An apoplastic fungal effector disrupts N-glycosylation of ZmLecRK1 for degradation to suppress disease resistance in maize

Pathogens deploy effectors to suppress host immune responses and enable successful colonization in plants.While apoplastic effectors play major roles in pathogenicity, whether and how they directly attack extracellular immune receptors remains unclear.Here, we identify an apoplastic effector FgLPMO9A from the fungal pathogen Fusarium graminearum that directly inhibits maize immune receptor ZmLecRK1-mediated resistance.FgLPMO9A belongs to the polysaccharide monooxygenase family, which depolymerizes polysaccharides.Deletion of FgLPMO9A attenuates F. graminearum virulence on maize, but this defect is fully rescued in the zmlecrk1 mutants.FgLPMO9A interacts with the extracellular S-domain of ZmLecRK1 and disrupts N-glycosylation at the N341 site, thereby promoting ZmLecRK1 degradation via the NBR1 (Neighbor of BRCA1 Gene1)-mediated autophagy pathway.Notably, the ZmLecRK1 variant with the N341Q substitution confers enhanced resistance to F. graminearum in maize.Together, we demonstrate that F. graminearum dampens maize immunity by deploying an apoplastic effector to induce extracellular immune receptor degradation.An apoplastic fungal effector disrupts N-glycosylation of ZmLecRK1 for degradation to suppress disease resistance in maize 1. Fusarium graminearum secretes FgLPMO9A to specifically inhibit ZmLecRK1-mediated resistance in maize Highlights The fungal apoplastic effector FgLPMO9A inhibits ZmLecRK1-mediated resistance in maize FgLPMO9A primarily interacts with the S-domain of ZmLecRK1 FgLPMO9A targets the N-glycosylation sites of ZmLecRK1 to induce its degradation FgLPMO9A mediates the autophagy-dependent degradation of ZmLecRK1 The modification of N341 site in ZmLecRK1 provides a new strategy for molecular design of disease resistance in maize This study provides a representative example of how a fungal apoplastic effector targets a pattern recognition receptor (PRR) and induces its degradation to suppress plant immunity 2. FgLPMO9A interacts with Y294 at the S-domain of ZmLecRK1 to inhibit its activity 3. FgLPMO9A mediates the autophagy-dependent degradation of ZmLecRK1 4. FgLPMO9A disrupts the N-glycosylation of N341 in ZmLecRK1 to suppress disease resistance in maize https://www.labxing.com/zhulab