A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation

Science. 2014 Mar 28;343(6178):1509-12. doi: 10.1126/science.1248849. Epub 2014 Mar 13.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Arabidopsis / immunology*
  • Arabidopsis / microbiology*
  • Arabidopsis Proteins / agonists
  • Arabidopsis Proteins / metabolism*
  • Bacterial Proteins / metabolism*
  • Peptide Elongation Factor Tu / metabolism*
  • Peptides / metabolism
  • Peptides / pharmacology
  • Phosphorylation
  • Protein Tyrosine Phosphatases / metabolism*
  • Pseudomonas syringae / enzymology
  • Pseudomonas syringae / pathogenicity*
  • Receptors, Pattern Recognition / agonists
  • Receptors, Pattern Recognition / metabolism*
  • Tyrosine / metabolism


  • Arabidopsis Proteins
  • Bacterial Proteins
  • EFR protein, Arabidopsis
  • Peptides
  • Receptors, Pattern Recognition
  • Tyrosine
  • Protein Tyrosine Phosphatases
  • Peptide Elongation Factor Tu