A trehalase-derived MAMP triggers LecRK-V-mediated immune responses in Arabidopsis

2025 · doi:10.1101/2025.02.02.636166
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Trehalase-derived peptides from nematodes activate LecRK-V-mediated immune responses in Arabidopsis, suggesting a broad-spectrum mechanism for detecting various pathogens.

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The study investigated how plants recognize microbe-associated molecular patterns (MAMPs) from plant-parasitic nematodes by using extracts from the free-living nematode Caenorhabditis elegans to stimulate Arabidopsis immune responses. After chromatography-based purification, the authors identified a secreted trehalase and mapped a conserved peptide region required for its MAMP activity, then used a similar peptide from root-knot nematode trehalase to identify lectin receptor kinases LecRK-V.5 and LecRK-V.6 as key components for inducing immunity. The authors report that this peptide region is conserved across insect and fungal pathogens and that LecRK-V kinases are required for immune responses to these peptides, though they note reliance on C. elegans as a surrogate because obligate plant-parasitic nematode material is limited. The paper does not explicitly discuss endometriosis or adenomyosis; it was included in the corpus via a keyword match in the upstream search index.

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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. Due to the limited availability of material from obligate PPNs, we used Caenorhabditis elegans , a free-living nematode, as a MAMP source. C. elegans extracts activated MAMP-triggered immune responses in Arabidopsis 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 insect 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. Teaser Trehalase-derived peptides trigger LecRK-V-mediated immune responses in plants, enabling broad detection of nematodes, insects, and fungi.
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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. Due to the limited availability of material from obligate PPNs, we used Caenorhabditis elegans, a free-living nematode, as a MAMP source. C. elegans extracts activated MAMP-triggered immune responses in Arabidopsis 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 insect 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. Teaser Trehalase-derived peptides trigger LecRK-V-mediated immune responses in plants, enabling broad detection of nematodes, insects, and fungi. Competing Interest Statement The authors have declared no competing interest.

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