Abstract
Sambucus ebulus L. (dwarf elder) is a medicinal plant, the usefulness of which also as food is restricted due to its toxicity. In the last few years, both the chemistry and pharmacology of Sambucus ebulus L. have been investigated. Among the structural and functional proteins present in the plant, sugar-binding proteins (lectins) with or without anti-ribosomal activity and single chain ribosome-inactivating proteins (RIPs) have been isolated. RIPs are enzymes (E.C. 3.2.2.22) that display N-glycosidase activity on the 28S rRNA subunit, leading to the inhibition of protein synthesis by arresting the step of polypeptide chain elongation. The biological role of all these proteins is as yet unknown. The evidence suggests that they could be involved in the defense of the plant against predators and viruses or/and a nitrogen store, with an impact on the nutritional characteristics and food safety. In this mini-review we describe all the isoforms of ebulin that have to date been isolated from dwarf elder, as well as their functional characteristics and potential uses, whilst highlighting concern regarding ebulin toxicity.
Highlights
From an archaeological point of view, the most widely studied elders were the European speciesSambucus ebulus L. and Sambucus nigra L
The cyan color of the ripe dwarf elder fruit is due to several anthocyanidins such as cyanidin-3-O-sambubioside, cyanidin-3-sambubioside-5-glucoside, cyanidin-3-O-glucoside, and cyanidin-3,5-diglucoside [13]
We review the literature on ebulin, a ribosome-inactivating protein found in S. ebulus L., considering the isoforms found in the different tissues, the structural studies carried out on the ebulin present in leaves, and the consequences of its enzymatic activity such as its use in targeted therapy as a toxic moiety of immunotoxins and conjugates, and the in vivo toxicity caused by its ingestion in large amounts
Summary
From an archaeological point of view, the most widely studied elders were the European species. The improvement of lipid profile, antimicrobial, antiulcerogenic, antiparasitic, anti-inflammatory applications, and wound healing activities have been cited [5,6,7,8,9,10]. We review the literature on ebulin, a ribosome-inactivating protein found in S. ebulus L., considering the isoforms found in the different tissues, the structural studies carried out on the ebulin present in leaves (ebulin l), and the consequences of its enzymatic activity such as its use in targeted therapy as a toxic moiety of immunotoxins and conjugates, and the in vivo toxicity caused by its ingestion in large amounts. In addition to the general structural and enzymatic protein characteristics of plant species, Sambucus contains bioactive proteins like single- and two-chain lectins and ribosome-inactivating proteins (RIPs) [15,16,17]. Among the RIPs of S. ebulus L. type 1 RIPs, like ebulitins α, β and γ, and type 2 RIPs, such as different forms of ebulin, have been found
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