Toxicity of Bacillus thuringiensis (L.) Cry proteins against summer fruit tortrix (Adoxophyes orana - Fischer von Rösslerstamm).
The activity of seven Cry1, one Cry9 and one hybrid Cry1 protoxins against neonate larvae of summer fruit tortrix (Adoxophyes orana - Fischer von Rösslerstamm) has been investigated. Cry1Ia is identified as the most toxic protein, followed by Cry1Aa and Cry1Ac. Cry1Ca, Cry1Cb, Cry1Da and Cry1Fa were less active, while SN19 (Cry1 hybrid protein with domain composition 1Ba/1Ia/1Ba) and Cry9Aa exhibited negligible toxicity against A. orana. In vitro trypsin-activated Cry1Ac is still less active than Cry1Ia protoxin, suggesting that toxicity of Cry1Ia is most probably due to more complex differences in further downstream processing, toxin-receptor interactions and pore formation in A. orana's midgut epithelium.
Department of Biochemistry, Faculty of Chemistry, Studentski trg 12, 11000 Belgrade, Serbia; Department of Plant Physiology and Molecular Biology, Faculty of Biology, University of Plovdiv "Paisii Hilendarski", Tzar Asen 24, 4000 Plovdiv, Bulgaria. Electronic address: radosavljevic@chem.bg.ac.rs.
Jelena
J
Radosavljevic
Department of Plant Physiology and Molecular Biology, Faculty of Biology, University of Plovdiv "Paisii Hilendarski", Tzar Asen 24, 4000 Plovdiv, Bulgaria.
Samir
S
Naimov
D000818:Animals; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000633:toxicity*; D004731:Endotoxins / Q000633:toxicity*; D006460:Hemolysin Proteins / Q000633:toxicity*; D009036:Moths; D010572:Pest Control, Biological / Q000379:methods*
D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D004731:Endotoxins; D006460:Hemolysin Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis
Adoxophyes orana (Fischer von Rösslerstamm); Bacillus thuringiensis; Cry proteins; Cry1Ia; Summer fruit tortrix moth