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Please use this identifier to cite or link to this item: http://hdl.handle.net/1807/23131

Title: P210k: The putative binding protein for Bacillus thuringiensis CryIA(c)delta-endotoxin in the midgut brush-border membrane of the lepidopteran Diatraea saccharalis
Issue Date: 31-Dec-1996
Publisher: Elfos Scientiae
Citation: Biotecnologia Aplicada (ISSN: 0684-4551) Vol 13 Num 2
Abstract: Biotechnologia Aplicada 1996; Vol. 13, No. 2 Roberto I Vazquez, Dmitri L Prieto, Ariel Martinez and Gustavo A de la Riva Code Number: BA96045 Sizes of Files: Text: 4.3K Graphics: Line drawing (gif) - 5.5K Introduction Bacillus thuringiensis is a gram-positive soil bacterium, able to produce insecticidal parasporal bodies during sporulation. These bodies -commonly of crystalline shape are composed of subunits called -endotoxins, or Cry proteins, encoded by cry genes, which form a large gene family. The Cry proteins are classified in classes and subclasses according to aminoacid sequence homology and target specificity (1). The mode of action of B. thuringiensis insecticidal proteins involves several stages (2). Upon ingestion by the insect larvae, the Cry proteins are proteolytically processed in the midgut, and bind to high-affinity specific membrane receptors located on the brush-border epithelium. Then, cation-specific channels are formed causing an electrolytic imbalance that ultimately kills the larva. Several authors report the identification and purification of Cry protein receptors from various insect species, as well as cloning and sequencing of their genes. Copyright 1996 Elfos Scientiae
URI: http://hdl.handle.net/1807/23131
Other Identifiers: http://www.bioline.org.br/abstract?id=ba96045
Rights: Copyright 1996 Elfos Scientiae
Appears in Collections:Bioline International Legacy Collection

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