Isolation, Characterization and Biological Action of Type-1 Ribosome-Inactivating Proteins from Tissues of <i>Salsola soda</i> L.
Ribosome-inactivating proteins (RIPs) are known as RNA N-glycosylases. They depurinate the major rRNA, damaging ribosomes and inhibiting protein synthesis. Here, new single-chain (type-1) RIPs named sodins were isolated from the seeds (five proteins), edible leaves (one protein) and roots (one prote...
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2022-08-01
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author | Nicola Landi Sara Ragucci Lucía Citores Angela Clemente Hafiza Z. F. Hussain Rosario Iglesias José M. Ferreras Antimo Di Maro |
author_facet | Nicola Landi Sara Ragucci Lucía Citores Angela Clemente Hafiza Z. F. Hussain Rosario Iglesias José M. Ferreras Antimo Di Maro |
author_sort | Nicola Landi |
collection | DOAJ |
description | Ribosome-inactivating proteins (RIPs) are known as RNA N-glycosylases. They depurinate the major rRNA, damaging ribosomes and inhibiting protein synthesis. Here, new single-chain (type-1) RIPs named sodins were isolated from the seeds (five proteins), edible leaves (one protein) and roots (one protein) of <i>Salsola soda</i> L. Sodins are able to release Endo’s fragment when incubated with rabbit and yeast ribosomes and inhibit protein synthesis in cell-free systems (IC<sub>50</sub> = 4.83–79.31 pM). In addition, sodin 5, the major form isolated from seeds, as well as sodin eL and sodin R, isolated from edible leaves and roots, respectively, display polynucleotide:adenosine glycosylase activity and are cytotoxic towards the Hela and COLO 320 cell lines (IC<sub>50</sub> = 0.41–1200 nM), inducing apoptosis. The further characterization of sodin 5 reveals that this enzyme shows a secondary structure similar to other type-1 RIPs and a higher melting temperature (Tm = 76.03 ± 0.30 °C) and is non-glycosylated, as other sodins are. Finally, we proved that sodin 5 possesses antifungal activity against <i>Penicillium digitatum</i>. |
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spelling | doaj.art-e73b7457c7ec4a5c8d63679c79a8745e2023-12-03T14:35:40ZengMDPI AGToxins2072-66512022-08-0114856610.3390/toxins14080566Isolation, Characterization and Biological Action of Type-1 Ribosome-Inactivating Proteins from Tissues of <i>Salsola soda</i> L.Nicola Landi0Sara Ragucci1Lucía Citores2Angela Clemente3Hafiza Z. F. Hussain4Rosario Iglesias5José M. Ferreras6Antimo Di Maro7Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania Luigi Vanvitelli, Via Vivaldi 43, 81100 Caserta, ItalyDepartment of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania Luigi Vanvitelli, Via Vivaldi 43, 81100 Caserta, ItalyDepartment of Biochemistry and Molecular Biology and Physiology, Faculty of Sciences, University of Valladolid, E-47011 Valladolid, SpainDepartment of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania Luigi Vanvitelli, Via Vivaldi 43, 81100 Caserta, ItalyDepartment of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania Luigi Vanvitelli, Via Vivaldi 43, 81100 Caserta, ItalyDepartment of Biochemistry and Molecular Biology and Physiology, Faculty of Sciences, University of Valladolid, E-47011 Valladolid, SpainDepartment of Biochemistry and Molecular Biology and Physiology, Faculty of Sciences, University of Valladolid, E-47011 Valladolid, SpainDepartment of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania Luigi Vanvitelli, Via Vivaldi 43, 81100 Caserta, ItalyRibosome-inactivating proteins (RIPs) are known as RNA N-glycosylases. They depurinate the major rRNA, damaging ribosomes and inhibiting protein synthesis. Here, new single-chain (type-1) RIPs named sodins were isolated from the seeds (five proteins), edible leaves (one protein) and roots (one protein) of <i>Salsola soda</i> L. Sodins are able to release Endo’s fragment when incubated with rabbit and yeast ribosomes and inhibit protein synthesis in cell-free systems (IC<sub>50</sub> = 4.83–79.31 pM). In addition, sodin 5, the major form isolated from seeds, as well as sodin eL and sodin R, isolated from edible leaves and roots, respectively, display polynucleotide:adenosine glycosylase activity and are cytotoxic towards the Hela and COLO 320 cell lines (IC<sub>50</sub> = 0.41–1200 nM), inducing apoptosis. The further characterization of sodin 5 reveals that this enzyme shows a secondary structure similar to other type-1 RIPs and a higher melting temperature (Tm = 76.03 ± 0.30 °C) and is non-glycosylated, as other sodins are. Finally, we proved that sodin 5 possesses antifungal activity against <i>Penicillium digitatum</i>.https://www.mdpi.com/2072-6651/14/8/566antifungal activityagretticytotoxicityedible plantsprotein purificationrRNA N-glycosylases |
spellingShingle | Nicola Landi Sara Ragucci Lucía Citores Angela Clemente Hafiza Z. F. Hussain Rosario Iglesias José M. Ferreras Antimo Di Maro Isolation, Characterization and Biological Action of Type-1 Ribosome-Inactivating Proteins from Tissues of <i>Salsola soda</i> L. Toxins antifungal activity agretti cytotoxicity edible plants protein purification rRNA N-glycosylases |
title | Isolation, Characterization and Biological Action of Type-1 Ribosome-Inactivating Proteins from Tissues of <i>Salsola soda</i> L. |
title_full | Isolation, Characterization and Biological Action of Type-1 Ribosome-Inactivating Proteins from Tissues of <i>Salsola soda</i> L. |
title_fullStr | Isolation, Characterization and Biological Action of Type-1 Ribosome-Inactivating Proteins from Tissues of <i>Salsola soda</i> L. |
title_full_unstemmed | Isolation, Characterization and Biological Action of Type-1 Ribosome-Inactivating Proteins from Tissues of <i>Salsola soda</i> L. |
title_short | Isolation, Characterization and Biological Action of Type-1 Ribosome-Inactivating Proteins from Tissues of <i>Salsola soda</i> L. |
title_sort | isolation characterization and biological action of type 1 ribosome inactivating proteins from tissues of i salsola soda i l |
topic | antifungal activity agretti cytotoxicity edible plants protein purification rRNA N-glycosylases |
url | https://www.mdpi.com/2072-6651/14/8/566 |
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