scholarly journals Binding of Bacillus thuringiensis Cry1 Toxins to the Midgut Brush Border Membrane Vesicles of Chilo suppressalis (Lepidoptera: Pyralidae): Evidence of Shared Binding Sites

1996 ◽  
Vol 62 (8) ◽  
pp. 3073-3073
Author(s):  
L Fiuza ◽  
C Nielsen-Leroux ◽  
E Goze ◽  
R Frutos ◽  
J Charles
Keyword(s):  
Bacillus Thuringiensis ◽  
Brush Border ◽  
Binding Sites ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Chilo Suppressalis ◽  
Lepidoptera Pyralidae

Volume 62, no. 5, p. 1544, Abstract, line 4: "Cry1Aa" should read "Cry1Ac." [This corrects the article on p. 1544 in vol. 62.].

scholarly journals Binding Sites for Bacillus thuringiensis Cry2Ae Toxin on Heliothine Brush Border Membrane Vesicles Are Not Shared with Cry1A, Cry1F, or Vip3A Toxin

2011 ◽  
Vol 77 (10) ◽  
pp. 3182-3188 ◽  
Author(s):  
C. Gouffon ◽  
A. Van Vliet ◽  
J. Van Rie ◽  
S. Jansens ◽  
J. L. Jurat-Fuentes
Keyword(s):  
Bacillus Thuringiensis ◽  
Brush Border ◽  
Binding Sites ◽  
Brush Border Membrane ◽  
Specific Binding ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Target Range ◽  
Content Type ◽  
Bt Toxins

ABSTRACTThe use of combinations ofBacillus thuringiensis(Bt) toxins with diverse modes of action for insect pest control has been proposed as the most efficient strategy to increase target range and delay the onset of insect resistance. Considering that most cases of cross-resistance to Bt toxins in laboratory-selected insect colonies are due to alteration of common toxin binding sites, independent modes of action can be defined as toxins sharing limited or no binding sites in brush border membrane vesicles (BBMV) prepared from the target insect larvae. In this paper, we report on the specific binding of Cry2Ae toxin to binding sites on BBMV from larvae of the three most commercially relevant heliothine species,Heliothis virescens,Helicoverpa zea, andHelicoverpa armigera. Using chromatographic purification under reducing conditions before labeling, we detected specific binding of radiolabeled Cry2Ae, which allowed us to perform competition assays using Cry1Ab, Cry1Ac, Cry1Fa, Vip3A, Cry2Ae, and Cry2Ab toxins as competitors. In these assays, Cry2Ae binding sites were shared with Cry2Ab but not with the tested Cry1 or Vip3A toxins. Our data support the use of Cry2Ae toxin in combination with Cry1 or Vip3A toxins in strategies to increase target range and delay the onset of heliothine resistance.

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

scholarly journals Changes in Permeability of Brush Border Membrane Vesicles fromSpodoptera littoralis Midgut Induced by Insecticidal Crystal Proteins from Bacillus thuringiensis

1998 ◽  
Vol 64 (4) ◽  
pp. 1563-1565 ◽  
Author(s):  
B. Escriche ◽  
N. De Decker ◽  
J. Van Rie ◽  
S. Jansens ◽  
E. Van Kerkhove
Keyword(s):  
Bacillus Thuringiensis ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Osmotic Swelling ◽  
Midgut Cell ◽  
Crystal Proteins ◽  
Light Scattering Technique ◽  
Insecticidal Crystal Proteins

ABSTRACT Bacillus thuringiensis insecticidal crystal proteins (ICPs) are thought to induce pore formation in midgut cell membranes of susceptible insects. Cry1Ca, which is significantly active inSpodoptera littoralis, made brush border membrane vesicles permeable to KCl (osmotic swelling was monitored by the light scattering technique); the marginally active ICPs Cry1Aa, Cry1Ab, and Cry1Ac did not.

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