Special Issue "Biological Activities of Ribosome-Inactivating Proteins"
A special issue of Toxins (ISSN 2072-6651).
Deadline for manuscript submissions: closed (31 July 2022) | Viewed by 8924
Interests: ribosome-inactivating proteins (RIPs); immunotoxins; protein synthesis inhibition; ribotoxins; structure–activity relationship
Interests: ribosome-inactivating proteins (RIPs); immunotoxins; protein synthesis inhibition; ribotoxins; protein translocation; intracellular transport; apoptosis
Ribosome-inactivating proteins (RIPs) are rRNA N-glycosylases (EC 184.108.40.206) isolated mainly from plants and some bacteria 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, being the most relevant their polynucleotide:adenosine glycosylase activity on all kinds of nucleic acids. RIPs have been classified into two types depending on the presence (type 2 RIPs) or the 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 into cells and display toxicity to cells and animals.
The exact biological role that RIPs play remains unknown, but it is thought to represent a defense mechanism of a plant 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 a component 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, as well as on the elucidation of the structure-activity relationships of these proteins.
Prof. Dr. José Miguel Ferreras
Prof. Dr. Lucía Citores
Manuscript Submission Information
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- ribosome-inactivating protein (RIP)
- rRNA N-glycosylase