Toxicity and membrane perturbation properties of the ribotoxin-like protein Ageritin
© The Author(s) 2021. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved..
Ageritin is the prototype of a new ribotoxin-like protein family, which has been recently identified also in basidiomycetes. The protein exhibits specific RNase activity through the cleavage of a single phosphodiester bond located at sarcin/ricin loop of the large rRNA, thus inhibiting protein biosynthesis at early stages. Conversely to other ribotoxins, its activity requires the presence of divalent cations. In the present study, we report the activity of Ageritin on both prokaryotic and eukaryotic cells showing that the protein has a prominent effect on cancer cells viability and no effects on eukaryotic and bacterial cells. In order to rationalize these findings, the ability of the protein to interact with various liposomes mimicking normal, cancer and bacterial cell membranes was explored. The collected results indicate that Ageritin can interact with DPPC/DPPS/Chol vesicles, used as a model of cancer cell membranes, and with DPPC/DPPG vesicles, used as a model of bacterial cell membranes, suggesting a selective interaction with anionic lipids. However, a different perturbation of the two model membranes, mediated by cholesterol redistribution, was observed and this might be at the basis of Ageritin selective toxicity towards cancer cells.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2021 |
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| Erschienen: |
2021 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:170 |
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| Enthalten in: |
Journal of biochemistry - 170(2021), 4 vom: 04. Dez., Seite 473-482 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Lampitella, Erosantonio [VerfasserIn] |
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| Links: |
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| Themen: |
97C5T2UQ7J |
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| Anmerkungen: |
Date Completed 27.12.2021 Date Revised 27.12.2021 published: Print Citation Status MEDLINE |
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| doi: |
10.1093/jb/mvab062 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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NLM325445672 |
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| 245 | 1 | 0 | |a Toxicity and membrane perturbation properties of the ribotoxin-like protein Ageritin |
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| 500 | |a Citation Status MEDLINE | ||
| 520 | |a © The Author(s) 2021. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved. | ||
| 520 | |a Ageritin is the prototype of a new ribotoxin-like protein family, which has been recently identified also in basidiomycetes. The protein exhibits specific RNase activity through the cleavage of a single phosphodiester bond located at sarcin/ricin loop of the large rRNA, thus inhibiting protein biosynthesis at early stages. Conversely to other ribotoxins, its activity requires the presence of divalent cations. In the present study, we report the activity of Ageritin on both prokaryotic and eukaryotic cells showing that the protein has a prominent effect on cancer cells viability and no effects on eukaryotic and bacterial cells. In order to rationalize these findings, the ability of the protein to interact with various liposomes mimicking normal, cancer and bacterial cell membranes was explored. The collected results indicate that Ageritin can interact with DPPC/DPPS/Chol vesicles, used as a model of cancer cell membranes, and with DPPC/DPPG vesicles, used as a model of bacterial cell membranes, suggesting a selective interaction with anionic lipids. However, a different perturbation of the two model membranes, mediated by cholesterol redistribution, was observed and this might be at the basis of Ageritin selective toxicity towards cancer cells | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Agrocybe aegerita | |
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| 700 | 1 | |a Bosso, Andrea |e verfasserin |4 aut | |
| 700 | 1 | |a De Lise, Federica |e verfasserin |4 aut | |
| 700 | 1 | |a Ragucci, Sara |e verfasserin |4 aut | |
| 700 | 1 | |a Arciello, Angela |e verfasserin |4 aut | |
| 700 | 1 | |a Petraccone, Luigi |e verfasserin |4 aut | |
| 700 | 1 | |a Pizzo, Elio |e verfasserin |4 aut | |
| 700 | 1 | |a Del Vecchio, Pompea |e verfasserin |4 aut | |
| 700 | 1 | |a Di Maro, Antimo |e verfasserin |4 aut | |
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