• lectin;
  • Sambucus nigra agglutinin;
  • Acyrthosiphon pisum;
  • Spodoptera exigua;
  • entomotoxicity;
  • DNA fragmentation;
  • caspase-3-like proteases


In this project, the toxicity and mechanism of action of the ricin-B-related lectin SNA-I from elderberry (Sambucus nigra) in the pea aphid (Acyrthosiphon pisum) and the beet armyworm (Spodoptera exigua), two important pest insects in agriculture, were studied. SNA-I is a chimeric lectin belonging to the class of ribosome-inactivating proteins and consists of an A-chain with N-glycosidase activity and a carbohydrate-binding B-chain. Incorporation of 2 mg/ml of SNA-I in the diet of neonates and adults of A. pisum caused 40–46% mortality within 2 days, while in third instars of S. exigua, the larval biomass was significantly reduced by 12% after feeding for 3 days on a diet containing 5 mg/g of SNA-I. Interestingly, extracts of the (mid)gut of treated A. pisum and S. exigua demonstrated DNA fragmentation and this was accompanied with an increase in caspase-3-like activity. The involvement of cell death or apoptosis in the entomotoxicity of SNA-I through induction of caspase-3-like activity was also confirmed by addition of the permeable caspase-3 inhibitor III in the diet, leading to a rescue of the treated aphid neonates. Finally, similar to the chimeric lectin SNA-I, the hololectin SNA-II, consisting of two carbohydrate-binding B-chains caused high mortality to neonate A. pisum aphids with an LC50 of 1.59 mg/ml, suggesting that the entomotoxic action of the lectins under study mainly relies on their carbohydrate-binding activity. © 2010 Wiley Periodicals, Inc.