Abstract
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.
Highlights
One of the main efforts of virologists and molecular biologists is the search for antivirals that can help in the fight against viruses causing diseases in animals and especially in humans
Regarding ribosome-inactivating proteins (RIPs), it is worth noting the fact that one of the first Ribosome-inactivating proteins (RIPs) to be purified was pokeweed antiviral protein (PAP) and many RIPs have been purified as protein synthesis inhibitors, many others have been isolated as powerful antivirals
RIPs have been studied as potent inhibitors of protein synthesis that can be used for the construction of immunotoxins [4]
Summary
One of the main efforts of virologists and molecular biologists is the search for antivirals that can help in the fight against viruses causing diseases in animals and especially in humans. RIPs have initially been studied as a family of proteins widely distributed among angiosperms they have been found in other taxons [6,7] They irreversibly inactivate ribosomes inhibiting protein synthesis and causing cell death [6,7]. 4324 and its ribose in the 60S subunit of rat ribosomes [11] or the equivalent one in sensitive ribosomes from other organisms [12] This adenine is located in the sarcin-ricin loop (SRL) that is crucial for anchoring the elongation factors EFG and EF2 on the ribosome during mRNA-tRNA translocation in prokaryotes and eukaryotes, respectively.
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