Ribosome-inactivating proteins and other lectins from Adenia (Passifloraceae)

Toxicon. 2005 Nov;46(6):658-63. doi: 10.1016/j.toxicon.2005.07.008. Epub 2005 Sep 13.

Abstract

The caudices of 10 Adenia species contain galactose-binding lectins that were purified by affinity chromatography. All lectins but three agglutinate human erythrocytes. Six lectins consist of two unequal chains, which can be separated by reduction, and inhibit protein synthesis both by a rabbit reticulocyte lysate and by HeLa and Raji cells. The lectins from A. goetzii, A. lanceolata and A. stenodactyla had the highest cytotoxicity, inhibiting cell protein synthesis with IC50s (concentration inhibiting by 50%) below 0.1 ng/ml, and deadenylate DNA, thus being type 2 ribosome-inactivating proteins.

Publication types

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

MeSH terms

  • Animals
  • Cell Line
  • Chromatography, Affinity
  • Chromatography, High Pressure Liquid
  • Cytotoxicity Tests, Immunologic
  • Electrophoresis, Polyacrylamide Gel
  • Humans
  • Passifloraceae / chemistry*
  • Plant Lectins / chemistry
  • Plant Lectins / isolation & purification*
  • Plants, Toxic / chemistry
  • Protein Synthesis Inhibitors / chemistry
  • Protein Synthesis Inhibitors / isolation & purification*
  • Protein Synthesis Inhibitors / toxicity
  • Rabbits
  • Ribosomes / drug effects
  • Species Specificity
  • Toxins, Biological / chemistry
  • Toxins, Biological / isolation & purification*
  • Toxins, Biological / toxicity

Substances

  • Plant Lectins
  • Protein Synthesis Inhibitors
  • Toxins, Biological