ISSN:
1432-1424
Keywords:
Key words: CrylAa δ-endotoxin —Bacillus thuringiensis—Bombyx mori larval midgut — K+/amino acid symporters — Brush border membrane vesicles — Isolated midgut
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Abstract. We have examined the type of inhibition exerted by an activated preparation of the Bacillus thuringiensisδ-endotoxin CrylAa on K+-dependent leucine transport into midgut brush border membrane vesicles or epithelial cells of the isolated midgut from Bombyx mori to study its possible interaction with the amino acid symporter. K+ permeability and the cation-dependent amino acid translocation into brush border membrane vesicles were evaluated by monitoring the fluorescence of the voltage-sensitive cyanine dye 3,3′-dipropylthiadicarbocyanine iodide. The symporter ability to accept Na+ instead of K+ was exploited and the dissipation of an imposed inside-negative potential (K+ gradient in〉out and valinomycin) was registered in the presence of a Na+ gradient (out〉in) and of the amino acid. The fluorescence quenching dissipated more rapidly when the amino acid was present. Preincubation of brush border membrane vesicles with CrylAa caused a significant decrease of the amino acid-dependent recovery of fluorescence, whereas K+ permeability was sparely affected. In the isolated midgut, CrylAa inhibits leucine uptake as well as the transepithelial electrical potential difference. The strong inhibition exerted by the δ-endotoxin was observed also in the absence of potassium and the transepithelial electrical potential difference. The results obtained strongly suggest a direct interaction of CrylAa δ-endotoxin with the K+/amino acid symporter.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s002329900284
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