Abstract
Protein modules, protein networks and cellular functions depend on the association of various components into macromolecular complexes. Recent development in mass-spectrometry-based technologies has provided insights into the composition, structure, function and control of the proteome, shedding light on complex biological processes. For example, structural proteomics techniques enable new opportunities to characterize protein structures and protein assemblies and to determine the topology of protein-protein interaction networks.
This presentation will highlight how the development of new quantitative and structural mass spectrometry techniques can determine the organization and dynamics of host-pathogen protein interaction networks, using the important human pathogen Streptococcus pyogenes as a model system. The formation of host-pathogen protein networks enables bacteria to evade, exploit and modulate the host’s immune system via a wide range of virulence factors. An important challenge in infection medicine is to clarify how these networks are formed, organized and how they dynamically change upon changing microenvironments.
The results demonstrate how increased host-adaptation alters the network topology indicating that the surface associated protein network can be linked to severe and invasive infectious diseases. The quantitative accuracy of the developed workflow supports the generation of comprehensive models outlining the organization and dynamics of host-pathogen protein interaction networks. Follow up experiments based on these models may add new knowledge regarding the relationship between bacterial pathogens and protective or pathological immune responses.
