scholarly journals The receptor for Bacillus thuringiensis CrylA(c) delta-endotoxin in the brush border membrane of the lepidopteran Manduca sexta is aminopeptidase N

1994 ◽  
Vol 11 (3) ◽  
pp. 429-436 ◽  
Author(s):  
Peter J. K. Knight ◽  
Neil Crickmore ◽  
David J. Ellar
Keyword(s):  
Bacillus Thuringiensis ◽  
Manduca Sexta ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Aminopeptidase N ◽  
Delta Endotoxin

scholarly journals Bacillus thuringiensis delta-endotoxin and larval Manduca sexta midgut brush-border membrane vesicles act synergistically to cause very large increases in the conductance of planar lipid bilayers.

1995 ◽  
Vol 198 (1) ◽  
pp. 91-96 ◽  
Author(s):  
F G Martin ◽  
M G Wolfersberger
Keyword(s):  
Bacillus Thuringiensis ◽  
Lipid Bilayers ◽  
Manduca Sexta ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Phospholipid Bilayers ◽  
Brush Border Membrane Vesicles ◽  
Delta Endotoxin ◽  
Manduca Sexta Larvae

Brush-border membrane vesicles prepared from midguts of Manduca sexta larvae were incorporated into planar phospholipid bilayers. Addition of Bacillus thuringiensis delta-endotoxin to the buffered salt solutions bathing these bilayers resulted in large irreversible increases in conductance. At pH 9.6, the smallest toxin-dependent increase in bilayer conductance observed was 13 nS. Similar conductance increases were never observed in the absence of delta-endotoxin or in delta-endotoxin-treated bilayers not containing components of insect brush-border membranes.

The Bacillus thuringiensis Cry1Ac toxin-induced permeability change in Manduca sexta midgut brush border membrane vesicles proceeds by more than one mechanism

1997 ◽  
Vol 110 (24) ◽  
pp. 3099-3104
Author(s):  
J. Carroll ◽  
M.G. Wolfersberger ◽  
D.J. Ellar
Keyword(s):  
Bacillus Thuringiensis ◽  
Manduca Sexta ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Aminopeptidase N ◽  
Insecticidal Toxin ◽  
Cry1ac Toxin ◽  
Posterior Midgut

Aminopeptidase N purified from whole Manduca sexta midgut binds the Cry1Ac insecticidal toxin from Bacillus thuringiensis and this binding is inhibited by N-acetylgalactosamine (GalNAc). We have examined the membrane permeabilising activity of the Cry1Ac toxin using brush border membrane vesicles (BBMV) prepared from the anterior (A-BBMV) and posterior (P-BBMV) subregions of the M. sexta midgut. A toxin mixing assay demonstrated a faster rate of toxin activity on P-BBMV than on A-BBMV. In the presence of GalNAc this rapid activity on P-BBMV was reduced to the rate seen with A-BBMV. GalNAc had no effect on the rate of A-BBMV permeabilisation by Cry1Ac. Aminopeptidase N assays of A- and P-BBMV demonstrated that this Cry1Ac binding protein is concentrated in the posterior midgut region of M. sexta. It therefore appears that there are two mechanisms by which Cry1Ac permeabilises the M. sexta midgut membrane: a GalNAc-sensitive mechanism restricted to the posterior midgut region, probably involving aminopeptidase N binding, and a previously undetected mechanism found in both the posterior and anterior regions.

scholarly journals Pore-forming properties of the Bacillus thuringiensis toxin Cry9Ca in Manduca sexta brush border membrane vesicles

2010 ◽  
Vol 1798 (6) ◽  
pp. 1111-1118 ◽  
Author(s):  
Jean-Frédéric Brunet ◽  
Vincent Vachon ◽  
Marc Juteau ◽  
Jeroen Van Rie ◽  
Geneviève Larouche ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Manduca Sexta ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Bacillus Thuringiensis Toxin
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