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

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

Deadline for manuscript submissions: 31 March 2022.

Special Issue Editor

Prof. Antimo Di Maro
E-Mail Website1 Website2
Guest Editor
Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania "Luigi Vanvitelli", I-81100 Caserta, Italy
Interests: amino acids; antimicrobial peptides; myoglobin; protein purification; ribosome inactivating proteins; ribotoxin-like proteins; sequence analysis

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
Guest Editor

Manuscript Submission Information

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Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2400 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 (3 papers)

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Research

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Article
Effects of Bioinsecticidal Aegerolysin-Based Cytolytic Complexes on Non-Target Organisms
Toxins 2021, 13(7), 457; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13070457 - 30 Jun 2021
Viewed by 796
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 [...] Read more.
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
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Article
Dissecting Out the Molecular Mechanism of Insecticidal Activity of Ostreolysin A6/Pleurotolysin B Complexes on Western Corn Rootworm
Toxins 2021, 13(7), 455; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13070455 - 29 Jun 2021
Viewed by 764
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 [...] Read more.
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
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Review

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Review
Ageritin from Pioppino Mushroom: The Prototype of Ribotoxin-Like Proteins, a Novel Family of Specific Ribonucleases in Edible Mushrooms
Toxins 2021, 13(4), 263; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13040263 - 07 Apr 2021
Cited by 2 | Viewed by 653
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 [...] Read more.
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
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Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Title: Ageritin from Agrocybe aegerita: the prototype of ribotoxin-like proteins, a novel family of specific ribonucleases in edible mushrooms
Authors: Ragucci et al.
Affiliation: Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania "Luigi Vanvitelli", I-81100 Caserta, Italy
Abstract: Ageritin is a specific ribonuclease, extracted from the edible mushroom Agrocybe aegerita, that 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 A. aegerita is unknown, recent studies showing the antifungal and insecticidal action of Ageritin support its involvement in defense mechanisms. Thus, in this review, we focus on both structural and enzymatic characteristics and the biological and antipathogenic actions of this ribotoxin-like protein in light of its biological relevance and potential biotechnological applications in agriculture as bio-pesticide and in medicine as therapeutic and diagnostic agent.

Title: Effects of bioinsecticidal aegerolysin-based cytolytic complexes on non-target organisms
Authors: Anastasija Panevska1; Gordana Glavan1; Anita Jemec Kokalj1; Veronika Kukuljan1,2; Tomaž Trobec3; Monika Cecilija Žužek3; Milka Vrecl3; Damjana Drobne1; Robert Frangež3; Kristina Sepčić1
Affiliation: 1Department of Biology, Biotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, 1000 Ljubljana, Slovenia 2Department of Biotechnology, University of Rijeka, Radmile Matejčić 2, 51000 Rijeka, Croatia 3Institute of Preclinical Sciences, Veterinary Faculty, University of Ljubljana, Gerbičeva 60, 1000 Ljubljana, Slovenia
Abstract: Aegerolysin proteins produced by the mushroom genus Pleurotus bind strongly to an insect-specific membrane sphingolipid and, together with a larger protein partner pleurotolysin B (PlyB) co-produced by the same organism, form transmembrane pore complexes. This pore formation is the basis for the potent and selective insecticidal activity of aegerolysin/PlyB complexes against two economically important coleopteran pests: the Colorado potato beetle and the western corn rootworm. In this work, we evaluated the safety of three selected aegerolysin/PlyB complexes by investigating their toxicity in feeding test against two ecologically important arthropod species: the woodlouse and the honeybee. The toxicity of the selected aegerolysin, erylysin A, in complex with PlyB was also evaluated after intravenous administration to mice. None of the aegerolysin/PlyB complexes tested were toxic against woodlice, but two of them were moderately toxic to honeybees with 7-day LC50 values of 0.22 and 0.39 mg/mL food. The erylysin A/PlyB complexes were not toxic to mice even at very high doses (3 mg/kg body mass). Considering their non-toxicity to mammals and environmentally beneficial arthropods, the erylysin A/PlyB complexes are of particular interest for the subsequent development of new bioinsecticides for specific control of Colorado potato beetle and western corn rootworm.

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