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Structure-Function Relationship of a Novel Fucoside-Binding Fruiting Body Lectin from Coprinopsis cinerea Exhibiting Nematotoxic Activity

Summary

This research discovered and characterized a new protein from mushrooms that can recognize and bind to specific sugar molecules. The protein forms a unique hexagonal structure and helps protect mushrooms from being eaten by tiny worms called nematodes. Understanding how this protein works could lead to new applications in biotechnology and agriculture. Impacts on everyday life: – Provides insights into how mushrooms naturally defend themselves against pests – Could lead to development of new natural pesticides for agriculture – Advances our understanding of protein-sugar interactions important in many biological processes – May contribute to development of new tools for studying complex sugars in medicine – Could inspire new approaches for designing proteins with specific functions

Background

Lectins are non-immunoglobulin proteins that bind to specific carbohydrate epitopes and play important roles in intra- and inter-organismic interactions. They occur in all kingdoms of life and are involved in various biological processes. Fungal lectins, particularly those from fruiting bodies, have unique features including small molecular weight, high water solubility, stability across various conditions, and resistance to proteolytic degradation.

Objective

To characterize a novel fucose-specific lectin (CML1) identified from fruiting body extracts of Coprinopsis cinerea, including its structure, binding specificity, and biological function.

Results

CML1 was found to fold as a sandwich of 2 antiparallel β-sheets and forms hexamers resulting from a trimer of dimers. One carbohydrate-binding site per protomer was found at the dimer interface. The protein showed specific binding to fucosylated oligosaccharides. Mutation of key binding residues (His54, Asn55, Trp94, and Arg114) abolished both carbohydrate-binding and nematotoxicity. The lectin inhibited development of C. tropicalis but not C. elegans nematodes.

Conclusion

CML1 represents the founding member of a novel family of fucoside-binding lectins involved in the defense of agaricomycete fruiting bodies against predation by fungivorous nematodes. The protein adopts a novel fold not previously described for lectins and forms an unusual hexameric arrangement with binding sites at dimer interfaces.
  • Published in:Glycobiology,
  • Study Type:Basic Research,
  • Source: 10.1093/glycob/cwac020
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