Melleatin, an antibiofilm multitasking protein with rRNA N-glycosylase and nuclease activity from Armillaria mellea fruiting bodies.

Autor: Hussain HZF; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, 81100 Caserta, Italy., Ragucci S; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, 81100 Caserta, Italy., Gentile MT; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, 81100 Caserta, Italy., Alberico L; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, 81100 Caserta, Italy., Landi N; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, 81100 Caserta, Italy; Institute of Crystallography, National Research Council, Via Vivaldi 43, 81100 Caserta, Italy., Bosso A; Department of Biology, University of Naples 'Federico II', Via Cinthia 26, 80126 Naples, Italy., Pizzo E; Department of Biology, University of Naples 'Federico II', Via Cinthia 26, 80126 Naples, Italy; Centro Servizi Metrologici e Tecnologici Avanzati (CeSMA), University of Naples 'Federico II', 80126 Naples, Italy., Saviano M; Institute of Crystallography, National Research Council, Via Vivaldi 43, 81100 Caserta, Italy., Pedone PV; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, 81100 Caserta, Italy., Citores L; Department of Biochemistry and Molecular Biology and Physiology, Faculty of Sciences, University of Valladolid, E-47011 Valladolid, Spain., Woodrow P; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, 81100 Caserta, Italy., Di Maro A; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, 81100 Caserta, Italy. Electronic address: antimo.dimaro@unicampania.it.
Jazyk: angličtina
Zdroj: International journal of biological macromolecules [Int J Biol Macromol] 2024 Dec 06; Vol. 286, pp. 138447. Date of Electronic Publication: 2024 Dec 06.
DOI: 10.1016/j.ijbiomac.2024.138447
Abstrakt: Several studies highlight the identification of some enzymes with additional abilities, especially those involved in metabolic pathways and/or host defence processes, classified as multitasking proteins. In this context, we report the characterization of melleatin (17.5-kDa), a multitasking enzyme isolated from Armillaria mellea fruiting bodies. Melleatin inhibits protein synthesis and displayed unexpected enzymatic action. Indeed, the structural characterization (primary structure and 3D model) showed that melleatin belongs to the His-Me finger endonucleases superfamily possessing a fold like the biofilm-dispersing nuclease NucB, the latter isolated from the marine Bacillus licheniformis. The enzymatic studies on melleatin showed that this enzyme is able to: i) inhibit protein synthesis in a rabbit reticulocyte lysate system (IC 50 value 16.48 ± 3.71 nM); ii) damage rabbit and Trichoderma harzianum ribosomes as a ribosome inactivating protein (β-fragment release after Endo's assay); and iii) hydrolyse DNA. Functionally, melleatin has antibiofilm action and antifungal activity towards T. harzianum and Botrytis cinerea affecting fungal ribosomes, while it does not exhibit cytotoxicity against different human cell lines, being unable to enter the cells. Overall, melleatin represents a novel multitasking protein that could be used as a biotechnological tool for its antibiofilm and antifungal activity or as a toxic component of biomedical bioconstructs.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 The Author(s). Published by Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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