The Rapid Evolution of Resistance to Vip3Aa Insecticidal Protein in Mythimna separata (Walker) Is Not Related to Altered Binding to Midgut Receptors

Toxins (Basel). 2021 May 20;13(5):364. doi: 10.3390/toxins13050364.

Abstract

Laboratory selection for resistance of field populations is a well-known and useful tool to understand the potential of insect populations to evolve resistance to insecticides. It provides us with estimates of the frequency of resistance alleles and allows us to study the mechanisms by which insects developed resistance to shed light on the mode of action and optimize resistance management strategies. Here, a field population of Mythimna separata was subjected to laboratory selection with either Vip3Aa, Cry1Ab, or Cry1F insecticidal proteins from Bacillus thuringiensis. The population rapidly evolved resistance to Vip3Aa reaching, after eight generations, a level of >3061-fold resistance, compared with the unselected insects. In contrast, the same population did not respond to selection with Cry1Ab or Cry1F. The Vip3Aa resistant population did not show cross resistance to either Cry1Ab or Cry1F. Radiolabeled Vip3Aa was tested for binding to brush border membrane vesicles from larvae from the susceptible and resistant insects. The results did not show any qualitative or quantitative difference between both insect samples. Our data, along with previous results obtained with other Vip3Aa-resistant populations from other insect species, suggest that altered binding to midgut membrane receptors is not the main mechanism of resistance to Vip3Aa.

Keywords: Bacillus thuringiensis; Bt toxins; cross resistance; oriental armyworm.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacillus thuringiensis / metabolism*
  • Bacillus thuringiensis Toxins / pharmacology
  • Bacterial Proteins / pharmacology*
  • Endotoxins / pharmacology
  • Hemolysin Proteins / pharmacology
  • Insecticide Resistance
  • Insecticides / isolation & purification
  • Insecticides / pharmacology*
  • Larva
  • Moths / physiology*
  • Protein Binding

Substances

  • Bacillus thuringiensis Toxins
  • Bacterial Proteins
  • Endotoxins
  • Hemolysin Proteins
  • Insecticides
  • Vip3A protein, Bacillus thuringiensis
  • insecticidal crystal protein, Bacillus Thuringiensis