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The Biological Action and Structural Characterization of Eryngitin 3 and 4, Ribotoxin-like Proteins from Pleurotus eryngii Fruiting Bodies

Summary

This research examined two proteins found in king trumpet mushrooms that can block protein production in cells. The study revealed how small differences in these proteins’ structures affect their ability to kill cancer cells and harmful fungi. This has important implications for developing new treatments and understanding how mushrooms defend themselves. Impacts on everyday life: • Could lead to new targeted cancer treatments with fewer side effects • May help develop better natural fungicides for agriculture • Improves understanding of medicinal mushroom properties • Contributes to knowledge about food safety of edible mushrooms • May lead to new applications in biotechnology and medicine

Background

Ribotoxin-like proteins (RL-Ps) are specific ribonucleases found in mushrooms that cleave a single phosphodiester bond in the sarcin-ricin loop (SRL) of large rRNA. This cleavage affects interactions with ribosomal proteins and blocks protein synthesis by preventing damaged ribosomes from interacting with elongation factors.

Objective

To determine the amino acid sequences of eryngitin 3 and 4 isolated from Pleurotus eryngii fruiting bodies in order to obtain structural information on this ribonuclease family from edible mushrooms and explore the structural determinants that explain their different biological and antipathogenic activities.

Results

Both eryngitin 3 and 4 consist of 132 amino acids with a single free cysteinyl residue. The key differences are an additional phenylalanyl residue at the N-terminus of eryngitin 3 and an additional arginyl residue at the C-terminus of eryngitin 4. Eryngitin 3 exhibited higher toxicity against tumor cell lines and model fungi compared to eryngitin 4. The 3D models showed slight differences in electrostatic surfaces at the N- and C-terminal regions that may explain their different biological activities.

Conclusion

The structural differences between eryngitin 3 and 4, particularly the additional amino acids at their termini, appear to be responsible for their different levels of biological activity. The additional positive charge at eryngitin 4’s C-terminus may interfere with substrate binding or recognition. Both proteins likely derive from the same gene transcript but undergo different post-translational processing to produce enzymes with distinct activities.
  • Published in:International Journal of Molecular Sciences,
  • Study Type:Laboratory Research,
  • Source: 10.3390/ijms241914435
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