A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation

Alberto P. Macho; Benjamin Schwessinger; Vardis Ntoukakis; Alexandre Brutus; Cécile Segonzac; Sonali Roy; Yasuhiro Kadota; Man Ho Oh; Jan Sklenar; Paul Derbyshire; Rosa Lozano-Durań; Frederikke Gro Malinovsky; Jacqueline Monaghan; Frank L. Menke; Steven C. Huber; Sheng Yang He; Cyril Zipfel

doi:10.1126/science.1248849

A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation

Alberto P. Macho, Benjamin Schwessinger, Vardis Ntoukakis, Alexandre Brutus, Cécile Segonzac, Sonali Roy, Yasuhiro Kadota, Man Ho Oh, Jan Sklenar, Paul Derbyshire, Rosa Lozano-Durań, Frederikke Gro Malinovsky, Jacqueline Monaghan, Frank L. Menke, Steven C. Huber, Sheng Yang He, Cyril Zipfel^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

128 Citations (Scopus)

Abstract

Innate immunity relies on the perception of pathogen-associated molecular patterns (PAMPs) by pattern-recognition receptors (PRRs) located on the host cell's surface. Many plant PRRs are kinases. Here, we report that the Arabidopsis receptor kinase EF-TU RECEPTOR (EFR), which perceives the elf18 peptide derived from bacterial elongation factor Tu, is activated upon ligand binding by phosphorylation on its tyrosine residues. Phosphorylation of a single tyrosine residue, Y836, is required for activation of EFR and downstream immunity to the phytopathogenic bacterium Pseudomonas syringae. A tyrosine phosphatase, HopAO1, secreted by P. syringae, reduces EFR phosphorylation and prevents subsequent immune responses. Thus, host and pathogen compete to take control of PRR tyrosine phosphorylation used to initiate antibacterial immunity.

Original language	English
Pages (from-to)	1509-1512
Number of pages	4
Journal	Science
Volume	343
Issue number	6178
DOIs	https://doi.org/10.1126/science.1248849
Publication status	Published - 2014
Externally published	Yes

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Macho, A. P., Schwessinger, B., Ntoukakis, V., Brutus, A., Segonzac, C., Roy, S., Kadota, Y., Oh, M. H., Sklenar, J., Derbyshire, P., Lozano-Durań, R., Malinovsky, F. G., Monaghan, J., Menke, F. L., Huber, S. C., He, S. Y., & Zipfel, C. (2014). A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation. Science, 343(6178), 1509-1512. https://doi.org/10.1126/science.1248849

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title = "A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation",

abstract = "Innate immunity relies on the perception of pathogen-associated molecular patterns (PAMPs) by pattern-recognition receptors (PRRs) located on the host cell's surface. Many plant PRRs are kinases. Here, we report that the Arabidopsis receptor kinase EF-TU RECEPTOR (EFR), which perceives the elf18 peptide derived from bacterial elongation factor Tu, is activated upon ligand binding by phosphorylation on its tyrosine residues. Phosphorylation of a single tyrosine residue, Y836, is required for activation of EFR and downstream immunity to the phytopathogenic bacterium Pseudomonas syringae. A tyrosine phosphatase, HopAO1, secreted by P. syringae, reduces EFR phosphorylation and prevents subsequent immune responses. Thus, host and pathogen compete to take control of PRR tyrosine phosphorylation used to initiate antibacterial immunity.",

author = "Macho, {Alberto P.} and Benjamin Schwessinger and Vardis Ntoukakis and Alexandre Brutus and C{\'e}cile Segonzac and Sonali Roy and Yasuhiro Kadota and Oh, {Man Ho} and Jan Sklenar and Paul Derbyshire and Rosa Lozano-Dura{\'n} and Malinovsky, {Frederikke Gro} and Jacqueline Monaghan and Menke, {Frank L.} and Huber, {Steven C.} and He, {Sheng Yang} and Cyril Zipfel",

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Macho, AP, Schwessinger, B, Ntoukakis, V, Brutus, A, Segonzac, C, Roy, S, Kadota, Y, Oh, MH, Sklenar, J, Derbyshire, P, Lozano-Durań, R, Malinovsky, FG, Monaghan, J, Menke, FL, Huber, SC, He, SY & Zipfel, C 2014, 'A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation', Science, vol. 343, no. 6178, pp. 1509-1512. https://doi.org/10.1126/science.1248849

TY - JOUR

T1 - A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation

AU - Macho, Alberto P.

AU - Schwessinger, Benjamin

AU - Ntoukakis, Vardis

AU - Brutus, Alexandre

AU - Segonzac, Cécile

AU - Roy, Sonali

AU - Kadota, Yasuhiro

AU - Oh, Man Ho

AU - Sklenar, Jan

AU - Derbyshire, Paul

AU - Lozano-Durań, Rosa

AU - Malinovsky, Frederikke Gro

AU - Monaghan, Jacqueline

AU - Menke, Frank L.

AU - Huber, Steven C.

AU - He, Sheng Yang

AU - Zipfel, Cyril

PY - 2014

Y1 - 2014

N2 - Innate immunity relies on the perception of pathogen-associated molecular patterns (PAMPs) by pattern-recognition receptors (PRRs) located on the host cell's surface. Many plant PRRs are kinases. Here, we report that the Arabidopsis receptor kinase EF-TU RECEPTOR (EFR), which perceives the elf18 peptide derived from bacterial elongation factor Tu, is activated upon ligand binding by phosphorylation on its tyrosine residues. Phosphorylation of a single tyrosine residue, Y836, is required for activation of EFR and downstream immunity to the phytopathogenic bacterium Pseudomonas syringae. A tyrosine phosphatase, HopAO1, secreted by P. syringae, reduces EFR phosphorylation and prevents subsequent immune responses. Thus, host and pathogen compete to take control of PRR tyrosine phosphorylation used to initiate antibacterial immunity.

AB - Innate immunity relies on the perception of pathogen-associated molecular patterns (PAMPs) by pattern-recognition receptors (PRRs) located on the host cell's surface. Many plant PRRs are kinases. Here, we report that the Arabidopsis receptor kinase EF-TU RECEPTOR (EFR), which perceives the elf18 peptide derived from bacterial elongation factor Tu, is activated upon ligand binding by phosphorylation on its tyrosine residues. Phosphorylation of a single tyrosine residue, Y836, is required for activation of EFR and downstream immunity to the phytopathogenic bacterium Pseudomonas syringae. A tyrosine phosphatase, HopAO1, secreted by P. syringae, reduces EFR phosphorylation and prevents subsequent immune responses. Thus, host and pathogen compete to take control of PRR tyrosine phosphorylation used to initiate antibacterial immunity.

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U2 - 10.1126/science.1248849

DO - 10.1126/science.1248849

M3 - Article

SN - 0036-8075

VL - 343

SP - 1509

EP - 1512

JO - Science

JF - Science

IS - 6178

ER -

A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation

Abstract

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