Bacillus thuringiensis Cry1Ac toxin bound to a 120-kDa protein isolated from the brush border membranes of bath susceptible and resistant larvae of Phaella xylostella, the diamondback moth. The 120-kDa protein was purified by Cry1Ac toxin affinity chromatogrophy. Like Cry1Ac-binding aminopeptidase N (EC 22.214.171.124) from other insects, this protein was eluted from the affinity column with 200 mM N-acetylgaloctosamine. The purified protein had aminopeptidase activity and bound Cry1Ac toxin on ligand blots. Purified aminopeptidase was recognized by antibodies to the cross-reacting determinant found on phosphotidylinositol-specific phospholipase C-solubilized proteins. The results show that the presence of Cry1Ac-binding aminopeptidase in the brush border membrane is not sufficient to confer susceptibility to Cry1Ac. Furthermore, the results do not support the hypothesis that resistance to Cry1Ac was caused by lack of a Cry1Ac-binding aminopeptidase.
ASJC Scopus subject areas
- Food Science
- Applied Microbiology and Biotechnology