| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2006227 | Peptides | 2013 | 6 Pages |
Bacillus thuringiensis Cry toxins recognizes their target cells in part by the binding to glycosyl–phosphatidyl–inositol (GPI) anchored proteins such as aminopeptidase-N (APN) or alkaline phosphatases (ALP). Treatment of Tenebrio molitor brush border membrane vesicles (BBMV) with phospholipase C that cleaves out GPI-anchored proteins from the membranes, showed that GPI-anchored proteins are involved in binding of Cry3Aa toxin to BBMV. A 68 kDa GPI-anchored ALP was shown to bind Cry3Aa by toxin overlay assays. The 68 kDa GPI-anchored ALP was preferentially expressed in early instar larvae in comparison to late instar larvae. Our work shows for the first time that GPI-anchored ALP is important for Cry3Aa binding to T. molitor BBMV suggesting that the mode of action of Cry toxins is conserved in different insect orders.
► Glycosyl–phosphatidyl–inositol (GPI)-anchored proteins are involved in binding of Bacillus thuringiensis Cry3Aa to Tenebrio molitor brush border membranes. ► A T. molitor GPI-anchored alkaline phosphatase ALP binds Cry3Aa toxin. ► The GPI-anchored ALP was preferentially expressed in T. molitor early instar larvae in comparison to late instar larvae. ► GPI-anchored ALP are involved in the mode of action of B. thuringiensis Cry toxins in three different insect orders.
