A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation.

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • 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

Published Date

  • March 2014

Published In

Volume / Issue

  • 343 / 6178

Start / End Page

  • 1509 - 1512

PubMed ID

  • 24625928

Electronic International Standard Serial Number (EISSN)

  • 1095-9203

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1248849


  • eng