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Volume 270,
Number 45,
Issue of November 10, 1995 pp. 27277-27282
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Identification,
Isolation, and Cloning of a Bacillus thuringiensis CryIAc
Toxin-binding Protein from the Midgut of the Lepidopteran Insect Heliothis virescens
(Received for publication, June 27,
1995; and in revised form, September 7, 1995)
Sarjeet S.
Gill
, ,
Elizabeth A.
Cowles
,
Vidyasagar
Francis
Bacillus thuringiensis toxins are insecticidal to a
variety of insect species. The selectivity of the toxins produced by
these bacteria is dependent on both the toxin structure and the
receptor sites that are present in different insect species. One of
these toxins, CryIAc, is highly insecticidal to the noctuid pest Heliothis virescens. Using toxin overlay assay, a 120-kDa
glycoprotein was identified as a toxin-binding protein. This protein
was partially purified, its N-terminal sequence was determined, and the
full-length cDNA encoding this protein was isolated from a H.
virescens midgut library. The B. thuringiensis toxin-binding protein, BTBP , has high homology to
aminopeptidase N from eukaryotes and prokaryotes.

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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.
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