Abstract
In both animals and plants, the perception of bacterial flagella by immune receptors elicits the activation of defence responses. Most plants are able to perceive the highly conserved epitope flg22 from flagellin, the main flagellar protein, from most bacterial species. However, flagellin from Ralstonia solanacearum, the causal agent of the bacterial wilt disease, presents a polymorphic flg22 sequence (flg22Rso) that avoids perception by all plants studied to date. In this work, we show that soybean has developed polymorphic versions of the flg22 receptors that are able to perceive flg22Rso. Furthermore, we identify key residues responsible for both the evasion of perception by flg22Rso in Arabidopsis and the gain of perception by the soybean receptors. Heterologous expression of the soybean flg22 receptors in susceptible plant species, such as tomato, enhances resistance to bacterial wilt disease, demonstrating the potential of these receptors to enhance disease resistance in crop plants.
Highlights
In both animals and plants, the perception of bacterial flagella by immune receptors elicits the activation of defence responses
The crystal structure of Arabidopsis FLAGELLIN-SENSITIVE 2 (FLS2) and BAK1 ectodomains has been solved in complex with flg[22] from P. aeruginosa[5,17]
Solanaceous plants have been reported as susceptible hosts for numerous R. solanacearum strains[19], and we previously found that several plant species from the Solanaceae family, including tomato, potato, pepper, tobacco, and N. benthamiana, cannot perceive flg22Rso[13]
Summary
In both animals and plants, the perception of bacterial flagella by immune receptors elicits the activation of defence responses. A glycine residue in the position 18 (G18) is present in most immune-eliciting flg[22] sequences, including those from P. aeruginosa (flg22Pae) or the notorious plant pathogen P. syringae (flg22Psy) (Supplementary Fig. 1a), and is essential for the interaction of FLS2-bound flg[22] with BAK15.
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