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.
Interests: amino acids; antimicrobial peptides; myoglobin; protein purification; ribosome inactivating proteins; ribotoxin-like proteins; sequence analysis
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
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 papers will be 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.
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- bioactive peptides
- biological activities
- protein toxins
- ribotoxin-like proteins
- rRNA N-glycosylases
- structure–function relationships
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.