Location: Great Basin Rangelands ResearchTitle: Proteomic analysis of novel Cry1Ac binding proteins in Helicoverpa armigera (Hübner) Author
Submitted to: Archives of Insect Biochemistry and Physiology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 10/21/2009
Publication Date: 2/1/2010
Citation: Chen, L.Z., Liang, G.M., Zhang, J., Wu, K.M., Guo, Y.Y., Rector, B.G. 2010. Proteomic analysis of novel Cry1Ac binding proteins in Helicoverpa armigera (Hübner). Archives of Insect Biochemistry and Physiology. 73:61-73. Interpretive Summary: Resistance to Bacillus thurigiensis (Bt) insecticidal proteins in targeted pest insects is a serious challenge facing farmers who use Bt sprays and genetically enhanced crops to control these insects. The purpose of this study was to identify proteins from the midgut cells of the Old World corn earworm (Helicoverpa armigera) that may be associated with resistance to the Bt protein Cry1Ac. Through proteomic analysis using two-dimensional gel electrophoresis and Western (protein-antibody) blotting, four different H. armigera midgut proteins were identified as candidate Cry1Ac binding proteins. These results contribute to the current understanding of the mode of action of Cry toxins in Lepidopteran insects, which is incomplete and somewhat controversial despite extensive, worldwide use of Bt-based insecticides and crops expressing Bt toxins.
Technical Abstract: Aminopeptidase N (APN) and cadherin-like proteins have been previously identified as Cry1Ac-binding proteins in Helicoverpa armigera (Hübner). In this study, a proteomic approach was used to identify novel Cry1Ac-binding proteins in H. armigera. Brush border membrane vesicles (BBMV) of H. armigera were extracted and separated by two-dimensional gel electrophoresis (2-DE). Cry1Ac-binding proteins were detected using antisera against Cry1Ac. Peptide mass fingerprinting (PMF) was used to identify Cry1Ac-binding proteins. In total, four proteins were identified as candidate Cry1Ac-binding proteins in H. armigera: vacuolar ATP synthase (V-ATPase) subunit B, actin, heat shock cognate protein (HSCP), and a novel protein.