Abstract
Plant plasma membrane localized pattern recognition receptors (PRRs) detect extracellular pathogen-associated molecules. PRRs such as Arabidopsis EFR and rice XA21 are taxonomically restricted and are absent from most plant genomes. Here we show that rice plants expressing EFR or the chimeric receptor EFR::XA21, containing the EFR ectodomain and the XA21 intracellular domain, sense both Escherichia coli- and Xanthomonas oryzae pv. oryzae (Xoo)-derived elf18 peptides at sub-nanomolar concentrations. Treatment of EFR and EFR::XA21 rice leaf tissue with elf18 leads to MAP kinase activation, reactive oxygen production and defense gene expression. Although expression of EFR does not lead to robust enhanced resistance to fully virulent Xoo isolates, it does lead to quantitatively enhanced resistance to weakly virulent Xoo isolates. EFR interacts with OsSERK2 and the XA21 binding protein 24 (XB24), two key components of the rice XA21-mediated immune response. Rice-EFR plants silenced for OsSERK2, or overexpressing rice XB24 are compromised in elf18-induced reactive oxygen production and defense gene expression indicating that these proteins are also important for EFR-mediated signaling in transgenic rice. Taken together, our results demonstrate the potential feasibility of enhancing disease resistance in rice and possibly other monocotyledonous crop species by expression of dicotyledonous PRRs. Our results also suggest that Arabidopsis EFR utilizes at least a subset of the known endogenous rice XA21 signaling components.
Original language | English |
---|---|
Article number | e1004809 |
Journal | PLoS Pathogens |
Volume | 11 |
Issue number | 3 |
Early online date | 30 Mar 2015 |
DOIs | |
Publication status | Published - Mar 2015 |
Keywords
- Arabidopsis Proteins
- Oryza
- Plant Proteins
- Genetically Modified Plants
- Protein-Serine-Threonine Kinases
- Pattern Recognition Receptors
- Recombinant Fusion Proteins
- Signal Transduction
Profiles
-
Cyril Zipfel
- The Sainsbury Laboratory - Senior Scientist (TSL)
- Plant Sciences - Member
Person: Research Group Member, Academic, Teaching & Research