A dominant-negative avirulence effector of the barley powdery mildew fungus provides mechanistic insight into barley MLA immune receptor activation

© The Author(s) 2023. Published by Oxford University Press on behalf of the Society for Experimental Biology.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 74(2023), 18 vom: 29. Sept., Seite 5854-5869
1. Verfasser: Crean, Emma E (VerfasserIn)
Weitere Verfasser: Bilstein-Schloemer, Merle, Maekawa, Takaki, Schulze-Lefert, Paul, Saur, Isabel M L
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2023
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Blumeria graminis AVR MLA Mildew Locus A NLR barley cell death fungal effector mehr... powdery mildew resistance Leucine GMW67QNF9C Carrier Proteins Plant Proteins
Beschreibung
Zusammenfassung:© The Author(s) 2023. Published by Oxford University Press on behalf of the Society for Experimental Biology.
Nucleotide-binding leucine-rich repeat receptors (NLRs) recognize pathogen effectors to mediate plant disease resistance often involving host cell death. Effectors escape NLR recognition through polymorphisms, allowing the pathogen to proliferate on previously resistant host plants. The powdery mildew effector AVRA13-1 is recognized by the barley NLR MLA13 and activates host cell death. We demonstrate here that a virulent form of AVRA13, called AVRA13-V2, escapes MLA13 recognition by substituting a serine for a leucine residue at the C-terminus. Counterintuitively, this substitution in AVRA13-V2 resulted in an enhanced MLA13 association and prevented the detection of AVRA13-1 by MLA13. Therefore, AVRA13-V2 is a dominant-negative form of AVRA13 and has probably contributed to the breakdown of Mla13 resistance. Despite this dominant-negative activity, AVRA13-V2 failed to suppress host cell death mediated by the MLA13 autoactive MHD variant. Neither AVRA13-1 nor AVRA13-V2 interacted with the MLA13 autoactive variant, implying that the binding moiety in MLA13 that mediates association with AVRA13-1 is altered after receptor activation. We also show that mutations in the MLA13 coiled-coil domain, which were thought to impair Ca2+ channel activity and NLR function, instead resulted in MLA13 autoactive cell death. Our results constitute an important step to define intermediate receptor conformations during NLR activation
Beschreibung:Date Completed 02.10.2023
Date Revised 04.10.2023
published: Print
Citation Status MEDLINE
ISSN:1460-2431
DOI:10.1093/jxb/erad285