Recognition and binding of the PF2 lectin to α-amylase from Zabrotes subfasciatus (Coleoptera:Bruchidae) larval midgut

I. Lagarda-Diaz, D. Geiser, A. M. Guzman-Partida, J. Winzerling, L. Vazquez-Moreno

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6 Scopus citations


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.

Original languageEnglish
Article numberA68
JournalJournal of Insect Science
Issue number1
StatePublished - 1 Jan 2014

Bibliographical note

Publisher Copyright:
© The Author 2014. Published by Oxford University Press on behalf of the Entomological Society of America.


  • Amylase
  • Insecticidal effect
  • Lectin
  • PF2
  • Zabrotes subfasciatus


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