Structural basis for size-selective perception of chitin in plants
Gysel, K.; Hansen, S. B.; Rübsam, H.; Alsarraf, H. M. A. B.; Madland, E.; Cheng, J. X. J.; Baadegaard, C.; Poulsen, E. C.; Vinther, M.; Fort, S.; Stougaard, J.; Andersen, K. R.
Show abstract
Plants detect microbes through pattern recognition receptors that perceive conserved microbial surface motifs known as microbe-associated molecular patterns (MAMPs). LysM receptors recognize and mediate downstream responses to chitinous MAMPs. Here, we elucidate the mechanism for the specific recognition of long-chain chitin oligomers and identify a hallmark bridge domain characteristic for the CHIP receptor class. Structural analysis of receptor-ligand complexes, biochemistry, and in planta functional studies using inhibitory nanobodies reveal the mechanism of size-selective, high affinity chitin perception in Lotus japonicus and Medicago truncatula. Additionally, we identify CERKs as low-affinity, yet essential co-receptors and propose a mechanistic model for a ligand-induced core signaling heterocomplex. Our findings provide mechanistic insights into plant chitin perception and the formation of receptor complexes critical for immune signaling.
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