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Abstract
This review provides a historical overview of the research on plant ribosome-inactivating proteins (RIPs), starting from the first studies at the end of eighteenth century involving the purification of abrin and ricin, as well as the immunological experiments of Paul Erlich. Interest in these plant toxins was revived in 1970 by the observation of their anticancer activity, which has given rise to a large amount of research contributing to the development of various scientific fields. Biochemistry analyses succeeded in identifying the enzymatic activity of RIPs and allowed for a better understanding of the ribosomal machinery. Studies on RIP/cell interactions were able to detail the endocytosis and intracellular routing of ricin, thus increasing our knowledge of how cells handle exogenous proteins. The identification of new RIPs and the finding that most RIPs are single-chain polypeptides, together with their genetic sequencing, has aided in the development of new phylogenetic theories. Overall, the biological properties of these proteins, including their abortifacient, anticancer, antiviral and neurotoxic activities, suggest that RIPs could be utilized in agriculture and in many biomedical fields, including clinical drug development.
Highlights
This review provides a historical overview of the research on plant ribosome-inactivating proteins (RIPs), starting from the first studies at the end of eighteenth century involving the purification of abrin and ricin, as well as the immunological experiments of Paul Erlich
These researchers clarified that both ricin and abrin have a heterodimeric structure consisting of two polypeptides: an A chain with toxic activity and a B chain with the properties of a galactose-specific lectin linked by a disulphide bond [17,18]
Based on an updated list of plant RIPs, the following statements appear clear: (i) they are broadly distributed among different plant genera; (ii) they are expressed by a variety of different tissues and in different isoforms; and (iii) most of them are single-chain proteins
Summary
A series of plants used from ancient times for medicinal purposes in various parts of the world (reviewed in [1]) produce proteins that are today referred to as ribosome-inactivating proteins (RIPs). In both cases, the toxins were identified at the end of nineteenth century to be proteins [4,5]. The toxins were identified at the end of nineteenth century to be proteins [4,5] They were partially purified at the University of Dorpat ( Tartu in Estonia) and named ricin [6] and abrin [7], respectively. The stage of RIP history involved the pioneering immunological research of Paul Ehrlich at the Institute of Infectious Diseases in Berlin. He observed protective effects from the toxicity of either abrin or ricin in mice by feeding them low amounts of the toxins. Similar results were later observed with jequirity, and the toxin abrin was isolated from Abrus agglutinin [12]
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