Interaction of Allium sativum leaf agglutinin with midgut brush border membrane vesicles proteins and its stability in Helicoverpa armigera

Proteomics. 2010 Dec;10(24):4431-40. doi: 10.1002/pmic.201000152. Epub 2010 Nov 17.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Digestive System / chemistry*
  • Digestive System / metabolism
  • Insect Proteins / chemistry*
  • Insect Proteins / metabolism
  • Mannose-Binding Lectins / chemistry*
  • Membrane Glycoproteins / chemistry*
  • Membrane Glycoproteins / metabolism
  • Microvilli / chemistry
  • Microvilli / metabolism
  • Moths / metabolism*
  • Plant Proteins / chemistry*
  • Protein Binding
  • Protein Stability
  • Tandem Mass Spectrometry

Substances

  • ASAI protein, Allium sativum
  • Insect Proteins
  • Mannose-Binding Lectins
  • Membrane Glycoproteins
  • Plant Proteins