A Plant Lectin Receptor-like Kinase Phosphorylates the Bacterial Effector AvrPtoB to Dampen Its Virulence in Arabidopsis.
Identifieur interne : 000239 ( Main/Exploration ); précédent : 000238; suivant : 000240A Plant Lectin Receptor-like Kinase Phosphorylates the Bacterial Effector AvrPtoB to Dampen Its Virulence in Arabidopsis.
Auteurs : Ning Xu [République populaire de Chine] ; Xuming Luo [République populaire de Chine] ; Wei Wu [République populaire de Chine] ; Yingying Xing [République populaire de Chine] ; Yingbo Liang [République populaire de Chine] ; Yanzhi Liu [République populaire de Chine] ; Huasong Zou [République populaire de Chine] ; Hai-Lei Wei [République populaire de Chine] ; Jun Liu [République populaire de Chine]Source :
- Molecular plant [ 1752-9867 ] ; 2020.
Abstract
Plasma membrane-localized receptor-like kinases (RLKs) perceive conserved pathogen-associated molecular patterns (PAMPs) in plants, leading to PAMP-triggered immunity (PTI). The Arabidopsis thaliana lectin RLK LecRK-IX.2 has been shown to regulate the bacterial flagellin-derived peptide flg22-induced PTI. Here, we discover that Pseudomonas syringae effector AvrPtoB targets LecRK-IX.2 for degradation, which subsequently suppresses LecRK-IX.2-mediated PTI and disease resistance. However, LecRK-IX.2 can interact with and phosphorylate AvrPtoB at serine site 335 (S335). AvrPtoB self-associates in vitro and in vivo, and the association appears to be essential for its E3 ligase activity in ubiquitinating substrate in plants. Phosphorylation of S335 disrupts the self-association and as a result, phosphomimetic AvrPtoBS335D cannot ubiquitinate LecRK-IX.2 efficiently, leading to the compromised virulence of AvrPtoB in suppressing PTI responses. flg22 enhances AvrPtoB S335 phosphorylation by inducing the expression and activating of LecRK-IX.2. Our study demonstrates that host RLKs can modify pathogen effectors to dampen their virulence and undermine their ability in suppressing PTI.
DOI: 10.1016/j.molp.2020.09.016
PubMed: 32977056
Affiliations:
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<front><div type="abstract" xml:lang="en">Plasma membrane-localized receptor-like kinases (RLKs) perceive conserved pathogen-associated molecular patterns (PAMPs) in plants, leading to PAMP-triggered immunity (PTI). The Arabidopsis thaliana lectin RLK LecRK-IX.2 has been shown to regulate the bacterial flagellin-derived peptide flg22-induced PTI. Here, we discover that Pseudomonas syringae effector AvrPtoB targets LecRK-IX.2 for degradation, which subsequently suppresses LecRK-IX.2-mediated PTI and disease resistance. However, LecRK-IX.2 can interact with and phosphorylate AvrPtoB at serine site 335 (S335). AvrPtoB self-associates in vitro and in vivo, and the association appears to be essential for its E3 ligase activity in ubiquitinating substrate in plants. Phosphorylation of S335 disrupts the self-association and as a result, phosphomimetic AvrPtoB<sup>S335D</sup>
cannot ubiquitinate LecRK-IX.2 efficiently, leading to the compromised virulence of AvrPtoB in suppressing PTI responses. flg22 enhances AvrPtoB S335 phosphorylation by inducing the expression and activating of LecRK-IX.2. Our study demonstrates that host RLKs can modify pathogen effectors to dampen their virulence and undermine their ability in suppressing PTI.</div>
</front>
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<Abstract><AbstractText>Plasma membrane-localized receptor-like kinases (RLKs) perceive conserved pathogen-associated molecular patterns (PAMPs) in plants, leading to PAMP-triggered immunity (PTI). The Arabidopsis thaliana lectin RLK LecRK-IX.2 has been shown to regulate the bacterial flagellin-derived peptide flg22-induced PTI. Here, we discover that Pseudomonas syringae effector AvrPtoB targets LecRK-IX.2 for degradation, which subsequently suppresses LecRK-IX.2-mediated PTI and disease resistance. However, LecRK-IX.2 can interact with and phosphorylate AvrPtoB at serine site 335 (S335). AvrPtoB self-associates in vitro and in vivo, and the association appears to be essential for its E3 ligase activity in ubiquitinating substrate in plants. Phosphorylation of S335 disrupts the self-association and as a result, phosphomimetic AvrPtoB<sup>S335D</sup>
cannot ubiquitinate LecRK-IX.2 efficiently, leading to the compromised virulence of AvrPtoB in suppressing PTI responses. flg22 enhances AvrPtoB S335 phosphorylation by inducing the expression and activating of LecRK-IX.2. Our study demonstrates that host RLKs can modify pathogen effectors to dampen their virulence and undermine their ability in suppressing PTI.</AbstractText>
<CopyrightInformation>Copyright © 2020 The Author. Published by Elsevier Inc. All rights reserved.</CopyrightInformation>
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<settlement><li>Fuzhou</li>
<li>Pékin</li>
</settlement>
</list>
<tree><country name="République populaire de Chine"><noRegion><name sortKey="Xu, Ning" sort="Xu, Ning" uniqKey="Xu N" first="Ning" last="Xu">Ning Xu</name>
</noRegion>
<name sortKey="Liang, Yingbo" sort="Liang, Yingbo" uniqKey="Liang Y" first="Yingbo" last="Liang">Yingbo Liang</name>
<name sortKey="Liu, Jun" sort="Liu, Jun" uniqKey="Liu J" first="Jun" last="Liu">Jun Liu</name>
<name sortKey="Liu, Yanzhi" sort="Liu, Yanzhi" uniqKey="Liu Y" first="Yanzhi" last="Liu">Yanzhi Liu</name>
<name sortKey="Luo, Xuming" sort="Luo, Xuming" uniqKey="Luo X" first="Xuming" last="Luo">Xuming Luo</name>
<name sortKey="Wei, Hai Lei" sort="Wei, Hai Lei" uniqKey="Wei H" first="Hai-Lei" last="Wei">Hai-Lei Wei</name>
<name sortKey="Wu, Wei" sort="Wu, Wei" uniqKey="Wu W" first="Wei" last="Wu">Wei Wu</name>
<name sortKey="Xing, Yingying" sort="Xing, Yingying" uniqKey="Xing Y" first="Yingying" last="Xing">Yingying Xing</name>
<name sortKey="Zou, Huasong" sort="Zou, Huasong" uniqKey="Zou H" first="Huasong" last="Zou">Huasong Zou</name>
</country>
</tree>
</affiliations>
</record>
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