Protein-glycan macromolecular complexes
We study the characteristics and effects of protein-glycan interactions in the extracellular matrix
Background
Glycan structures on the surfaces of pathogens can be recognised and detected by immune cells via their surface lectin receptors, but some pathogens can exploit this interaction for immune evasion.
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WORLDWIDE
What are we doing?
Please hover over the schematic below to visualise internalisation of pathogens by immune cells after recognition through lectin-glycan interactions
The Richter labs is focusing on the interaction of the pathogen recognition receptor with the pathogens glycans in surface-based assays. Two model systems were designed, one with Glycan surfaces and the other with lectin surfaces. The schematic below demonstrates the simplified concept. The glycan model tests the hypothesis that the different glycan densities on different pathogens could affect binding and therefore recognition. The lectin model allows investigation of how different glycan nanoparticles can affect the clustering of lectins. Understanding the underlying biophysical mechanisms of pathogen recognition receptor binding is important for the development of effective multivalent inhibitors against viral infection and to provide guidance for regulating immune responses.
Tools used within our protein- glycan research:
For more information about what these techniques are and how they are used, please click on the icons.
To characterise the biomolecular interactions involved in ​glycan-lectin interactions
Used in each technique to model biological surfaces
To characterise the biomolecular interactions involved in ​glycan-lectin interactions