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. 2022 May 31;11(11):1475. doi: 10.3390/plants11111475

Figure 4.

Figure 4

Interaction of Brachpodium leucine-rich repeat (LRR) protein sequences with bacterial flagellin protein (flg22). (a) Representative oxidative burst assays (reactive oxygen species) as assessed by the measurement of emitted photons as a proxy for Arabidopsis immune response. Results are shown for untransformed wildtype Arabidopsis (Col-0), Col-0 plants transformed with an empty vector (pCambia1305.1, shown as pCambia), and Arabidopsis lines expressing the BdIRI1, BdIRI3, and BdIRI7-encoded LRR protein products shown as LRR1, LRR3, and LRR7, respectively. The flg22 epitopes used were the flg22-γ (shown as γ) and flg22-α (shown as α) peptides previously shown to be immunogenic and non-immunogenic, respectively, to Arabidopsis. Blank controls consisting of no epitope (-) were also included. Lowercase letter groupings represent statistically significant differences (p < 0.001, one way ANOVA) and assays were repeated in triplicate with similar results. (b) Simplified illustration of how FLAGELLIN-SENSITIVE 2 (FLS2) induces the downstream release of extracellular ROS upon detection of flg22-γ epitopes. (c) Simplified illustration of how BdLRRs may attenuate with the FLS2-dependent release of extracellular ROS in the presence of flg22-γ epitopes. Illustration made using BioRender.com.