Toxicity and membrane perturbation properties of the ribotoxin-like protein Ageritin
| Autor: | Nicola Landi, Andrea Bosso, Angela Arciello, Erosantonio Lampitella, Antimo Di Maro, Elio Pizzo, Pompea Del Vecchio, Federica De Lise, Rosa Gaglione, Rosario Oliva, Luigi Petraccone, Sara Ragucci |
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| Přispěvatelé: | Lampitella, Erosantonio, Landi, Nicola, Oliva, Rosario, Gaglione, Rosa, Bosso, Andrea, De Lise, Federica, Ragucci, Sara, Arciello, Angela, Petraccone, Luigi, Pizzo, Elio, Del Vecchio, Pompea, Di Maro, Antimo, Lampitella, E., Landi, N., Oliva, R., Gaglione, R., Bosso, A., de Lise, F., Ragucci, S., Arciello, A., Petraccone, L., Pizzo, E., Del Vecchio, P., Di Maro, A. |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Protein family Cell Survival Antineoplastic Agents Calorimetry Cleavage (embryo) Biochemistry Cell Line Divalent Mice 03 medical and health sciences chemistry.chemical_compound Ribonucleases Neoplasms Agrocybe Protein biosynthesis Animals Molecular Biology chemistry.chemical_classification Bacteria 030102 biochemistry & molecular biology Basidiomycota Vesicle Cell Membrane Agrocybe aegerita General Medicine Mycotoxins Liposome Ribotoxin-like proteins Cholesterol 030104 developmental biology Membrane Ricin Membrane interaction chemistry RNA Ribosomal Protein Biosynthesis Liposomes Cancer cell Biophysics Ribosomes |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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