Submit to Toxins Review for Toxins Propose a Special Issue

Journal Menu

Journal Browser

► Journal Browser

Toxic Proteins from Mushrooms: From Defence Roles to Biotechnological Tools for the Future

Print Special Issue Flyer
Special Issue Editors
Special Issue Information
Keywords
Published Papers

A special issue of Toxins (ISSN 2072-6651).

Deadline for manuscript submissions: closed (30 September 2023) | Viewed by 20162

Share This Special Issue

Special Issue Editors

Prof. Antimo Di Maro

E-Mail Website
Guest Editor

Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania ‘Luigi Vanvitelli’, Via Vivaldi 43, 81100 Caserta, Italy
Interests: protein purification; protein structure; ribosome-inactivating proteins (RIPs); ribotoxin-like proteins (RL-Ps); structure-function relationship

Dr. Sara Ragucci

E-Mail Website
Co-Guest Editor

Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania ‘Luigi Vanvitelli’, Via Vivaldi, 43-81100 Caserta, Italy
Interests: protein purification; protein characterization; enzyme activity; toxins; myoglobin; ribotoxin-like proteins; ribosome inactivating proteins; amino acid composition; mass spectrometry

Special Issue Information

Dear Colleagues,

Mushrooms are a group of macrofungi belonging to basidiomycetes and ascomycetes with fruiting bodies during the reproductive phase, which is necessary to produce spores, and aids in fungal propagation. Mushrooms fruiting bodies have always symbolised the "yin and yang", being a source of poisons, and at same time a reservoir of bioactive compounds with health benefits.

Mushrooms (edible and non-mushrooms) are a source of substances for biotechnological and medicinal applications. In addition, edible mushrooms are particularly renowned as functional food and are popular given their taste, aroma and nutritional values, being rich of antioxidants, β-glucans and metabolites with health benefits (e.g.: anti-diabetic, anti-cancerous, anti-obesity, immunomodulatory, hypocholesteremia, hepatoprotection and anti-aging).

Despite the knowledge acquired in mycology field, mushroom poisoning still represents a frequent cause of fatal accidents, mainly due to misidentification. Indeed, mushroom poisoning can cause both benign symptoms of generalized gastrointestinal upset and potentially devastating manifestations, which include liver failure, kidney failure, and neurologic sequelae, depending on the species, kind of toxin, and amount ingested. Among poisonous compounds retrieved in mushrooms, there are specific toxic proteins/peptides that promote toxic effects acting on different targets (e.g., ribosome-inactivating proteins and ribotoxin-like proteins damaging ribosomes; proteins with haemolytic effect; lectins able to destroy erythrocytes and cyclic peptides that are selective inhibitors of RNA polymerase II).

On the other hand, in the foreseeable future, these toxic polypeptides may become a possible tool for their use in the treatment of several human diseases or in plant biotechnology applications to attain resistance against pests/pathogens.

Therefore, this Special Issue aims to be a summary on toxic proteins/peptides from mushrooms and their potential applications in medicine and crop protection. A challenge for the future to turn this natural "poisons" in possible "magic bullets" with the potentiality to change the course of history on the plagues of society.

Prof. Antimo Di Maro
Dr. Sara Ragucci
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a double-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Toxins is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

bioactive peptides
biological activities
lectins
mushrooms
protein toxins
ribonucleases
ribotoxins
ribotoxin-like proteins
rRNA N-glycosylases
structure–function relationships

Published Papers (5 papers)

Download All Papers

Research

Jump to: Review

13 pages, 25432 KiB

Open AccessArticle

Effects of Bioinsecticidal Aegerolysin-Based Cytolytic Complexes on Non-Target Organisms

by Anastasija Panevska, Gordana Glavan, Anita Jemec Kokalj, Veronika Kukuljan, Tomaž Trobec, Monika Cecilija Žužek, Milka Vrecl, Damjana Drobne, Robert Frangež and Kristina Sepčić

Toxins 2021, 13(7), 457; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13070457 - 30 Jun 2021

