Amino acid substitution in alpha-helix 7 of Cry1Ac delta-endotoxin of Bacillus thuringiensis leads to enhanced toxicity to Helicoverpa armigera Hubner.

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 Lett

journal_title

FEBS letters

authors

Chandra A,Ghosh P,Mandaokar AD,Bera AK,Sharma RP,Das S,Kumar PA

doi

10.1016/s0014-5793(99)01157-6

keywords:

subject

Has Abstract

pub_date

1999-09-17 00:00:00

pages

175-9

issue

2

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(99)01157-6

journal_volume

458

pub_type

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