Our goal is to understand the various facets of host-pathogen interactions at the atomic level and thus provide a rationale for new approaches to specifically interfere with infection processes.
A major focus of our research is dealing with the structural and functional investigation of virulence factors from human pathogenic bacteria, like Listeria monocytogenes, Streptococci, Pseudomonas aeruginosa and Yersinae. In addition we are studying proteins relevant to infections causes by viruses and fungi. Furthermore the structure and activity of functional protein aggregates, like fimbriae and prions is examined using both solution and solid state NMR.
Our research is supported by an on-site state-of-the-art analytical instrumentation platform, providing e.g. mass spectrometry, protein sequencing and various spectroscopic analyses. The Division of Structural Biology also hosts, together with the Max-Delbrück-Centre (MDC) Berlin, the newly established Helmholtz Protein Sample Production Facility (PSPF) providing equipment and expertise in eukaryotic cell culture techniques, protein expression and purification. This facility will allow for the large-scale production of intrinsically "difficult" proteins for structural analysis.
We are trying to address the following basic questions in infection biology:
- Does structural information of proteins relevant to infection provide new
insight into the mechanisms of infection processes?
- Can the deduced structure-function relationships serve as a paradigm for
infection processes employed by other pathogens?
- How do microbial pathogens mimic host cell processes at the molecular/atomic level?
- Do structural homologies uncover or suggest hitherto unrecognized molecular principles or processes?
- Are the microbial proteins under study suitable targets for new therapeutics?
- Is it possible to explain observed phenotypes caused by specific mutations at the atomic level?