Our research is directed at understanding structure, mechanism of host protein recognition and function of bacterial and viral virulence factors, with an emphasis on Gram-positive bacterial surface proteins. My group specialises in structural biology and protein biochemistry, complemented with biophysical and cell-based techniques. We have a particular interest in TIE (thioester, isopeptide, ester domain) proteins of Gram-positive pathogens including group A streptococci, vancomycin-resistant enterococci, Bacillus anthracis and Clostridium difficile. Our most significant contribution to the field was the discovery of bacteria-encoded, TIE protein-mediated covalent binding as a novel molecular principle in host-microbe interactions. The lab also exploits TIE domains for protein engineering to develop molecular tools for diagnostics, therapy and nanotechnology. Another focus of the group is the structural characterization of GAS M proteins, and the analysis of molecular mechanisms of post-streptococcal rheumatic sequelae. We also investigate structure and functions of single strand RNA virus NSs proteins, key virulence factors of a large class of clinically and economically important pathogens, with a focus on Rift Valley fever phlebovirus.

Protein structure and function; biomolecular NMR; X-ray crystallography; biophysical techniques; host-pathogen interactions; protein engineering

Cryo-EM analysis of bacterial surface appendages, and intranuclear filaments formed by Rift Valley fever phlebovirus NSs protein.

We develop tools for covalent protein tagging, which can replace antibody-based approaches, or can be used for protein-based nanomaterials. We use protein engineering to generate super-stabilised proteins for therapeutic and diagnostic applications.