Evolution of Plant Ribosome-Inactivating Proteins

Peumans, Willy J.; Damme, Els J.M. Van

doi:10.1007/978-3-642-12176-0_1

Cited by 21 publications

(20 citation statements)

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“…Sequence analyses have shown that RIPs are widely distributed, even if not ubiquitous, in the plant kingdom (reviewed in [75]). Knowledge concerning the genomic sequences of an increasing number of RIPs has allowed for phylogenetic analysis of their evolutionary history.…”

Section: Studies Of the Genetics And Phylogenesis Of Ribosome-inacmentioning

confidence: 99%

“…They could have provided the lectin domain for the fusion with an ancestral RIP domain developed in flowering plants 300 million years ago, thus giving rise to type 2 RIPs. With regard to type 1 RIPs, they could have originated independently through a convergent evolutionary process either from the ancestral gene or from the deletion of the lectin domain (reviewed in [75]).…”

Section: Studies Of the Genetics And Phylogenesis Of Ribosome-inacmentioning

confidence: 99%

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Ribosome-Inactivating Proteins from Plants: A Historical Overview

et al. 2016

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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.Keywords: anticancer drugs; antiviral proteins; immunotoxins; plant lectins; plant toxins; ribosome-inactivating proteins; ricin; science history The First StudiesA 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) (reviewed in [2]). Some of these RIP-expressing medicinal plants are very toxic, and their toxicity has been known since antiquity (reviewed in [3]).The history of RIPs began when the interest of the scientific community turned to the toxicity of plant poisons, in particular those from the seeds of Ricinus communis L. (castor bean) and Abrus precatorius L. (jequirity bean). In both cases, the toxins were identified at the end of nineteenth century to be proteins [4,5]. They were partially purified at the University of Dorpat (now Tartu in Estonia) and named ricin [6] and abrin [7], respectively. These studies, performed for a doctoral thesis, identified ricin and abrin as haemagglutinins, and their toxicity was erroneously attributed to their ability to agglutinate red blood cells.The next 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. The immunized animals still conserved sensitivity to the other toxin, demonstrating the specificity of the immunity. He found that the serum of the immunized animals contained proteins that were able to precipitate the specific immunizing toxin but not the other toxin. He also found that the anti-toxin immunity could be transferred from the mother to the offspring both through bl...

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Section: Studies Of the Genetics And Phylogenesis Of Ribosome-inacmentioning

confidence: 99%

Section: Studies Of the Genetics And Phylogenesis Of Ribosome-inacmentioning

confidence: 99%

Ribosome-Inactivating Proteins from Plants: A Historical Overview

et al. 2016

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“…Phylogenetic analysis suggested that most type 1 RIPs found in dicots are evolutionary related to type 2 RIPs [6]. The type 1 RIPs from Iris x hollandica are derived from the deletion of the lectin domain of the type 2 RIPs.…”

Section: Discussionmentioning

confidence: 99%

“…However, RIP sequences are not ubiquitous in plants. For example, no RIP sequence could be retrieved from the complete genome of Arabidopsis thaliana [6]. At present, RIPs have been reported frequently in the plant families Cucurbitaceae, Euphorbiaceae, Sambucaceae, Phytolaccaceae, Poaceae, and Caryophyllaceae [7].…”

Section: Introductionmentioning

confidence: 99%

“…Most RIPs identified and studied today are expressed at high level which enabled the purification of the protein and characterization of their activities. Since more genome/transcriptome sequences have become available for plants in the last decades, these data also yielded more information with respect to the distribution and evolution of RIP sequences [5,6,17,18]. At present, it is clear that the distribution of RIPs is underestimated, since many RIPs are expressed at levels that are too low to allow purification of the protein.…”

Section: Introductionmentioning

confidence: 99%

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Ribosome Inactivating Proteins from Rosaceae

2016

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Ribosome-inactivating proteins (RIPs) are widespread among higher plants of different taxonomic orders. In this study, we report on the RIP sequences found in the genome/transcriptome of several important Rosaceae species, including many economically important edible fruits such as apple, pear, peach, apricot, and strawberry. All RIP domains from Rosaceae share high sequence similarity with conserved residues in the catalytic site and the carbohydrate binding sites. The genomes of Malus domestica and Pyrus communis contain both type 1 and type 2 RIP sequences, whereas for Prunus mume, Prunus persica, Pyrus bretschneideri, and Pyrus communis a complex set of type 1 RIP sequences was retrieved. Heterologous expression and purification of the type 1 as well as the type 2 RIP from apple allowed to characterize the biological activity of the proteins. Both RIPs from Malus domestica can inhibit protein synthesis. Furthermore, molecular modelling suggests that RIPs from Rosaceae possess three-dimensional structures that are highly similar to the model proteins and can bind to RIP substrates. Screening of the recombinant type 2 RIP from apple on a glycan array revealed that this type 2 RIP interacts with terminal sialic acid residues. Our data suggest that the RIPs from Rosaceae are biologically active proteins.

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