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Protease inhibitors fail to prevent pore formation by the activated Bacillus thuringiensis toxin Cry1Aa in insect brush border membrane vesicles

Article Abstract:

A study was conducted on the rate of pore formation by the trypsin-activated Cry1Aa in the presence of a variety of protease inhibitors with Manduca sexta midgut brush border membrane vesicles, to investigate whether membrane protease are involved in the activity of Bacillus thuringiensis insecticidal toxin. It was observed that, once activated, Cry1Aa is completely functional and does not require further proteolysis.

Author: Schwartz, Jean-Louis, Vachon, Vincent, Laprade, Raynald, Kirouac, Martin, Quievy, Delphine
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2006
Bacterial toxins

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Protease inhibitors fail to prevent pore formation by the activated Bacillus thuringiensis toxin Cry1Aa in insect brush border membrane vesicles

Article Abstract:

A study was conducted on the rate of pore formation by the trypsin-activated Cry1Aa in the presence of a variety of protease inhibitors with Manduca sexta midgut brush border membrane vesicles, to investigate whether membrane protease are involved in the activity of Bacillus thuringiensis insecticidal toxin. It was observed that, once activated, Cry1Aa is completely functional and does not require further proteolysis.

Author: Schwartz, Jean-Louis, Vachon, Vincent, Laprade, Raynald, Kirouac, Martin, Quievy, Delphine
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2006
Composition, Proteolysis

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Interaction between functional domains of Bacillus thuringiensis insecticidal crystal proteins

Article Abstract:

The three structural domains of Bacillus thuringiensis Cry1 toxins were investigated using the functional analysis of chimeric proteins. It has been found that the Bacillus thuringiensis produces a crystalline inclusion body that contains highly specific insecticidal proteins known as sigma-endotoxins. The study suggests that functional interaction among these domains may be crucial to the toxin.

Author: Bosch, Dirk, Schwartz, Jean-Louis, Vachon, Vincent, Laprade, Raynald, Frutos, Roger, Rang, Cecile, Maagd, Rudd A. de, Villalon, Mario
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1999
Endotoxins, Bacterial cell walls

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Subjects list: Research, Protease inhibitors, Bacillus thuringiensis
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