Extended Data Fig. 6: FgLPMO9A targets the N341 residue of ZmLecRK1 to inhibit ZmLecRK1-mediated cell death in N. benthamiana leaves. | Nature Plants

Extended Data Fig. 6: FgLPMO9A targets the N341 residue of ZmLecRK1 to inhibit ZmLecRK1-mediated cell death in N. benthamiana leaves.

From: An apoplastic fungal effector disrupts N-glycosylation of ZmLecRK1, inducing its degradation to suppress disease resistance in maize

Extended Data Fig. 6

a, N341Q does not affect the interaction between ZmLecRK1ECD+TM and FgLPMO9A, as shown by the co-IP assay in N. benthamiana. b, FgLPMO9A treatment does not change the N-glycosylation level of ZmLecRK1ECD+TM with N341Q mutation, as shown by the Concanavalin A assay in N. benthamiana. c, Representative full scan MS spectra of the glycans released from ZmLecRK1ECD+TM following in vitro treatment with FgLPMO9A, exemplified by the glycan structure H(3)N(4)F(1)X(1). d, FgLPMO9A does not induce degradation of the ZmLecRK1N341Q variant, as shown by the western blot in N. benthamiana. e, FgLPMO9A cannot suppress ZmLecRK1N341Q-triggered cell death in N. benthamiana. f, Quantification of canonical N-glycosylation modification at N215 of ZmLecRK1ECD+TM with FgLPMO9A and FgLPMO9AH107A, as shown by spectrometry assay. These experiments were repeated 3 times with similar results.

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