Biological Activities of Ribosome-Inactivating Proteins
Ribosome-inactivating proteins (RIPs) are rRNA N-glycosylases isolated mainly from plants that catalyze the hydrolysis of the N-glycosidic bond of a specific adenosine in the sarcin-ricin loop (SRL) of the major ribosomal RNA. Because the SRL is crucial for anchoring translation elongation factors,...
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MDPI - Multidisciplinary Digital Publishing Institute
2023
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| גישה מקוונת: | ONIX_20230405_9783036568225_138 |
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| _version_ | 1869518132071104512 |
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| collection | Directory of Open Access Books |
| description | Ribosome-inactivating proteins (RIPs) are rRNA N-glycosylases isolated mainly from plants that catalyze the hydrolysis of the N-glycosidic bond of a specific adenosine in the sarcin-ricin loop (SRL) of the major ribosomal RNA. Because the SRL is crucial for anchoring translation elongation factors, RIPs cause inactivation of ribosomes. They have been classified into two types based on the presence (type 2 RIPs) or absence (type 1 RIPs) of a lectin chain that can turn type 2 RIPs into potent toxins, such as ricin or abrin. The biological role of these proteins is unknown, but they are thought to be a defense mechanism of some plants against pathogens and predators. Because of their enzymatic action, RIPs show several biological activities, among which antiviral, antifungal and antiproliferative activities stand out. The most promising application of RIPs is their use as a component of immunotoxins, in which RIPs are linked to antibodies that mediate their binding and internalization by malignant cells. In agriculture, RIPs have been shown to increase resistance against viruses, fungi and insects in transgenic plants. The studies collected in this book provide the reader with an overview of the most current and interesting lines of research in the field of RIPs and their applications in medicine and agriculture. Thus, the reprint includes the isolation and biological properties of some new RIPs, both type 1 and type 2, the mechanisms of toxicity of previously described RIPs and two extensive reviews, one on the antiviral activity of RIPs and the other on the strategies used to improve their pharmacological properties. |
| format | Online |
| id | doab-20.500.12854ir-98859 |
| institution | Directory of Open Access Books |
| language | eng |
| publishDate | 2023 |
| publishDateRange | 2023 |
| publishDateSort | 2023 |
| publisher | MDPI - Multidisciplinary Digital Publishing Institute |
| publisherStr | MDPI - Multidisciplinary Digital Publishing Institute |
| record_format | ojs |
| spelling | doab-20.500.12854ir-988592024-03-28T03:33:21Z Biological Activities of Ribosome-Inactivating Proteins Ferreras, José Miguel Citores, Lucía ribosome inactivating protein therapeutic applications immunotoxin anti-HIV anti-cancer antiviral proteins ribosome inactivating proteins Phytolacca dioica L. protein purification tobacco necrosis virus Adenia apoptosis kirkiin lectins neuroblastoma ribosome-inactivating proteins ricin toxic enzymes adenine polynucleotide glycosylase antiviral therapy human virus ribosome-inactivating protein (RIP) rRNA glycosylase (EC 3.2.2.22) virus-resistant transgenic plant (VRTP) clathrin dynamin ebulin endocytosis intracellular transport lectin rRNA N-glycosylase ribosome-inactivating protein plant toxin type I RIP rRNA glycosylase activity (EC 3.2.2.22) protein isolation protein sequencing mass spectrometry antifungal activity agretti cytotoxicity edible plants rRNA N-glycosylases anticancer agents galactose nanoLC–tandem mass spectrometry (nLC-MS/MS) protein synthesis (inhibition) sugar binding abrin intranasal lungs alveolar epithelial type II cells neutrophils alveolar–capillary barrier junction proteins glycocalyx Curcin Curcin C osteosarcoma U20S cells n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences Ribosome-inactivating proteins (RIPs) are rRNA N-glycosylases isolated mainly from plants that catalyze the hydrolysis of the N-glycosidic bond of a specific adenosine in the sarcin-ricin loop (SRL) of the major ribosomal RNA. Because the SRL is crucial for anchoring translation elongation factors, RIPs cause inactivation of ribosomes. They have been classified into two types based on the presence (type 2 RIPs) or absence (type 1 RIPs) of a lectin chain that can turn type 2 RIPs into potent toxins, such as ricin or abrin. The biological role of these proteins is unknown, but they are thought to be a defense mechanism of some plants against pathogens and predators. Because of their enzymatic action, RIPs show several biological activities, among which antiviral, antifungal and antiproliferative activities stand out. The most promising application of RIPs is their use as a component of immunotoxins, in which RIPs are linked to antibodies that mediate their binding and internalization by malignant cells. In agriculture, RIPs have been shown to increase resistance against viruses, fungi and insects in transgenic plants. The studies collected in this book provide the reader with an overview of the most current and interesting lines of research in the field of RIPs and their applications in medicine and agriculture. Thus, the reprint includes the isolation and biological properties of some new RIPs, both type 1 and type 2, the mechanisms of toxicity of previously described RIPs and two extensive reviews, one on the antiviral activity of RIPs and the other on the strategies used to improve their pharmacological properties. 