Ebulin from dwarf elder (Sambucus ebulus L.): a mini-review

Toxins (Basel). 2015 Feb 25;7(3):648-58. doi: 10.3390/toxins7030648.


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. 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Cloning, Molecular
  • Lectins / chemistry
  • Lectins / isolation & purification
  • Plants, Medicinal / chemistry
  • Protein Biosynthesis
  • RNA, Ribosomal, 28S / genetics
  • Ribosome Inactivating Proteins, Type 2 / chemistry*
  • Ribosome Inactivating Proteins, Type 2 / isolation & purification
  • Sambucus / chemistry*


  • Lectins
  • RNA, Ribosomal, 28S
  • Ribosome Inactivating Proteins, Type 2
  • ebulin 1 protein, Sambucus ebulus
  • ebulin f, Sambucus ebulus
  • ebulin r protein, Sambucus ebulus