Functional amyloid fibrils: operating for and against microbial infection and detection

Fri 17 May 2019 12:00pm


Level 2

There is a growing recognition that the stable, cross-beta amyloid protein architecture forms the structural basis for many oligomeric protein assemblies. While the amyloid structure can be a pathological fold when associated with protein misfolding, a number of functional amyloid fibrils have now been described in which the biologically active form of the protein is retained or generated in the fibrillar form. Functional amyloid fibrils play diverse roles in the interactions between fungi, viruses and bacteria and infected host organisms.

My groups focuses on understanding the structure of fungal and viral amyloids and revealing the nature of the interface between microbial functional amyloids and plant and animal hosts. I will present biophysical and structural studies of fungal amyloid structures that are used as protective shields against host recognition of infection and viral amyloids that form "decoy" fibrils to prevent host cell death by necroptosis.

Host: Professor Glenn King