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Kinetic proofreading of lipochitooligosaccharides determines signal activation of symbiotic plant receptors

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DOI

  • Kira Gysel
  • Mette Laursen
  • ,
  • Mikkel B Thygesen, Department of Chemistry, University of Copenhagen
  • ,
  • Damiano Lironi
  • ,
  • Zoltán Bozsóki
  • ,
  • Christian T Hjuler, Department of Chemistry, University of Copenhagen
  • ,
  • Nicolai N Maolanon, Department of Chemistry, University of Copenhagen
  • ,
  • Jeryl Cheng
  • ,
  • Peter K Bjørk
  • Maria Vinther
  • Lene H Madsen
  • Henriette Rübsam
  • Artur Muszyński, Complex Carbohydrate Research Center, University of Georgia, United States;
  • ,
  • Arshia Ghodrati, Complex Carbohydrate Research Center, University of Georgia, United States;
  • ,
  • Parastoo Azadi, Complex Carbohydrate Research Center, University of Georgia, United States;
  • ,
  • John T. Sullivan, Department of Microbiology and Immunology, University of Otago
  • ,
  • Clive W Ronson, Department of Microbiology and Immunology, University of Otago
  • ,
  • Knud J Jensen, Department of Chemistry, University of Copenhagen
  • ,
  • Mickaël Blaise, Montpellier University, UMR 1183, Montpellier, France
  • ,
  • Simona Radutoiu
  • Jens Stougaard
  • Kasper R Andersen

Plants and animals use cell surface receptors to sense and interpret environmental signals. In legume symbiosis with nitrogen-fixing bacteria, the specific recognition of bacterial lipochitooligosaccharide (LCO) signals by single-pass transmembrane receptor kinases determines compatibility. Here, we determine the structural basis for LCO perception from the crystal structures of two lysin motif receptor ectodomains and identify a hydrophobic patch in the binding site essential for LCO recognition and symbiotic function. We show that the receptor monitors the composition of the amphiphilic LCO molecules and uses kinetic proofreading to control receptor activation and signaling specificity. We demonstrate engineering of the LCO binding site to fine-tune ligand selectivity and correct binding kinetics required for activation of symbiotic signaling in plants. Finally, the hydrophobic patch is found to be a conserved structural signature in this class of LCO receptors across legumes that can be used for in silico predictions. Our results provide insights into the mechanism of cell-surface receptor activation by kinetic proofreading of ligands and highlight the potential in receptor engineering to capture benefits in plant-microbe interactions.

Original languageEnglish
Article numbere2111031118
JournalProceedings of the National Academy of Sciences of the United States of America
Volume118
Issue44
ISSN0027-8424
DOIs
Publication statusPublished - Nov 2021

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Copyright © 2021 the Author(s). Published by PNAS.

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