Crataeva tapia bark lectin is an affinity adsorbent and insecticidal agent

Hemagglutinating activity has been associated to presence of lectin, carbohydrate-binding proteins. In this work Crataeva tapia bark lectin (CrataBL) was purified in milligram quantities (28 mg per g of bark) by ion exchange chromatography. The lectin was thermo-stable, ion-independent and N-terminal sequence analysis demonstrated similarity with miraculin and miraculin-like proteins (plant defensive proteins). Glycosylated nature of CrataBL was revealed using glycoprotein staining (periodic acid–Schiff's reagent), positive for polypeptides of apparent molecular masses 21 and 40 kDa on SDS-PAGE. Gel diffusion assay showed that glucose/mannose isolectins from Cratylia mollis recognized CrataBL glycan moiety. CrataBL hemagglutinating activity was inhibited by glycoproteins and CrataBL immobilized on cyanogen bromide-activated sepharose 4B (1 mL) bound 0.54 mg of glycoprotein (casein, fetuin and ovalbumin) per cycle. CrataBL was an insecticide agent against Nasutitermes corniger workers (termite that attack woods) with LC50 of 0.475 mg mL−1 for 6 days.

► Crataeva tapia bark lectin (CrataBL) was purified by ion exchange chromatography.
► CrataBL was a thermo-stable, ion-independent and glycosylated protein.
► CrataBL N-terminal sequence showed similarity with miraculin-like proteins.
► CrataBL-Sepharose matrix bound glycoproteins (casein, fetuin and ovalbumin).
► CrataBL was an insecticide agent against Nasutitermes corniger workers.