Falko Hochgräfe "PTMomics to uncover molecular switches in host-pathogen-interactions"
PTMs - such as phosphorylations at serine, threonine, and tyrosine residues as well as thiol-oxidations at cysteine residues - are critical in the rapid modulation of protein activities and are essential in the transduction of signals in the cells. We hypothesize that protein modifications in host-pathogen-interactions are particularly important for the orchestrated response of host cells in the infectious process.
What is the advantage of mass spectrometry-based techniques in the analyses of posttranslational modifications?
MS-based proteomics allows an unbiased and system-wide view on PTMs that are modulated during the process of an infection. In my talk, I will introduce our strategies for the comprehensive quantitative description of phosphorylation-based signaling networks and thiol-redox modifications. By combining quantitative high-resolution mass spectrometry based proteomics with PTM-enrichment strategies we, e.g., identified the key signaling hubs that determine the cell-specific responses of human bronchial cells to staphylococcal alpha-toxin. We also highlighted protein kinases characteristic for macrophage-like cells and characterized their role in differentiation and function.
What is the benefit of characterizing PTMs in host-pathogen interactions from a clinical perspective?
Antimicrobial resistance is an increasingly serious threat to global public health. The characterization of PTM profiles during host-pathogen-interactions will not only lead to a better understanding of the molecular mechanisms of infections but may also identify critical targets in the host that advance the development of novel pharmaceutical intervention strategies.
Helmholtzzentrum für Infektionsforschung
Building and room
Dr. Falko Hochgräfe,
Competence Center Functional Genomics, Junior Research Group Pathoproteomics, University of Greifswald
- Cellular Proteome Research - Prof. Dr. Lothar Jänsch