LYK4 is a component of a tripartite chitin receptor complex in Arabidopsis thaliana

LYK1, LYK4, and LYK5 form a tripartite receptor complex in Arabidopsis to perceive chitin, with constitutive LYK4–LYK5 and chitin-induced LYK1–LYK5 ectodomain interactions, and LYK4 functioning as a LYK5-associated co-receptor or scaffold protein.

Mechanisms Underlying Establishment of Arbuscular Mycorrhizal Symbioses

Most land plants engage in mutually beneficial interactions with arbuscular mycorrhizal (AM) fungi, the fungus providing phosphate and nitrogen in exchange for fixed carbon. During presymbiosis, both organisms communicate via oligosaccharides and butenolides. The requirement for a rice chitin receptor in symbiosis-induced lateral root development suggests that cell division programs operate in inner root tissues during both AM and nodule symbioses. Furthermore, the identification of transcription factors underpinning arbuscule development and degeneration reemphasized the plant's regulatory dominance in AM symbiosis. Finally, the finding that AM fungi, as lipid auxotrophs, depend on plant fatty acids (FAs) to complete their asexual life cycle revealed the basis for fungal biotrophy. Intriguingly, lipid metabolism is also central for asexual reproduction and interaction of the fungal sister clade, the Mucoromycotina, with endobacteria, indicative of an evolutionarily ancient role for lipids in fungal mutualism.

The fungal ligand chitin directly binds and signals inflammation dependent on oligomer size and TLR2

Chitin is a highly abundant polysaccharide and linked to fungal infection and asthma. Unfortunately, its polymeric structure has hampered the identification of immune receptors directly binding chitin and signaling immune activation and inflammation, because purity, molecular structure and molarity are not well definable for a polymer typically extracted from biomass. Therefore, by using defined chitin (N-acetyl-glucosamine) oligomers, we identified six subunit long chitin chains as the smallest immunologically active motif and the innate immune receptor Toll-like receptor (TLR) 2 as the primary fungal chitin receptor on human and murine immune cells. Chitin oligomers directly bound TLR2 with nanomolar affinity and showed both overlapping and distinct signaling outcomes compared to known mycobacterial TLR2 ligands. Conversely, chitin oligomers shorter than 6 subunits were inactive or showed antagonistic effects on chitin/TLR2-mediated signaling, hinting to a size-dependent sensing/activation system unexpectedly conserved in plants and humans. Since blocking the chitin-TLR2 interaction effectively prevented chitin-mediated inflammation in vitro and in vivo, our study highlights the chitin TLR2 interaction as a potential target for developing novel therapies in chitin-related pathologies and fungal disease.

Chitosan perception in Arabidopsis requires the chitin receptor AtCERK1 suggesting an improved model for receptor structure and function

Chitin, a linear polymer of N-acetyl-D-glucosamine, and chitosans, fully or partially deacetylated derivatives of chitin, are known to elicit defense reactions in higher plants. We compared the ability of chitin and chitosan oligomers and polymers (chitin oligomers with degree of polymerization 3 to 8; chitosan oligomers with degree of acetylation 0% to 35% and degree of polymerization 3 to 15; chitosan polymers with degree of acetylation 1% to 60% and degree of polymerization ~1300) to elicit an oxidative burst indicative of induced defense reactions in A. thaliana seedlings. Fully deacetylated chitosans were not able to trigger a response; elicitor activity increased with increasing degree of acetylation of chitosan polymers. Partially acetylated chitosan oligomers required a minimum degree of polymerization of 6 and at least four N-acetyl groups to trigger a response. Invariably, elicitation of an oxidative burst required the presence of the chitin receptor AtCERK1. Our results as well as previously published studies on chitin and chitosan perception in plants are best explained by a new general model of LysM-containing receptor complexes where two partners form a long, but off-set chitin-binding groove and are, thus, dimerized by one chitin or chitosan molecule, sharing a central GlcNAc unit with which both LysM domains interact. To verify this model and to distinguish it from earlier models, we assayed elicitor and inhibitor activities of selected partially acetylated chitosan oligomers with fully defined structures. In contrast to the initial “continuous groove”, the original “sandwich”, or the current “sliding mode” models for the chitin/chitosan receptor, the here proposed “slipped sandwich” model - which builds on these earlier models and represents a consensus combination of these - is in agreement with all experimental observations.