Biological Activities of Ribosome Inactivating Proteins II
A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Plant Toxins".
Deadline for manuscript submissions: 15 April 2025 | Viewed by 8848
Special Issue Editors
Interests: ribosome-inactivating proteins (RIPs); immunotoxins; protein synthesis inhibition; ribotoxins; structure–activity relationship
Special Issues, Collections and Topics in MDPI journals
Interests: ribosome-inactivating proteins (RIPs); immunotoxins; protein synthesis inhibition; ribotoxins; protein translocation; intracellular transport; apoptosis
Special Issues, Collections and Topics in MDPI journals
Interests: plant toxins; ribosome-inactivating proteins (RIPs); ribotoxins; immunotoxins; plant fungal pathogenesis; antifun-gal proteins
Special Issue Information
Dear Colleagues,
Ribosome-inactivating proteins (RIPs) are rRNA N-glycosylases (EC 3.2.2.22) that specifically catalyze the hydrolysis of the second N-glycosidic bond from the GAGA tetraloop located in the sarcin–ricin loop (SRL) of the large ribosomal RNA. Because the SRL is crucial for anchoring the elongation factors on the ribosome, depurination causes the irreversible inactivation of ribosomes. In addition, RIPs usually display other enzymatic activities, the most relevant being their adenine polynucleotide glycosylase activity on all kinds of nucleic acids. RIPs have been classified into two types depending on the presence (type 2 RIPs) or absence (type 1 RIPs) of a lectin chain (B chain). The presence of the B chain may turn type 2 RIPs into powerful toxins, such as ricin or abrin. Regardless, despite the absence of the B chain, type 1 RIPs at higher concentrations are also able to enter cells and display toxicity to cells and animals.
Most RIPs have been isolated from angiosperm plants, while one has been obtained from algae and a few from bacteria or fungi.
The exact biological role played by RIPs remains unknown, but it is thought to represent a defense mechanism of plants against pathogens and predators.
As a consequence of their enzymatic action, RIPs display several biological activities, including antiviral, antibacterial, antifungal, antifeedant, and antiproliferative activities, which may be relevant to their functions and biotechnological applications.
The most promising applications of RIPs in experimental medicine, especially in anticancer therapy, are related to their use as components of immunotoxins, in which the RIP is 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 focus of this Special Issue of Toxins will be on the biological activities of RIPs that may be relevant to their biological functions and biotechnological applications, and on the elucidation of the structure–activity relationships of these proteins.
Prof. Dr. José Miguel Ferreras
Prof. Dr. Lucía Citores
Prof. Dr. Rosario Iglesias
Guest Editors
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Keywords
- antifeedant
- antifungal
- antitumoral
- antiviral
- apoptosis
- immunotoxin
- ribosome-inactivating protein (RIP)
- rRNA N-glycosylase
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