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Altered binding of the Cry1Ac toxin to larval membranes but not to the toxin-binding protein in Plodia interpunctella selected for resistance to different Bacillus thuringiensis isolates

Article Abstract:

The Bacillus thuringiensis-produced Cry1Ab and the Cry1Ac toxins fail to show any differences in their binding to the protein of ca.80-kDa in Plodia interpunctella strains resistant to the toxins. The binding protein is necessary for toxicity and differs in size from the aminopeptidase N antigens responsible for binding in other insects. The toxins bind to the membranes of susceptible larvae but not to those of resistant larvae. This indicates that the resistant P. interpunctella strains have altered accessibility of Cry1A-binding protein rather than altered binding properties.

Author: Mohammed, Sulma I., Johnson, Donovan E., Aronson, Arthur I.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1996
Analysis, Physiological aspects, Moths, Insects, Protein binding, Insect larvae

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Evidence for production of paralytic shellfish toxins by bacteria associated with Alexandrium spp. (Dinophyta) in culture

Article Abstract:

An analysis of five cultures of Alexandrium, isolated from different dinoflagellate cultures, shows that the bacteria autonomously produce paralytic shellfish toxins (PSTs). All the bacteria produce gonyautoxin (GTX) 1 and 4. Some Alexandrium species also produce GTX 2 and 3, C toxins, saxitoxin (STX) and neo-STX. The bacterial cultures produce the PSTs in amounts comparable to those obtained from fish, shellfish and seawater.

Author: Flynn, K.J., Gallacher, S., Franco, J.M., Brueggemann, E.E., Hines, H.B.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1997
Observations, Paralytic shellfish poisoning

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Identification of residues in domain III of Bacillus thuringiensis Cry1Ac toxin that affect binding and toxicity

Article Abstract:

Research was conducted to determine the amino acid residues involved in the binding and toxicity properties of the Cry1Ac toxin using alanine substituted mutants. Results show that binding affinity relative to toxicity was affected which depended on the particular residue that was being substituted.

Author: Dean, Donald H., Lee, Mi Kyong, Gould, Fred L., You, Taek H.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1999
United States, Alanine, Amino acids, Amino acid structure-activity relationships, Toxicity testing, Toxicity tests

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Subjects list: Bacterial toxins, Research
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