TY - JOUR
T1 - Convergent evolution of plant pattern recognition receptors sensing cysteine-rich patterns from three microbial kingdoms
AU - Yang, Yuankun
AU - Steidele, Christina E.
AU - Rössner, Clemens
AU - Löffelhardt, Birgit
AU - Kolb, Dagmar
AU - Leisen, Thomas
AU - Zhang, Weiguo
AU - Ludwig, Christina
AU - Felix, Georg
AU - Seidl, Michael F.
AU - Becker, Annette
AU - Nürnberger, Thorsten
AU - Hahn, Matthias
AU - Gust, Bertolt
AU - Gross, Harald
AU - Hückelhoven, Ralph
AU - Gust, Andrea A.
PY - 2023/6/19
Y1 - 2023/6/19
N2 - The Arabidopsis thaliana Receptor-Like Protein RLP30 contributes to immunity against the fungal pathogen Sclerotinia sclerotiorum. Here we identify the RLP30-ligand as a small cysteine-rich protein (SCP) that occurs in many fungi and oomycetes and is also recognized by the Nicotiana benthamiana RLP RE02. However, RLP30 and RE02 share little sequence similarity and respond to different parts of the native/folded protein. Moreover, some Brassicaceae other than Arabidopsis also respond to a linear SCP peptide instead of the folded protein, suggesting that SCP is an eminent immune target that led to the convergent evolution of distinct immune receptors in plants. Surprisingly, RLP30 shows a second ligand specificity for a SCP-nonhomologous protein secreted by bacterial Pseudomonads. RLP30 expression in N. tabacum results in quantitatively lower susceptibility to bacterial, fungal and oomycete pathogens, thus demonstrating that detection of immunogenic patterns by Arabidopsis RLP30 is involved in defense against pathogens from three microbial kingdoms.
AB - The Arabidopsis thaliana Receptor-Like Protein RLP30 contributes to immunity against the fungal pathogen Sclerotinia sclerotiorum. Here we identify the RLP30-ligand as a small cysteine-rich protein (SCP) that occurs in many fungi and oomycetes and is also recognized by the Nicotiana benthamiana RLP RE02. However, RLP30 and RE02 share little sequence similarity and respond to different parts of the native/folded protein. Moreover, some Brassicaceae other than Arabidopsis also respond to a linear SCP peptide instead of the folded protein, suggesting that SCP is an eminent immune target that led to the convergent evolution of distinct immune receptors in plants. Surprisingly, RLP30 shows a second ligand specificity for a SCP-nonhomologous protein secreted by bacterial Pseudomonads. RLP30 expression in N. tabacum results in quantitatively lower susceptibility to bacterial, fungal and oomycete pathogens, thus demonstrating that detection of immunogenic patterns by Arabidopsis RLP30 is involved in defense against pathogens from three microbial kingdoms.
U2 - 10.1038/s41467-023-39208-8
DO - 10.1038/s41467-023-39208-8
M3 - Article
C2 - 37336953
AN - SCOPUS:85162270261
SN - 2041-1723
VL - 14
JO - Nature Communications
JF - Nature Communications
IS - 1
M1 - 3621
ER -