Abstract:
:Insecticidal proteins or delta-endotoxins of Bacillus thuringiensis are highly toxic to a wide range of agronomically important pests. The toxins are formed of three structural domains. The N-terminal domain is a bundle of eight alpha-helices and is implicated in pore formation in insect midgut epithelial membranes. All the delta-endotoxins share a common hydrophobic motif of eight amino acids in alpha-helix 7. A similar motif is also present in fragment B of diphtheria toxin (DT). Site-directed mutagenesis of Cry1Ac delta-endotoxin of B. thuringiensis was carried out to substitute its hydrophobic motif with that of DT fragment B. The mutant toxin was shown to be more toxic to the larvae of Helicoverpa armigera (cotton bollworm) than the wild-type toxin. Voltage clamp analysis with planar lipid bilayers revealed that the mutant toxin opens larger ion channels and induces higher levels of conductance than the wild-type toxin.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Chandra A,Ghosh P,Mandaokar AD,Bera AK,Sharma RP,Das S,Kumar PAdoi
10.1016/s0014-5793(99)01157-6keywords:
subject
Has Abstractpub_date
1999-09-17 00:00:00pages
175-9issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(99)01157-6journal_volume
458pub_type
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