Margie Sunde

Margie Sunde completed her undergraduate studies at the University of Cape Town and her PhD in chemical enzymology at the University of Cambridge. Her interest in the structure and formation of amyloid fibrils started with her postdoctoral studies on lysozyme amyloidosis, with Colin Blake in Oxford. She followed this with a research fellowship in Chris Dobson’s group, investigating the mechanism of amyloid formation as a protein misfolding event, before moving back to Cambridge to start her own research group with the support of a Royal Society Fellowship. In 2001 she relocated to Australia and after taking time to focus on family, Margie initiated a program investigating functional amyloid structures, in particular microbial amyloids with diverse biological activities.

Her group has worked extensively on the structure of small fungal proteins called hydrophobins that form amyloid fibrils and coat the surfaces of fungal structures that contact the environment. Hydrophobins spontaneously switch to an amyloid form at hydrophobic:hydrophilic interfaces. Her group is now mostly focused on understanding the role of functional mammalian and viral amyloid fibrils in microbial infection or the evasion of the host response to infection. Mammalian cells utilise functional amyloid complexes to signal for programmed death via necroptosis following inflammatory damage or viral infection. Several herpesviruses express proteins that undermine this response, to maintain viral replication. Margie’s group has demonstrated that amyloid-forming viral proteins interfere with host programmed cell death through the formation of host:virus hybrid amyloid complexes. They aim to develop an understanding of the formation of hybrid or heteromeric amyloids that illuminates normal biology as well as disease processes, and to identify routes for the application of synthetic amyloids for diagnostic or therapeutic purposes.