Bacillus thuringiensis delta-endotoxin Cry1Ac domain III enhances activity against Heliothis virescens in some, but not all Cry1-Cry1Ac hybrids.
We investigated the role of domain III of Bacillus thuringiensis delta-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.
Karlova
Rumyana
R
Department of Plant Physiology and Molecular Biology, University of Plovdiv, 4000 Plovdiv, Bulgaria.
Weemen-Hendriks
Mieke
M
Naimov
Samir
S
Ceron
Jairo
J
Dukiandjiev
Stefan
S
de Maagd
Ruud A
RA
D000595:Amino Acid Sequence; D000818:Animals; D001413:Bacillus thuringiensis / Q000502:physiology*; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000633:toxicity*; D001427:Bacterial Toxins / Q000737:chemistry / Q000235:genetics / Q000633:toxicity*; D004731:Endotoxins / Q000737:chemistry / Q000235:genetics / Q000633:toxicity*; D006460:Hemolysin Proteins; D007915:Lepidoptera / Q000187:drug effects / Q000382:microbiology*; D008969:Molecular Sequence Data; D010572:Pest Control, Biological; D011994:Recombinant Proteins / Q000235:genetics / Q000633:toxicity
D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D004731:Endotoxins; D006460:Hemolysin Proteins; D011994:Recombinant Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis