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Two different Bacillus thuringiensis delta-endotoxin receptors in the midgut brush border membrane of the European corn borer, Ostrinia nubilalis (Hubner) (Lepidoptera: Pyralidae)

By: Contributor(s): Material type: ArticleArticleLanguage: En Publication details: 1993ISSN:
  • 1098-5336 (Revista en electrónico)
  • 0099-2240
Subject(s): DDC classification:
  • 95-014133
 In: Applied and Environmental Microbiology v. 59, no. 6, p. 1828-183795-014133Summary: Binding of three Bacillus thuringiensis insecticidal crystal proteins (ICPs) to the midgut epithelium of Ostrinia nubilalis larvae was characterized by performing binding experiments with both isolated brush border membrane vesicles and gut tissue sections. Our results demonstrate that two independent ICP receptors are present in the brush border of O. nubilalis gut epithelium. From competition binding experiments performed with 125I-labeled and native ICPs it was concluded that CryIA(b) and CryIA(c) are recognized by the same receptor. An 11-fold-higher binding affinity of CryIA(b) for this receptor correlated with a 10-fold-higher toxicity of this ICP
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Item type Current library Collection Call number Copy number Status Date due Barcode Item holds
Article CIMMYT Knowledge Center: John Woolston Library AGRIS Collection 95-014133 (Browse shelf(Opens below)) 1 Available 95-014133
Total holds: 0

Peer-review: Yes - Open Access: Yes|http://science.thomsonreuters.com/cgi-bin/jrnlst/jlresults.cgi?PC=MASTER&ISSN=0099-2240

Binding of three Bacillus thuringiensis insecticidal crystal proteins (ICPs) to the midgut epithelium of Ostrinia nubilalis larvae was characterized by performing binding experiments with both isolated brush border membrane vesicles and gut tissue sections. Our results demonstrate that two independent ICP receptors are present in the brush border of O. nubilalis gut epithelium. From competition binding experiments performed with 125I-labeled and native ICPs it was concluded that CryIA(b) and CryIA(c) are recognized by the same receptor. An 11-fold-higher binding affinity of CryIA(b) for this receptor correlated with a 10-fold-higher toxicity of this ICP

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