tuberculosis (TB), which sums up to over 2 million deaths each year. Therefore,
the World Health Organization as well as the European Commission consider fighting
TB as one of the main goals for the coming years. The agent causing TB is Mycobacterium tuberculosis (Mtb). Mtb
infects, resides and multiplies in alveolar macrophages. Mtb causes the
formation of granulomas, where this pathogen is exposed to reactive oxygen
species (ROS) and reactive nitrogen species, which generate a toxic environment
aimed to kill the bacteria. Mtb engages advanced strategies to fight oxidative
stress. One of the key enzymes in the defence mechanism of Mtb is the one-cys
peroxiredoxin AhpE. AhpE scavenges ROS by its active site cysteine. In this
process, the cysteine is oxidized to the sulfenic acid. We will study how the
enzymatic environment influences the cysteine sulfenylation, and the
electron-transfer pathways in which AhpE is involved. We will use a
multidisciplinary approach involving structural and kinetic experiments, and
theoretical calculations to establish the rate determining structural
environment for cysteine sulfenylation. The moment we understand the details of
this ROS-scavenging enzyme, we might start to think about strategies to
interfere with this defense mechanism of Mtb.
Requirements: Applicants should have obtained a Master
degree with a strong background and interest in protein biochemistry,
structural biology and enzymology. Candidates are expected to have strong work
ethics, excellent organization and communication skills, and critical thinking
abilities. We offer a friendly, enthusiastic and interactive environment. Our
staff is international and the working language is English. Please send a cover
letter discussing your interests in the laboratory and the project as well as
your CV and list of 3 individuals as references to [log in to unmask].
Kind regards,