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Nonenzymatic glycosylation of lepidopteran-active Bacillus thuringiensis protein crystals

Article Abstract:

Nonenzymatic glycosylation gave rise to glucose, fucose, arabinose/rhamnose, galactose, galactosamine, glucosamine, glucose and mannose and this was revealed because the sugars could not eliminated by N or O glycanases, they were affected by the medium in which there was bacterial growth and by the time at which the crystals were harvested and the chemical identity & stochiometry of the sugars traced did not fit known glycoprotein models. High-pH amion-exchange chromatography with pubed amperometric detection was used to determine the monosccharides covalently attached to Bacillus thuringiensis HD-1 crystals.

Author: Nickerson, Kenneth W., Bhattacharya, Meenakshi, Plantz, Bradley A., Swanson-Kobler, Jane D.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1993
Glycolysis

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The Bacillus thuringiensis insecticidal toxin binds biotin-containing proteins

Article Abstract:

The brush border membrane vesicles (BBMVs) from larvae of Manduca sexta, a tobacco hornworm, have two streptavidin-binding proteins that are ca. 120 and 85 kDa. The binding can be prevented by incubating BBMVs with Bacillus thuringiensis, which is biotin-binding. The toxins bind to pyruvate carboxylase, a biotin-containing enzyme, and biotinylated bovine serum albumin and ovalbumin rather than to their nonbiotinylated compounds. The biotin binding site is present in domain III of the toxin and has a sequence similarity to those of streptavidin, avidin, and a biotin specific monoclonal antibody.

Author: Nickerson, Kenneth W., Du, Cheng
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1996
Bacterial toxins, Microbial insecticides

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Surface display of recombinant proteins on Bacillus thuringiensis spores

Article Abstract:

The insecticidal protoxin from Bacillus thuringiensis is shown to be a major component of the spore coat. A novel surface display system is developed using Bacillus thuringiensis spores in which the N-terminal portion of the protoxin is replaced with a heterologous protein.

Author: Nickerson, Kenneth W., Cheng Du, Wing C. Chan, McKiethan, Timothy W.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2005
Science & research, Recombinant proteins, Genetic research

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Subjects list: Research, Bacillus thuringiensis
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