Journal
TOXINS
Volume 13, Issue 2, Pages -Publisher
MDPI
DOI: 10.3390/toxins13020080
Keywords
adenine polynucleotide glycosylase; antiviral therapy; human virus; immunotoxin; ribosome-inactivating protein (RIP); rRNA glycosylase (EC 3; 2; 2; 22); virus-resistant transgenic plant (VRTP)
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Funding
- Consejeria de Educacion (Junta de Castilla y Leon) [VA033G19]
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Ribosome-inactivating proteins (RIPs) are enzymes from plants that inhibit protein synthesis and have been studied for decades for their antiviral properties. With the challenges posed by new viruses and difficult-to-treat viral infections, interest in RIPs is increasing. Moreover, the need to control crop diseases without using harmful phytosanitary products has led to RIPs being explored as promising tools for developing virus-resistant transgenic plants.
Ribosome-inactivating proteins (RIPs) are rRNA N-glycosylases from plants (EC 3.2.2.22) that inactivate ribosomes thus inhibiting protein synthesis. The antiviral properties of RIPs have been investigated for more than four decades. However, interest in these proteins is rising due to the emergence of infectious diseases caused by new viruses and the difficulty in treating viral infections. On the other hand, there is a growing need to control crop diseases without resorting to the use of phytosanitary products which are very harmful to the environment and in this respect, RIPs have been shown as a promising tool that can be used to obtain transgenic plants resistant to viruses. The way in which RIPs exert their antiviral effect continues to be the subject of intense research and several mechanisms of action have been proposed. The purpose of this review is to examine the research studies that deal with this matter, placing special emphasis on the most recent findings.
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