Unknown

Dataset Information

0

Tricking the guard: exploiting plant defense for disease susceptibility.


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.

SUBMITTER: Lorang J 

PROVIDER: S-EPMC4125361 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

Tricking the guard: exploiting plant defense for disease susceptibility.

Lorang J J   Kidarsa T T   Bradford C S CS   Gilbert B B   Curtis M M   Tzeng S-C SC   Maier C S CS   Wolpert T J TJ  

Science (New York, N.Y.) 20121018 6107


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  ...[more]

Similar Datasets

| S-EPMC5853972 | biostudies-literature
| S-EPMC8392720 | biostudies-literature
| S-EPMC11212984 | biostudies-literature
| S-EPMC10122035 | biostudies-literature
| S-EPMC5561662 | biostudies-literature
| S-EPMC1976202 | biostudies-literature
| S-EPMC5742127 | biostudies-literature
| S-EPMC4246327 | biostudies-literature
| S-EPMC9284291 | biostudies-literature
| S-EPMC4515301 | biostudies-literature