Enhancement of Bacillus thuringiensis insecticidal activity by combining Cry1Ac and bi-functional toxin HWTX-XI from spider

J Invertebr Pathol. 2016 Mar:135:60-2. doi: 10.1016/j.jip.2015.02.005. Epub 2015 Feb 23.

Abstract

In order to assess the potency of bi-functional HWTX-XI toxin from spider Ornithoctonus huwena in improving the insecticidal activity of Bacillus thuringiensis, a fusion gene of cry1Ac and hwtx-XI was constructed and expressed in an acrystalliferous B. thuringiensis strain Cry(-)B. Western blot analysis and microscopic observation revealed that the recombinant strain could express 140-kDa Cry1Ac-HWTX-XI fusion protein and produce parasporal inclusions during sporulation. Bioassay using the larvae of Helicoverpa armigera and Spodoptera exigua showed that the Cry1Ac-HWTX-XI fusion was more toxic than the control Cry1Ac protoxin, as revealed by 95% lethal concentration. Our study indicated that the HWTX-XI from spider might be a candidate for enhancing the toxicity of B. thuringiensis products.

Keywords: Bacillus thuringiensis; Cry1Ac; Fusion protein; Insecticidal activity; Spider toxin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacillus thuringiensis / drug effects
  • Bacillus thuringiensis / physiology*
  • Bacillus thuringiensis Toxins
  • Bacterial Proteins / pharmacology*
  • Biological Assay
  • Endotoxins / pharmacology*
  • Hemolysin Proteins / pharmacology*
  • Insecticides / chemistry
  • Insecticides / pharmacology*
  • Larva / drug effects
  • Lethal Dose 50
  • Moths / drug effects*
  • Recombinant Fusion Proteins / pharmacology
  • Spider Venoms / pharmacology*
  • Spiders / chemistry*
  • Spodoptera / drug effects

Substances

  • Bacillus thuringiensis Toxins
  • Bacterial Proteins
  • Endotoxins
  • Hemolysin Proteins
  • Insecticides
  • Recombinant Fusion Proteins
  • Spider Venoms
  • insecticidal crystal protein, Bacillus Thuringiensis