Structural highlights
Publication Abstract from PubMedEffector proteins are central to the success of plant pathogens, while immunity in host plants is driven by receptor-mediated recognition of these effectors. Understanding the molecular details of effector-receptor interactions is key for the engineering of novel immune receptors. Here, we experimentally determined the crystal structure of the Puccinia graminis f. sp. tritici (Pgt) effector AvrSr27, which was not accurately predicted using AlphaFold2. We characterised the role of the conserved cysteine residues in AvrSr27 using in vitro biochemical assays and examined Sr27-mediated recognition using transient expression in Nicotiana spp. and wheat protoplasts. The AvrSr27 structure contains a novel beta-strand rich modular fold consisting of two structurally similar domains that bind to Zn(2+) ions. The N-terminal domain of AvrSr27 is sufficient for interaction with Sr27 and triggering cell death. We identified two Pgt proteins structurally related to AvrSr27 but with low sequence identity that can also associate with Sr27, albeit more weakly. Though only the full-length proteins, trigger Sr27-dependent cell death in transient expression systems. Collectively, our findings have important implications for utilising protein prediction platforms for effector proteins, and those embarking on bespoke engineering of immunity receptors as solutions to plant disease. AvrSr27 is a zinc-bound effector with a modular structure important for immune recognition.,Outram MA, Chen J, Broderick S, Li Z, Aditya S, Tasneem N, Arndell T, Blundell C, Ericsson DJ, Figueroa M, Sperschneider J, Dodds PN, Williams SJ New Phytol. 2024 Jul;243(1):314-329. doi: 10.1111/nph.19801. Epub 2024 May 10. PMID:38730532[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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