Role of bacillus thuringiensis toxin domains in toxicity and receptor binding in the diamondback moth

@article{Ballester1999RoleOB,
  title={Role of bacillus thuringiensis toxin domains in toxicity and receptor binding in the diamondback moth},
  author={Ballester and Granero and RA deMaagd and Bosch and Mensua and Ferre},
  journal={Applied and environmental microbiology},
  year={1999},
  volume={65 5},
  pages={1900-3}
}
The toxic fragment of Bacillus thuringiensis crystal proteins consists of three distinct structural domains. There is evidence that domain I is involved in pore formation and that domain II is involved in receptor binding and specificity. It has been found that, in some cases, domain III is also important in determining specificity. Furthermore, involvement of domain III in binding has also been reported recently. To investigate the role of toxin domains in the diamondback moth (Plutella… CONTINUE READING