A lectin S-domain receptor kinase mediates lipopolysaccharide sensing in Arabidopsis thaliana

Plants have a vast array of pattern-recognition receptor to detect microbial ligands, but how they sense lipopolysaccharide has remained unknown. Ranf et al. identify the receptor-like kinase SD1-29 as a de facto pattern-recognition receptor for lipopolysaccharide in Arabidopsis . The sensing of mic...

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Published inNature immunology Vol. 16; no. 4; pp. 426 - 433
Main Authors Ranf, Stefanie, Gisch, Nicolas, Schäffer, Milena, Illig, Tina, Westphal, Lore, Knirel, Yuriy A, Sánchez-Carballo, Patricia M, Zähringer, Ulrich, Hückelhoven, Ralph, Lee, Justin, Scheel, Dierk
Format Journal Article
LanguageEnglish
Published New York Nature Publishing Group US 01.04.2015
Nature Publishing Group
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Summary:Plants have a vast array of pattern-recognition receptor to detect microbial ligands, but how they sense lipopolysaccharide has remained unknown. Ranf et al. identify the receptor-like kinase SD1-29 as a de facto pattern-recognition receptor for lipopolysaccharide in Arabidopsis . The sensing of microbe-associated molecular patterns (MAMPs) triggers innate immunity in animals and plants. Lipopolysaccharide (LPS) from Gram-negative bacteria is a potent MAMP for mammals, with the lipid A moiety activating proinflammatory responses via Toll-like receptor 4 (TLR4). Here we found that the plant Arabidopsis thaliana specifically sensed LPS of Pseudomonas and Xanthomonas . We isolated LPS-insensitive mutants defective in the bulb-type lectin S-domain-1 receptor–like kinase LORE (SD1-29), which were hypersusceptible to infection with Pseudomonas syringae . Targeted chemical degradation of LPS from Pseudomonas species suggested that LORE detected mainly the lipid A moiety of LPS. LORE conferred sensitivity to LPS onto tobacco after transient expression, which demonstrated a key function in LPS sensing and indicated the possibility of engineering resistance to bacteria in crop species.
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ISSN:1529-2908
1529-2916
DOI:10.1038/ni.3124