Bacillus thuringiensis delta-endotoxin Cry1Ac domain III enhances activity against Heliothis virescens in some, but not all Cry1-Cry1Ac hybrids

R.B. Karlova, W.M.J. Weemen, S. Naimov, J. Ceron, S. Dukiandjiev, R.A. de Maagd

Research output: Contribution to journalArticleAcademicpeer-review

21 Citations (Scopus)

Abstract

We investigated the role of domain III of Bacillus thuringiensis d-endotoxin Cry1Ac in determining toxicity against Heliothis virescens. Hybrid toxins, containing domain III of Cry1Ac with domains I and II of Cry1Ba, Cry1Ca, Cry1Da, Cry1Ea, and Cry1Fb, respectively, were created. In this way Cry1Ca, Cry1Fb, and to a lesser extent Cry1Ba were made considerably more toxic.
Original languageEnglish
Pages (from-to)169-172
JournalJournal of Invertebrate Pathology
Volume88
Issue number2
DOIs
Publication statusPublished - 2005

Keywords

  • aminopeptidase-n-receptor
  • spodoptera-exigua
  • crystal proteins
  • insect midgut
  • specificity
  • binding
  • toxin
  • membrane
  • larvae
  • acetylgalactosamine

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