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

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126 Citations (Scopus)


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 languageEnglish
Pages (from-to)1509-1512
Number of pages4
Issue number6178
Publication statusPublished - 28 Mar 2014


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

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