Potential of the Lectin/Inhibitor Isolated from Crataeva tapia Bark (CrataBL) for Controlling Callosobruchus maculatus Larva Development

J Agric Food Chem. 2015 Dec 9;63(48):10431-6. doi: 10.1021/acs.jafc.5b03634. Epub 2015 Dec 1.

Abstract

Callosobruchus maculatus is an important predator of cowpeas. Due to infestation during storage, this insect affects the quality of seed and crop yield. This study aimed to investigate the effects of CrataBL, a multifunction protein isolated from Crataeva tapia bark, on C. maculatus larva development. The protein, which is stable even in extreme pH conditions, showed toxic activity, reducing the larval mass 45 and 70% at concentrations of 0.25 and 1.0% (w/w), respectively. Acting as an inhibitor, CrataBL decreased by 39% the activity of cysteine proteinases from larval gut. Conversely, the activity of serine proteinases was increased about 8-fold. The toxic properties of CrataBL may also be attributed to its capacity of binding to glycoproteins or glycosaminoglycans. Such binding interferes with larval metabolism, because CrataBL-FITC was found in the fat body, Malpighian tubules, and feces of larvae. These results demonstrate the potential of this protein for controlling larva development.

Keywords: C. maculatus; Crataeva tapia; bioinsecticide; glycosaminoglycan; inhibitor; lectin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Capparaceae / chemistry*
  • Coleoptera / drug effects*
  • Coleoptera / enzymology
  • Coleoptera / growth & development
  • Cysteine Proteases / metabolism
  • Cysteine Proteinase Inhibitors / pharmacology
  • Insect Proteins / metabolism
  • Larva / drug effects
  • Larva / enzymology
  • Larva / growth & development*
  • Lectins / pharmacology*
  • Plant Bark / chemistry*
  • Plant Extracts / pharmacology*

Substances

  • Cysteine Proteinase Inhibitors
  • Insect Proteins
  • Lectins
  • Plant Extracts
  • Cysteine Proteases