Cry4Ba and Cyt1Aa proteins from Bacillus thuringiensis israelensis: Interactions and toxicity mechanism against Aedes aegypti

Toxicon. 2015 Sep 15:104:83-90. doi: 10.1016/j.toxicon.2015.07.337. Epub 2015 Jul 31.

Abstract

Individual crystal proteins from Bacillus thuringiensis israelensis exhibit variable levels of insecticidal activities against mosquito larvae. In all cases, they are much less active compared to the whole crystal proteins due to described complex synergistic interactions among them. In the present study we investigated the effects of Cyt1A98 (a Cyt1Aa type protein) on Cry4BLB (a Cry4Ba type toxin) insecticidal activity toward the dengue vector Aedes aegypti. The bioassay analyses demonstrated the ability of Cyt1A98 protein to enhance Cry4BLB toxin larvicidal activity even at a low proportion in the mixture (1%). In vitro interaction assays showed that Cyt1A98 provides supplementary binding sites for Cry4BLB in A. aegypti BBMVs. Moreover, it enhances the formation of Cry4BLB oligomeric structure. These results support that Cyt1A98 protein could act as a membrane-bound receptor fixing Cry4BLB δ-endotoxins and promoting its oligomerization.

Keywords: Aedes aegypti; Bacillus thuringiensis israelensis; Cry4BLB toxin; Cytolytic protein Cyt1A98; Synergism.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aedes / drug effects*
  • Animals
  • Bacillus thuringiensis / chemistry*
  • Bacillus thuringiensis Toxins
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / pharmacology*
  • Biological Assay
  • Drug Synergism
  • Endotoxins / chemistry
  • Endotoxins / pharmacology*
  • Hemolysin Proteins / chemistry
  • Hemolysin Proteins / pharmacology*
  • Insecticides / chemistry
  • Insecticides / pharmacology
  • Larva / drug effects
  • Microvilli / drug effects

Substances

  • Bacillus thuringiensis Toxins
  • Bacterial Proteins
  • Endotoxins
  • Hemolysin Proteins
  • Insecticides
  • insecticidal crystal protein, Bacillus Thuringiensis