2023-04-05T12:54:55Z 2023-04-05T12:54:55Z 2023 book ONIX_20230405_9783036568225_138 9783036568225 9783036568232 https://directory.doabooks.org/handle/20.500.12854/98859 eng application/octet-stream Attribution 4.0 International https://mdpi.com/books/pdfview/book/6912 https://mdpi.com/books/pdfview/book/6912 MDPI - Multidisciplinary Digital Publishing Institute 10.3390/books978-3-0365-6823-2 10.3390/books978-3-0365-6823-2 46cabcaa-dd94-4bfe-87b4-55023c1b36d0 9783036568225 9783036568232 196 Basel open access |
| spellingShingle | ribosome inactivating protein therapeutic applications immunotoxin anti-HIV anti-cancer antiviral proteins ribosome inactivating proteins Phytolacca dioica L. protein purification tobacco necrosis virus Adenia apoptosis kirkiin lectins neuroblastoma ribosome-inactivating proteins ricin toxic enzymes adenine polynucleotide glycosylase antiviral therapy human virus ribosome-inactivating protein (RIP) rRNA glycosylase (EC 3.2.2.22) virus-resistant transgenic plant (VRTP) clathrin dynamin ebulin endocytosis intracellular transport lectin rRNA N-glycosylase ribosome-inactivating protein plant toxin type I RIP rRNA glycosylase activity (EC 3.2.2.22) protein isolation protein sequencing mass spectrometry antifungal activity agretti cytotoxicity edible plants rRNA N-glycosylases anticancer agents galactose nanoLC–tandem mass spectrometry (nLC-MS/MS) protein synthesis (inhibition) sugar binding abrin intranasal lungs alveolar epithelial type II cells neutrophils alveolar–capillary barrier junction proteins glycocalyx Curcin Curcin C osteosarcoma U20S cells n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences Biological Activities of Ribosome-Inactivating Proteins |
| title | Biological Activities of Ribosome-Inactivating Proteins |
| title_full | Biological Activities of Ribosome-Inactivating Proteins |
| title_fullStr | Biological Activities of Ribosome-Inactivating Proteins |
| title_full_unstemmed | Biological Activities of Ribosome-Inactivating Proteins |
| title_short | Biological Activities of Ribosome-Inactivating Proteins |
| title_sort | biological activities of ribosome inactivating proteins |
| topic | ribosome inactivating protein therapeutic applications immunotoxin anti-HIV anti-cancer antiviral proteins ribosome inactivating proteins Phytolacca dioica L. protein purification tobacco necrosis virus Adenia apoptosis kirkiin lectins neuroblastoma ribosome-inactivating proteins ricin toxic enzymes adenine polynucleotide glycosylase antiviral therapy human virus ribosome-inactivating protein (RIP) rRNA glycosylase (EC 3.2.2.22) virus-resistant transgenic plant (VRTP) clathrin dynamin ebulin endocytosis intracellular transport lectin rRNA N-glycosylase ribosome-inactivating protein plant toxin type I RIP rRNA glycosylase activity (EC 3.2.2.22) protein isolation protein sequencing mass spectrometry antifungal activity agretti cytotoxicity edible plants rRNA N-glycosylases anticancer agents galactose nanoLC–tandem mass spectrometry (nLC-MS/MS) protein synthesis (inhibition) sugar binding abrin intranasal lungs alveolar epithelial type II cells neutrophils alveolar–capillary barrier junction proteins glycocalyx Curcin Curcin C osteosarcoma U20S cells n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences |
| topic_facet | ribosome inactivating protein therapeutic applications immunotoxin anti-HIV anti-cancer antiviral proteins ribosome inactivating proteins Phytolacca dioica L. protein purification tobacco necrosis virus Adenia apoptosis kirkiin lectins neuroblastoma ribosome-inactivating proteins ricin toxic enzymes adenine polynucleotide glycosylase antiviral therapy human virus ribosome-inactivating protein (RIP) rRNA glycosylase (EC 3.2.2.22) virus-resistant transgenic plant (VRTP) clathrin dynamin ebulin endocytosis intracellular transport lectin rRNA N-glycosylase ribosome-inactivating protein plant toxin type I RIP rRNA glycosylase activity (EC 3.2.2.22) protein isolation protein sequencing mass spectrometry antifungal activity agretti cytotoxicity edible plants rRNA N-glycosylases anticancer agents galactose nanoLC–tandem mass spectrometry (nLC-MS/MS) protein synthesis (inhibition) sugar binding abrin intranasal lungs alveolar epithelial type II cells neutrophils alveolar–capillary barrier junction proteins glycocalyx Curcin Curcin C osteosarcoma U20S cells n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences |
| url | ONIX_20230405_9783036568225_138 |