Abstract
Allium sativum leaf agglutinin (ASAL) binds to several proteins in the midgut of Helicoverpa armigera and causes toxicity. Most of these were glycosylated. Six ASAL-binding proteins were selected for identification. PMF and MS/MS data showed their similarity with midgut aminopeptidase APN2, polycalins and alkaline phosphatase of H. armigera, cadherin-N protein (partial AGAP009726-PA) of Acyrthosiphon pisum, cytochrome P450 (CYP315A1) of Manduca sexta and alkaline phosphatase of Heliothis virescens. Some of the ASAL-binding midgut proteins were similar to the larval receptors responsible for the binding of δ-endotoxin proteins of Bacillus thuringiensis. Galanthus nivalis agglutinin also interacted with most of the ASAL-binding proteins. The ASAL showed resistance to midgut proteases and was detected in the larval hemolymph and excreta. Immunohistochemical staining revealed the presence of ASAL in the body tissue also. © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
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Upadhyay, S. K., Mishra, M., Singh, H., Ranjan, A., Chandrashekar, K., Verma, P. C., … Tuli, R. (2010). Interaction of Allium sativum leaf agglutinin with midgut brush border membrane vesicles proteins and its stability in Helicoverpa armigera. Proteomics, 10(24), 4431–4440. https://doi.org/10.1002/pmic.201000152
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