IDENTIFICATION, ISOLATION, AND CLONING OF A BACILLUS-THURINGIENSIS CRYIAC TOXIN-BINDING PROTEIN FROM THE MIDGUT OF THE LEPIDOPTERAN INSECT HELIOTHIS-VIRESCENS
IDENTIFICATION, ISOLATION, AND CLONING OF A BACILLUS-THURINGIENSIS CRYIAC TOXIN-BINDING PROTEIN FROM THE MIDGUT OF THE LEPIDOPTERAN INSECT HELIOTHIS-VIRESCENS
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DOI：
10.1074/jbc.270.45.27277
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发表时间：
1995-11-10
影响因子：
4.8
通讯作者：
FRANCIS, V
中科院分区：
文献类型：
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作者：
GILL, SS;COWLES, EA;FRANCIS, V
苏云金芽孢杆菌（Bacillus thuringiensis）毒素对多种昆虫具有杀虫活性，其选择性取决于毒素的结构和不同昆虫的受体位点，其中CryIAc对棉铃虫具有很强的杀虫活性。使用毒素覆盖测定，120 kDa的糖蛋白被确定为毒素结合蛋白。对该蛋白进行了部分纯化，测定了其N端序列，并从一株H. virescens中肠文库，The B.苏云金杆菌毒素结合蛋白BTBP 1与原核生物和真核生物的氨肽酶N具有高度同源性。
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, BTBP1, has high homology to aminopeptidase N from eukaryotes and prokaryotes.