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.
Date: 27.10.2014, 14:00
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