Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

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

Sara Ragucci
ORCID logo ,
Nicola Landi
,
Lucía Citores
ORCID logo ,
Rosario Iglesias
,
Rosita Russo
ORCID logo ,
Angela Clemente
,
Michele Saviano
ORCID logo ,
Paolo Vincenzo Pedone
,
Angela Chambery
ORCID logo ,
José M. Ferreras
ORCID logo ,
Antimo Di Maro
* ORCID logo
Version 1 : Received: 28 August 2023 / Approved: 28 August 2023 / Online: 29 August 2023 (03:26:45 CEST)

A peer-reviewed article of this Preprint also exists.

Ragucci, S.; Landi, N.; Citores, L.; Iglesias, R.; Russo, R.; Clemente, A.; Saviano, M.; Pedone, P.V.; Chambery, A.; Ferreras, J.M.; Di Maro, A. The Biological Action and Structural Characterization of Eryngitin 3 and 4, Ribotoxin-like Proteins from Pleurotus eryngii Fruiting Bodies. Int. J. Mol. Sci. 2023, 24, 14435. Ragucci, S.; Landi, N.; Citores, L.; Iglesias, R.; Russo, R.; Clemente, A.; Saviano, M.; Pedone, P.V.; Chambery, A.; Ferreras, J.M.; Di Maro, A. The Biological Action and Structural Characterization of Eryngitin 3 and 4, Ribotoxin-like Proteins from Pleurotus eryngii Fruiting Bodies. Int. J. Mol. Sci. 2023, 24, 14435.

Abstract

Ribotoxin-like proteins (RL-Ps) are specific ribonucleases found in mushrooms that are able to cleave a single phosphodiester bond located in the Sarcin-Ricin Loop (SRL) of the large rRNA. The cleaved SRL interacts differently with some ribosomal proteins (P-stalk). This action blocks protein synthesis because the damaged ribosomes are unable to interact with elongation factors. Here, the amino acid sequence of eryngitin 3 and 4, RL-Ps isolated from Pleurotus eryngii fruiting bodies, was determined to: i) obtain structural information on this specific ribonuclease family from edible mushrooms; and ii) explore the structural determinants which justify their different biological and antipathogenic activities. Indeed, eryngitin 3 (exhibited higher toxicity with respect to eryngitin 4 against tumoral cell lines and model fungi. Structurally, eryngitin 3 and 4 consist of 132 amino acids, most of them identical and exhibit a single free cysteinyl residue. The amino acidic differences between the two toxins are: i) an additional phenylalanyl residue at the N-terminus of eryngitin 3, not retrieved in eryngitin 4; and ii) an additional arginyl residue at C-terminus of eryngitin 4, not retrieved in eryngitin 3. The 3D-models of eryngitins show slight differences at the N- and C-terminal regions. In particular, the positive electrostatic surface at C-terminal of eryngitin 4 is due to the additional arginyl residue not retrieved in eryngitin 3. This additional positive charge could interfere with the binding to the SRL (substrate) or with some ribosomal proteins (P-stalk structure), during substrate recognition.

Keywords

amino acid sequence; green mold; king trumpet mushroom; MALDI-ToF; ribotoxin-like proteins (RL-Ps); Sarcin-Ricin Loop

Subject

Biology and Life Sciences, Biochemistry and Molecular Biology

Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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