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Abstract: The fungal pathogen, Magnaporthe oryzae, causes disease on many economically important cereal crops such as rice, wheat and barley. During infection, the pathogen utilises effectors to enhance virulence and the establishment of infection. Many of these effectors specifically target plant heavy metal-associated (HMA) domain proteins to manipulate the plant host. To counteract pathogen infection, cereal crops have evolved immune receptors that contain integrated HMA domains to bait effector binding and initiate an immune response, with a well-studied example being the Pik-1 receptors within the nucleotide-binding leucine-rich repeat (NLR) class. Recently, integrated HMAs have been identified within the tandem kinase protein (TKP) immune receptor class. However, the mechanism of how TKP receptors recognise effectors and activate upon effector binding remains unknown. Here, we structurally elucidated the interaction between integrated HMA domains from TKPs with their associated effector pair. Utilising this structural knowledge, we engineered the HMA domain to gain binding to effectors in vitro and incorporated them back into TKPs to produce engineered receptors that have an expanded effector recognition profile.

Biography: Daniel completed his undergraduate studies at ANU, where he did his honours project within the Williams group focussing on the structural and functional investigation of a broad-spectrum cell death inducing effector from Fusarium oxysporum. He was awarded the AINSE postgraduate research fellowship and continued within the Williams group for his PhD, maintaining the research focus on structural and functional characterisation of effectors from F. oxysporum, but broadening the scope to utilise structural biology to understand the molecular basis of plant immunity in the F. oxysporum f. sp. lycopersici-tomato pathosystem. Daniel is currently a postdoctoral researcher at the John Innes Centre within the Banfield group, focussing on understanding the structural basis of recognition mediated by cereal tandem kinase protein receptors and utilising that knowledge for immune receptor engineering.