My main research interest is to explore structural and molecular level mechanism of host-pathogen interactions during an infection, and to determine how pathogens use defined virulence determinants to target central components of the host’s innate and adaptive immune systems.
My research is centred around characterising the host interactomes of isolated virulence determinants and intact bacteria, with the overall aim to gain a deeper understanding of the transition from mild to severe and invasive infections. The main methods I apply include affinity-purification combined with state-of-the-art quantitative mass spectrometry (AP-MS), structural proteomics; namely cross-linking mass spectrometry (XL-MS) and hydrogen-deuterium exchange mass spectrometry (HDX-MS) together with single-particle cryoEM, and hence spans from target discovery to structural determination of protein complexes for the development of treatment strategies aimed towards blocking key interaction interfaces.
Identification and description of host-pathogen protein-protein interaction interfaces as potential sites for therapeutic intervention and drug development will have an important role in combatting pathogen mediated diseases. Knowledge about host-pathogen protein-protein interactions and high-resolution structural data on the formed complexes is often a prerequisite for drug and vaccine development.