Insecticidal action of Annona coriacea lectin against the flour moth Anagasta kuehniella and the rice moth Corcyra cephalonica (Lepidoptera: Pyralidae)

Annona coriacea lectin (ACLEC) was tested for insecticidal activity against larvae of two pyralid moths, Anagasta kuehniella and Corcyra cephalonica. ACLEC produced ∼ 50% mortality and mass loss in A. kuehniella larvae when incorporated into an artificial diet at levels of 1.5% and 1.0% (w/w), respe...

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Published in:Comparative biochemistry and physiology. Toxicology & pharmacology 2007-09, Vol.146 (3), p.406-414
Main Authors: Coelho, Mirela B., Marangoni, Sérgio, Macedo, Maria Lígia R.
Format: Article
Language:English
Subjects:
Anagasta kuehniella
Animals
Annona
Annona coriacea seed
Corcyra cephalonica
Dose-Response Relationship, Drug
Eating - drug effects
Gastrointestinal Tract - drug effects
Gastrointestinal Tract - metabolism
Insect Control - methods
Insect proteases
Insecticides - pharmacokinetics
Insecticides - toxicity
Larva - drug effects
Larva - growth & development
Lepidoptera
Lethal Dose 50
Moths - drug effects
Nutritional parameters
Oryza sativa
Plant Extracts - pharmacokinetics
Plant Extracts - toxicity
Plant lectin
Plant Lectins - isolation & purification
Plant Lectins - pharmacokinetics
Plant Lectins - toxicity
Pyralidae
Seeds - chemistry
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Summary:Annona coriacea lectin (ACLEC) was tested for insecticidal activity against larvae of two pyralid moths, Anagasta kuehniella and Corcyra cephalonica. ACLEC produced ∼ 50% mortality and mass loss in A. kuehniella larvae when incorporated into an artificial diet at levels of 1.5% and 1.0% (w/w), respectively. In contrast, the inclusion of up to 2% ACLEC in the diet did not significantly decrease the survival or weight of C. cephalonica larvae. The nutritional indices for A. kuehniella and C. cephalonica suggested that ACLEC had a multi-mechanistic mode of action and was an antifeedant for both insects. The toxicity in A. kuehniella apparently resulted from a change in the gut membrane environment and consequent disruption of digestive enzyme recycling mechanisms. Affinity chromatography showed that ACLEC bound to midgut proteins of A. kuehniella and C. cephalonica. However, the 14 kDa subunit of ACLEC was not digested by midgut proteases of A. kuehniella, but was degraded by the corresponding C. cephalonica proteases within a few hours. These findings suggest the possibility of using ACLEC to engineer crop plants.
ISSN:1532-0456
1878-1659
DOI:10.1016/j.cbpc.2007.05.001