A trehalase-derived MAMP triggers LecRK-V-mediated immune responses in <i>Arabidopsis</i>.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 40737394.
- Also identified by DOI 10.1126/sciadv.adv8896 and PMC identifier 12309661.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
Plant-parasitic nematodes (PPNs) cause major agricultural losses worldwide, yet the molecular basis of plant immunity against these pathogens remains poorly understood. To investigate how plants recognize PPNs, we aimed to identify microbe-associated molecular patterns (MAMPs) from nematodes and the corresponding plant immune components. Because of the limited availability of material from obligate PPNs, we used <i>Caenorhabditis elegans</i>, a free-living nematode, as a MAMP source. <i>C. elegans</i> extract activated MAMP-triggered immune responses in <i>Arabidopsis</i> Col-0. Through chromatography-based purification, we identified a secreted trehalase and pinpointed a conserved peptide region essential for its MAMP activity. A corresponding peptide from root-knot nematode trehalase enabled the identification of lectin receptor kinases LecRK-V.5 and LecRK-V.6 as key components in immune induction. Notably, this peptide region is conserved across some phytophagous insects and fungal pathogens, with LecRK-Vs required for immune responses to these peptides, highlighting the role of LecRK-V-mediated mechanism for broad-spectrum pathogen detection via trehalase-derived peptides.
Medical subject headings
- Arabidopsis
- Trehalase
- Plant Immunity
- Arabidopsis Proteins
- Pathogen-Associated Molecular Pattern Molecules