title: Oligomerization of Cry11Aa from Bacillus thuringiensis has an important role in toxicity against Aedes aegypti.
abstract: 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.
authors.affiliation: Universidad Nacional Autónoma de México, Cuernavaca 62250, Morelos, Mexico.
authors.forename: Carlos
authors.initials: C
authors.lastname: Muñoz-Garay
authors.forename: Claudia
authors.initials: C
authors.lastname: Rodríguez-Almazán
authors.forename: Jose N
authors.initials: JN
authors.lastname: Aguilar
authors.forename: Leivi
authors.initials: L
authors.lastname: Portugal
authors.forename: Isabel
authors.initials: I
authors.lastname: Gómez
authors.forename: Gloria
authors.initials: G
authors.lastname: Saab-Rincon
authors.forename: Mario
authors.initials: M
authors.lastname: Soberón
authors.forename: Alejandra
authors.initials: A
authors.lastname: Bravo
mesh_terms: 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
chemical_list: D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D004731:Endotoxins; D006460:Hemolysin Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis