1. Recognition and binding of the PF2 lectin to α-amylase from Zabrotes subfasciatus (Coleoptera:Bruchidae) larval midgut.
- Author
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Lagarda-Diaz I, Geiser D, Guzman-Partida AM, Winzerling J, and Vazquez-Moreno L
- Subjects
- Animals, Digestive System metabolism, Fabaceae metabolism, Larva drug effects, Larva physiology, Plant Lectins, alpha-Amylases antagonists & inhibitors, Coleoptera physiology, Digestive System drug effects, Fabaceae chemistry, Lectins metabolism, Plant Proteins metabolism, alpha-Amylases biosynthesis
- Abstract
Amylases are an important family of enzymes involved in insect carbohydrate metabolism that are required for the survival of insect larvae. For this reason, enzymes from starch-dependent insects are targets for insecticidal control. PF2 (Olneya tesota) is a lectin that is toxic to Zabrotes subfasciatus (Coleoptera: Bruchidae) larvae. In this study, we evaluated recognition of the PF2 lectin to α-amylases from Z. subfasciatus midgut and the effect of PF2 on α-amylase activity. PF2 caused a decrease of total amylase activity in vitro. Subsequently, several α-amylase isoforms were isolated from insect midgut tissues using ion exchange chromatography. Three enzyme isoforms were verified by an in-gel assay for amylase activity; however, only one isoform was recognized by antiamylase serum and PF2. The identity of this Z. subfasciatus α-amylase was confirmed by liquid chromatography-tandem mass spectrometry. The findings strongly suggest that a glycosylated α-amylase isoform from larval Z. subfasciatus midgut interacts with PF2, which interferes with starch digestion., (© The Author 2014. Published by Oxford University Press on behalf of the Entomological Society of America.)
- Published
- 2014
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