Abstract
Typically, pathogens deploy virulence effectors to disable defense. Plants defeat effectors with resistance proteins that guard effector targets. We found that a pathogen exploits a resistance protein by activating it to confer susceptibility in Arabidopsis. The guard mechanism of plant defense is recapitulated by interactions among victorin (an effector produced by the necrotrophic fungus Cochliobolus victoriae), TRX-h5 (a defense-associated thioredoxin), and LOV1 (an Arabidopsis susceptibility protein). In LOV1's absence, victorin inhibits TRX-h5, resulting in compromised defense but not disease by C. victoriae. In LOV1's presence, victorin binding to TRX-h5 activates LOV1 and elicits a resistance-like response that confers disease susceptibility. We propose that victorin is, or mimics, a conventional pathogen virulence effector that was defeated by LOV1 and confers virulence to C. victoriae solely because it incites defense.
MeSH Terms
Arabidopsis/immunology,metabolism,microbiology
Arabidopsis Proteins/chemistry,genetics,metabolism
Ascomycota/metabolism,pathogenicity
DNA-Binding Proteins/chemistry,genetics,metabolism
Disease Susceptibility
Fungal Proteins/metabolism
Mutation
Mycotoxins/metabolism
Oxidation-Reduction
Plant Diseases/immunology,microbiology
Plant Immunity
Protein Binding
Protein Interaction Domains and Motifs
Thioredoxins/genetics,metabolism
Tobacco/genetics,metabolism
Virulence Factors/metabolism
Chemicals
Arabidopsis Proteins
DNA-Binding Proteins
Fungal Proteins
LOV1 protein, Arabidopsis
Mycotoxins
NPR1 protein, Arabidopsis
Virulence Factors
Victorin protein, Cochliobolus victoriae
Thioredoxins
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Lorang J
Department of Botany and Plant Pathology and Center for Genome Research and Biocomputing, Oregon State University, Corvallis, OR 97331, USA.
Kidarsa T
Bradford C S
Gilbert B
Curtis M
Tzeng S-C
Maier C S
Wolpert T J
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