Toxicity of lectins and processing of ingested proteins in the pea aphidAcyrthosiphon pisum

Acute toxicity of thirty lectins was tested against the pea aphidAcyrthosiphon pisum (Harris) (Homoptera, Aphididae: Macrosiphini). Activity was measured on artificial diets containing moderate concentrations of lectins (10–250 μg/ml) by scoring mortality and growth inhibition over the whole nymphal period (7 days at 20°C). Most of the proteins tested exhibited low toxicity, but some induced significant mortality; these included the lectins from jackbean (Concanavalin A), amaranth, lentil and snowdrop. There was no direct correlation between toxicity and sugar specificity of the lectin; however, many mannose-binding lectins were toxic towardsA. pisum. Concanavalin A was also tested on five other aphid species (Aphis gossypii, Aulacortum solani, Macrosiphum euphorbiae, Macrosiphum albifrons andMyzus persicae) at concentrations between 10–1500 μg/ml. Mortality was very variable from one species to another. Strong growth inhibition invariably occurred within this concentration range, although dose-response curves differed substantially between aphid species. The peptidase complement ofA. pisum’s digestive tract was also investigated, as well as the oral toxicity of some protease inhibitors (PIs) to this aphid. Most protein PIs were inactive, and no part of the digestive tract contained detectable amounts of endo-protease activity. This is in contrast to the strong amino-peptidase activity which was shown to occur predominantly in the midgut and crop portions of the digestive tract. The potential of lectins in transgenic crops to confer Host-Plant Resistance to aphids is discussed.