Plasticity of the β-Trefoil Protein Fold in the Recognition and Control of Invertebrate Predators and Parasites by a Fungal Defence System
- Author: mycolabadmin
- 2012-05-17
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Summary
This research reveals how mushrooms protect themselves against tiny predators like roundworms and insects using specialized proteins called lectins. The studied lectin (CCL2) acts like a targeted weapon that specifically recognizes and binds to sugar molecules found only on the predators’ cells, not on the mushroom’s own cells. This allows the mushroom to defend itself without causing self-harm.
Impacts on everyday life:
– Provides insights into developing new natural pesticides for agriculture
– Could lead to novel treatments for parasitic worm infections in humans and animals
– Demonstrates nature’s elegant solutions for self-defense that could inspire new therapeutic approaches
– Helps understand how organisms can specifically target threats while avoiding damage to themselves
– Could be used as a tool for detecting specific sugar molecules in medical diagnostics
Background
Discrimination between self and non-self is essential for any defence mechanism. In innate defence, this discrimination is often mediated by lectins that recognize non-self carbohydrate structures. Recently, cytoplasmic lectins from fungal fruiting bodies have been shown to play a role in defending multicellular fungi against predators and parasites.
Objective
To characterize a novel fruiting body lectin, CCL2, from the ink cap mushroom Coprinopsis cinerea and determine its structure, specificity, and role in fungal defense against invertebrate predators.
Results
CCL2 was found to adopt a β-trefoil fold and bind with high specificity and affinity to α1,3-fucosylated chitobiose using a novel binding site. The lectin showed strong toxicity towards C. elegans and D. melanogaster but not other tested organisms. This toxicity was dependent on the presence of specific fucosylated N-glycan core structures in the target organisms. Fluorescence microscopy showed CCL2 binding to intestinal glycoproteins in C. elegans.
Conclusion
The study demonstrates how fungi exploit the plasticity of the β-trefoil fold to create novel lectin specificities for defense. CCL2 specifically recognizes invertebrate-specific glycans absent in fungi, allowing discrimination between self and non-self. The high-affinity binding site enables toxicity through a novel mechanism that does not require lectin multimerization.
- Published in:PLoS Pathogens,
- Study Type:Basic Research,
- Source: 10.1371/journal.ppat.1002706