Cited by 7 | Viewed by 2842

Abstract

Aegerolysin proteins ostreolysin A6 (OlyA6), pleurotolysin A2 (PlyA2) and erylysin A (EryA) produced by the mushroom genus Pleurotus bind strongly to an invertebrate-specific membrane sphingolipid, and together with a protein partner pleurotolysin B (PlyB), form transmembrane pore complexes. This pore formation is the basis for the selective insecticidal activity of aegerolysin/PlyB complexes against two economically important coleopteran pests: the Colorado potato beetle and the western corn rootworm. In this study, we evaluated the toxicities of these aegerolysin/PlyB complexes using feeding tests with two ecologically important non-target arthropod species: the woodlouse and the honey bee. The mammalian toxicity of the EryA/PlyB complex was also evaluated after intravenous administration to mice. None of the aegerolysin/PlyB complexes were toxic against woodlice, but OlyA6/PlyB and PlyA2/PlyB were toxic to honeybees, with 48 h mean lethal concentrations (LC₅₀) of 0.22 and 0.39 mg/mL, respectively, in their food. EryA/PlyB was also tested intravenously in mice up to 3 mg/kg body mass, without showing toxicity. With no toxicity seen for EryA/PlyB for environmentally beneficial arthropods and mammals at the tested concentrations, these EryA/PlyB complexes are of particular interest for development of new bioinsecticides for control of selected coleopteran pests. Full article

(This article belongs to the Special Issue Toxic Proteins from Mushrooms: From Defence Roles to Biotechnological Tools for the Future)

► Show Figures

Graphical abstract

16 pages, 2882 KiB

Open AccessArticle

Dissecting Out the Molecular Mechanism of Insecticidal Activity of Ostreolysin A6/Pleurotolysin B Complexes on Western Corn Rootworm

by Matej Milijaš Jotić, Anastasija Panevska, Ioan Iacovache, Rok Kostanjšek, Martina Mravinec, Matej Skočaj, Benoît Zuber, Ana Pavšič, Jaka Razinger, Špela Modic, Francesco Trenti, Graziano Guella and Kristina Sepčić

Toxins 2021, 13(7), 455; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13070455 - 29 Jun 2021

Cited by 12 | Viewed by 2984

Abstract

Ostreolysin A6 (OlyA6) is a protein produced by the oyster mushroom (Pleurotus ostreatus). It binds to membrane sphingomyelin/cholesterol domains, and together with its protein partner, pleurotolysin B (PlyB), it forms 13-meric transmembrane pore complexes. Further, OlyA6 binds 1000 times more strongly to the insect-specific membrane sphingolipid, ceramide phosphoethanolamine (CPE). In concert with PlyB, OlyA6 has potent and selective insecticidal activity against the western corn rootworm. We analysed the histological alterations of the midgut wall columnar epithelium of western corn rootworm larvae fed with OlyA6/PlyB, which showed vacuolisation of the cell cytoplasm, swelling of the apical cell surface into the gut lumen, and delamination of the basal lamina underlying the epithelium. Additionally, cryo-electron microscopy was used to explore the membrane interactions of the OlyA6/PlyB complex using lipid vesicles composed of artificial lipids containing CPE, and western corn rootworm brush border membrane vesicles. Multimeric transmembrane pores were formed in both vesicle preparations, similar to those described for sphingomyelin/cholesterol membranes. These results strongly suggest that the molecular mechanism of insecticidal action of OlyA6/PlyB arises from specific interactions of OlyA6 with CPE, and the consequent formation of transmembrane pores in the insect midgut. Full article

(This article belongs to the Special Issue Toxic Proteins from Mushrooms: From Defence Roles to Biotechnological Tools for the Future)

► Show Figures

Graphical abstract

Review

Jump to: Research

17 pages, 2962 KiB

Open AccessFeature PaperEditor’s ChoiceReview

Ribotoxic Proteins, Known as Inhibitors of Protein Synthesis, from Mushrooms and Other Fungi According to Endo’s Fragment Detection

by Nicola Landi, Hafiza Z. F. Hussain, Paolo V. Pedone, Sara Ragucci and Antimo Di Maro

Toxins 2022, 14(6), 403; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins14060403 - 13 Jun 2022

