The Rysto immune receptor recognises a broadly conserved feature of potyviral coat proteins

Bibliographische Detailangaben
Veröffentlicht in:	The New phytologist. - 1979. - 235(2022), 3 vom: 01. Aug., Seite 1179-1195
1. Verfasser:	Grech-Baran, Marta (VerfasserIn)
Weitere Verfasser:	Witek, Kamil, Poznański, Jarosław T, Grupa-Urbańska, Anna, Malinowski, Tadeusz, Lichocka, Małgorzata, Jones, Jonathan D G, Hennig, Jacek
Format:	Online-Aufsatz
Sprache:	English
Veröffentlicht:	2022
Zugriff auf das übergeordnete Werk:	The New phytologist
Schlagworte:	Journal Article Research Support, Non-U.S. Gov't Potyvirus resistance engineering Rysto cell death coat protein structure potato virus Y Capsid Proteins

Beschreibung
Zusammenfassung:	© 2022 The Authors New Phytologist © 2022 New Phytologist Foundation. Knowledge of the immune mechanisms responsible for viral recognition is critical for understanding durable disease resistance and successful crop protection. We determined how potato virus Y (PVY) coat protein (CP) is recognised by Rysto , a TNL immune receptor. We applied structural modelling, site-directed mutagenesis, transient overexpression, co-immunoprecipitation, infection assays and physiological cell death marker measurements to investigate the mechanism of Rysto -CP interaction. Rysto associates directly with PVY CP in planta that is conditioned by the presence of a CP central 149 amino acids domain. Each deletion that affects the CP core region impairs the ability of Rysto to trigger defence. Point mutations in the amino acid residues Ser125 , Arg157 , and Asp201 of the conserved RNA-binding pocket of potyviral CP reduce or abolish Rysto binding and Rysto -dependent responses, demonstrating that appropriate folding of the CP core is crucial for Rysto -mediated recognition. Rysto recognises the CPs of at least 10 crop-damaging viruses that share a similar core region. It confers immunity to plum pox virus and turnip mosaic virus in both Solanaceae and Brassicaceae systems, demonstrating potential utility in engineering virus resistance in various crops. Our findings shed new light on how R proteins detect different viruses by sensing conserved structural patterns
Beschreibung:	Date Completed 01.07.2022 Date Revised 08.03.2023 published: Print-Electronic RefSeq: M96425.1, GT015011, NC_008393, AB734777.1, AF395135.1, GU181199.1, HQ185577.1, AF015540.1, NC_002509.2, NC_014791.1, AB576045.1 Citation Status MEDLINE
ISSN:	1469-8137
DOI:	10.1111/nph.18183