Disulfide Catalysis and Protein Folding in Bacterial Virulence (2010–2012)
This project investigates a key step in protein folding, the introduction of disulfide bonds between cysteine residues. Many bacteria use an oxidative protein folding machinery to assemble proteins that are essential for cell integrity and to produce virulence factors. However, bacterial oxidative folding mechanisms vary enormously and remain to be properly characterised. Here we will combine molecular biology, biochemistry and structural biology to study the functional properties of novel disulfide catalysts from two major human pathogens (E. coli and Salmonella). The research will provide a detailed picture of oxidative protein folding mechanisms and improve our understanding of the role of redox folding catalysts in bacterial pathogens.