Cited by 11 | Viewed by 2749

Abstract

rRNA N-glycosylases (EC 3.2.2.22) remove a specific adenine (A₄₃₂₄, rat 28S rRNA) in the sarcin ricin loop (SRL) involved into ribosome interaction with elongation factors, causing the inhibition of translation, for which they are known as plant ‘ribosome inactivating proteins’ (RIPs). However, protein synthesis inactivation could be the result of other enzymes, which often have rRNA as the target. In this scenario, Endo’s assay is the most used method to detect the enzymes that are able to hydrolyze a phosphodiester bond or cleave a single N-glycosidic bond (rRNA N-glycosylases). Indeed, the detection of a diagnostic fragment from rRNA after enzymatic action, with or without acid aniline, allows one to discriminate between the N-glycosylases or hydrolases, which release the β-fragment after acid aniline treatment or α-fragment without acid aniline treatment, respectively. This assay is of great importance in the mushroom kingdom, considering the presence of enzymes that are able to hydrolyze phosphodiester bonds (e.g., ribonucleases, ribotoxins and ribotoxin-like proteins) or to remove a specific adenine (rRNA N-glycosylases). Thus, here we used the β-fragment experimentally detected by Endo’s assay as a hallmark to revise the literature available on enzymes from mushrooms and other fungi, whose action consists of protein biosynthesis inhibition. Full article

(This article belongs to the Special Issue Toxic Proteins from Mushrooms: From Defence Roles to Biotechnological Tools for the Future)

► Show Figures

Graphical abstract

19 pages, 1974 KiB

Open AccessReview

An Updated Review of Bioactive Peptides from Mushrooms in a Well-Defined Molecular Weight Range

by Nicola Landi, Angela Clemente, Paolo V. Pedone, Sara Ragucci and Antimo Di Maro

Toxins 2022, 14(2), 84; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins14020084 - 22 Jan 2022

Cited by 20 | Viewed by 6040

Abstract

Here, we report the current status of the bioactive peptides isolated and characterized from mushrooms during the last 20 years, considering ‘peptide’ a succession from to 2 to 100 amino acid residues. According to this accepted biochemical definition, we adopt ~10 kDa as the upper limit of molecular weight for a peptide. In light of this, a careful revision of data reported in the literature was carried out. The search revealed that in the works describing the characterization of bioactive peptides from mushrooms, not all the peptides have been correctly classified according to their molecular weight, considering that some fungal proteins (>10 kDa MW) have been improperly classified as ‘peptides’. Moreover, the biological action of each of these peptides, the principles of their isolation as well as the source/mushroom species were summarized. Finally, this review highlighted that these peptides possess antihypertensive, antifungal, antibiotic and antimicrobial, anticancer, antiviral, antioxidant and ACE inhibitory properties. Full article

(This article belongs to the Special Issue Toxic Proteins from Mushrooms: From Defence Roles to Biotechnological Tools for the Future)

► Show Figures

Graphical abstract

17 pages, 20981 KiB

Open AccessReview

Ageritin from Pioppino Mushroom: The Prototype of Ribotoxin-Like Proteins, a Novel Family of Specific Ribonucleases in Edible Mushrooms

by Sara Ragucci, Nicola Landi, Rosita Russo, Mariangela Valletta, Paolo Vincenzo Pedone, Angela Chambery and Antimo Di Maro

Toxins 2021, 13(4), 263; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13040263 - 07 Apr 2021

Cited by 21 | Viewed by 3647

Abstract

Ageritin is a specific ribonuclease, extracted from the edible mushroom Cyclocybe aegerita (synonym Agrocybe aegerita), which cleaves a single phosphodiester bond located within the universally conserved alpha-sarcin loop (SRL) of 23–28S rRNAs. This cleavage leads to the inhibition of protein biosynthesis, followed by cellular death through apoptosis. The structural and enzymatic properties show that Ageritin is the prototype of a novel specific ribonucleases family named ‘ribotoxin-like proteins’, recently found in fruiting bodies of other edible basidiomycetes mushrooms (e.g., Ostreatin from Pleurotus ostreatus, Edulitins from Boletus edulis, and Gambositin from Calocybe gambosa). Although the putative role of this toxin, present in high amount in fruiting body (>2.5 mg per 100 g) of C. aegerita, is unknown, its antifungal and insecticidal actions strongly support a role in defense mechanisms. Thus, in this review, we focus on structural, biological, antipathogenic, and enzymatic characteristics of this ribotoxin-like protein. We also highlight its biological relevance and potential biotechnological applications in agriculture as a bio-pesticide and in biomedicine as a therapeutic and diagnostic agent. Full article

(This article belongs to the Special Issue Toxic Proteins from Mushrooms: From Defence Roles to Biotechnological Tools for the Future)

► Show Figures