Oligomerization of Cry11Aa from Bacillus thuringiensis has an important role in toxicity against Aedes aegypti.
Cry11Aa and Cyt1Aa of Bacillus thuringiensis are active against mosquitoes and show synergism. Cyt1Aa functions as a membrane receptor inducing Cry11Aa oligomerization. Here we characterized Cry11Aa helix alpha-3 mutants impaired in oligomerization and toxicity against Aedes aegypti, indicating that oligomerization of Cry11Aa is important for toxin action. Cyt1Aa did not recover the insecticidal activity of Cry11Aa mutants.
Muñoz-Garay
Carlos
C
Universidad Nacional Autónoma de México, Cuernavaca 62250, Morelos, Mexico.
Rodríguez-Almazán
Claudia
C
Aguilar
Jose N
JN
Portugal
Leivi
L
Gómez
Isabel
I
Saab-Rincon
Gloria
G
Soberón
Mario
M
Bravo
Alejandra
A
D000330:Aedes / Q000187:drug effects*; D000818:Animals; D001413:Bacillus thuringiensis / Q000378:metabolism*; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism* / Q000633:toxicity*; D004731:Endotoxins / Q000235:genetics / Q000378:metabolism* / Q000633:toxicity*; D006460:Hemolysin Proteins / Q000235:genetics / Q000378:metabolism* / Q000633:toxicity*; D055503:Protein Multimerization; D017384:Sequence Deletion
D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D004731:Endotoxins; D006460:Hemolysin Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis