Identification of Cry1Ac binding proteins in the midgut of Heliothis virescens using proteomic analyses
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Bacillus thuringiensis (Bt) toxins are specifically toxic to larvae in the taxa Lepidoptera, Diptera and Coleoptera. Heliothis virescens, commonly known as the tobacco budworm, is the major crop pest controlled by Bt cotton. In the past, brush border membrane vesicles of insects have been researched to identify toxin-binding proteins because of their significance in eliciting resistance to toxins. However several of the components are still unknown because of inadequate resolution of such complex samples on a single dimension polyacrylamide gel. In this study, we identify novel Cry1Ac binding proteins by the use of two-dimensional gel resolution. A subproteome of glycosylphosphatidyl inositol (GPI) anchored proteins was analyzed because several known Cry1Ac binding proteins are GPI anchored. Peptide mass fingerprints generated from the spots of interest were searched in protein databases. Alkaline phosphatase and V-ATPase subunits A and B were identified as novel Cry1Ac binding proteins, the former is GPI anchored, while the latter are not.