Abstract
There is evidence that the gypsy moth,
Lymantria dispar, midgut epithelial brush border membrane has membrane-bound glycoconjugates, such as BTR-270 and aminopeptidase N (APN), which function as high affinity binding sites (receptors) for the insecticidal proteins produced by
Bacillus thuringiensis (
Bt). As gypsy moth larvae become older, they become resistant to the entomocidal activity of Bt, suggesting there may be a change in the expression of these toxin-binding glycoconjugates in older larvae.
Parent Publication
Citation
Valaitis, Algimantas P. 2011. Histochemical study of lectin binding sites in fourth and fifth instar gypsy moth larval midgut epithelium. In: McManus, Katherine A; Gottschalk, Kurt W., eds. 2010. Proceedings. 21st U.S. Department of Agriculture interagency research forum on invasive species 2010; 2010 January 12-15; Annapolis, MD. Gen. Tech. Rep. NRS-P-75. Newtown Square, PA: U.S. Department of Agriculture, Forest Service, Northern Research Station: 139.