scholarly journals Aminopeptidase-N from the Helicoverpa armigera (Hubner) Brush Border Membrane Vesicles as a Receptor of Bacillus thuringiensis Cry1Ac δ-Endotoxin

2001 ◽  
Vol 43 (4) ◽  
pp. 255-259 ◽  
Author(s):  
Sanjay S. Ingle ◽  
Nidhi Trivedi ◽  
Rakesh Prasad ◽  
Jes Kuruvilla ◽  
Koteshwara Kukatla Rao ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Helicoverpa Armigera ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Aminopeptidase N ◽  
Helicoverpa Armígera ◽  
Helicoverpa Armigera Hubner

Interaction of Allium sativum leaf agglutinin with midgut brush border membrane vesicles proteins and its stability in Helicoverpa armigera

PROTEOMICS ◽  
2010 ◽  
Vol 10 (24) ◽  
pp. 4431-4440 ◽  
Author(s):  
Santosh Kumar Upadhyay ◽  
Manisha Mishra ◽  
Harpal Singh ◽  
Amol Ranjan ◽  
Krishnappa Chandrashekar ◽  
...  
Keyword(s):  
Helicoverpa Armigera ◽  
Brush Border ◽  
Allium Sativum ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Helicoverpa Armígera

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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