Premium
Interaction of Allium sativum leaf agglutinin with midgut brush border membrane vesicles proteins and its stability in Helicoverpa armigera
Author(s) -
Upadhyay Santosh Kumar,
Mishra Manisha,
Singh Harpal,
Ranjan Amol,
Chandrashekar Krishnappa,
Verma Praveen Chandra,
Singh Pradhyumna Kumar,
Tuli Rakesh
Publication year - 2010
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201000152
Subject(s) - midgut , biology , helicoverpa armigera , bombyx mori , biochemistry , agglutinin , hemolymph , brush border , allium sativum , lectin , alkaline phosphatase , microbiology and biotechnology , enzyme , botany , larva , vesicle , membrane , gene
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.