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Mechanisms of the insecticidal action of TEL ( Talisia esculenta lectin) against Callosobruchus maculatus (Coleoptera: Bruchidae)
Author(s) -
Macedo Maria Lígia Rodrigues,
De Castro Márcia Mota,
Freire Maria Das Graças Machado
Publication year - 2004
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.10145
Subject(s) - midgut , callosobruchus maculatus , biology , lectin , biochemistry , proteases , mannose , affinity chromatography , trehalose , proteolysis , digestion (alchemy) , glycoprotein , glycoconjugate , enzyme , larva , botany , chemistry , chromatography , pest analysis
Plant lectins have insecticidal activity that is probably mediated through their ability to bind carbohydrates. To examine the influence of sugars on the insecticidal activity of a lectin from Talisia esculenta seeds (TEL), the lectin was mixed with mannose, glucose, or mannose plus glucose. Mannose abolished the insecticidal activity. Affinity chromatography showed that TEL bound to midgut proteins of the insect Callosobruchus maculatus . Immunoblotting showed that TEL recognized some proteins, probably glycoproteins, present in the midgut membrane of this insect. The principal proteases responsible for digestive proteolysis in fourth instar larvae of C. maculatus were purified by chromatography on activated thiol‐Sepharose. These purified proteases were unable to digest TEL after a 15‐h incubation. These results suggest that the insecticidal activity of TEL involves a specific carbohydrate‐lectin interaction with glycoconjugates on the surface of digestive tract epithelial cells, as well as binding to assimilatory glycoproteins present in midgut extracts and resistance to enzymatic digestion by cysteine proteinases. Arch. Insect Biochem. Physiol. 56:84–96, 2004. © 2004 Wiley‐Liss, Inc.