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-Durán; 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-Durán, Frederikke Gro Malinovsky, Jacqueline Monaghan, Frank L Menke, Steven C Huber, Sheng Yang He, Cyril Zipfel

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 - 28 Mar 2014

Keywords

Arabidopsis
Arabidopsis Proteins
Bacterial Proteins
Peptide Elongation Factor Tu
Peptides
Phosphorylation
Protein Tyrosine Phosphatases
Pseudomonas syringae
Receptors, Pattern Recognition
Tyrosine

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10.1126/science.1248849

Frank Menke
- F.Menkeuea.acuk
- School of Biological Sciences - Honorary Associate Professor
- The Sainsbury Laboratory - Head of Proteomics (TSL)
Person: Honorary, Research & Analogous
Jan Sklenar
- J.Sklenaruea.acuk
- The Sainsbury Laboratory - Proteomics Support Officer (TSL)
Person: Research & Analogous
Cyril Zipfel
- C.Zipfeluea.acuk
- The Sainsbury Laboratory - Senior Scientist (TSL)
- Plant Sciences - Member
Person: Research Group Member, Academic, Teaching & Research

Signaling to plant immunity responses (PathoNet)
Zipfel, C.
Biotechnology and Biological Sciences Research Council
1/10/09 → 30/09/12
Project: Research

Cite this

Macho, A. P., Schwessinger, B., Ntoukakis, V., Brutus, A., Segonzac, C., Roy, S., Kadota, Y., Oh, M-H., Sklenar, J., Derbyshire, P., Lozano-Durán, 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.",

keywords = "Arabidopsis, Arabidopsis Proteins, Bacterial Proteins, Peptide Elongation Factor Tu, Peptides, Phosphorylation, Protein Tyrosine Phosphatases, Pseudomonas syringae, Receptors, Pattern Recognition, Tyrosine",

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 Man-Ho Oh and Jan Sklenar and Paul Derbyshire and Rosa Lozano-Dur{\'a}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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doi = "10.1126/science.1248849",

language = "English",

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Macho, AP, Schwessinger, B, Ntoukakis, V, Brutus, A, Segonzac, C, Roy, S, Kadota, Y, Oh, M-H, Sklenar, J , Derbyshire, P, Lozano-Durán, 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-Durán, Rosa

AU - Malinovsky, Frederikke Gro

AU - Monaghan, Jacqueline

AU - Menke, Frank L

AU - Huber, Steven C

AU - He, Sheng Yang

AU - Zipfel, Cyril

PY - 2014/3/28

Y1 - 2014/3/28

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.

KW - Arabidopsis

KW - Arabidopsis Proteins

KW - Bacterial Proteins

KW - Peptide Elongation Factor Tu

KW - Peptides

KW - Phosphorylation

KW - Protein Tyrosine Phosphatases

KW - Pseudomonas syringae

KW - Receptors, Pattern Recognition

KW - Tyrosine

U2 - 10.1126/science.1248849

DO - 10.1126/science.1248849

M3 - Article

C2 - 24625928

VL - 343

SP - 1509

EP - 1512

JO - Science

JF - Science

SN - 0036-8075

IS - 6178

ER -

A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation

Abstract

Keywords

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Profiles

Frank Menke

Jan Sklenar

Cyril Zipfel

Projects

Signaling to plant immunity responses (PathoNet)

Cite this