TY - JOUR T1 - The Ry<sub>sto</sub> immune receptor recognizes a broadly conserved feature of potyviral coat proteins JF - bioRxiv DO - 10.1101/2021.05.20.444601 SP - 2021.05.20.444601 AU - Marta Grech-Baran AU - Kamil Witek AU - Jarosław Poznański AU - Anna Grupa-Urbańska AU - Tadeusz Malinowski AU - Małgorzata Lichocka AU - Jonathan DG Jones AU - Jacek Hennig Y1 - 2021/01/01 UR - http://biorxiv.org/content/early/2021/05/21/2021.05.20.444601.abstract N2 - Potyviruses are the largest group of plant RNA viruses, causing significant losses in many crops. Among them, potato virus Y (PVY) is particularly important, and enhances the severity of infections by other viruses. The Rysto gene confers PVY resistance and encodes a TIR-NLR intracellular immune receptors that recognizes PVY coat protein (CP). To define a minimal CP fragment sensed by Rysto, we created a series of truncated CP variants and expressed these CP derivatives in Rysto transgenic plants. Deletions that affect the 149 amino acid CP core region lose the ability to trigger Rysto-dependent defence activation. Furthermore, point mutations in the amino acid residues Ser126, Arg157, and Asp201 of the highly conserved RNA-binding pocket of potyviral CP, reduce or abolish Rysto-dependent responses, demonstrating that appropriate folding of the CP core is required for Rysto-mediated recognition. Consistent with these data, we found Rysto recognises CPs of various viruses that share a similar core region, but not those lacking it. Finally, we demonstrated that Rysto provides immunity to plum pox virus and turnip mosaic virus, demonstrating its wide range of applications in disease-resistant crop engineering. In parallel, we showed that CP triggered Rysto activation is SAG101- but not PAD4- or SA-level dependent. Our findings shed new light on how R proteins can detect viruses by sensing highly conserved structural patterns.Competing Interest StatementThe authors have declared no competing interest. ER -