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首页> 外文期刊>Journal of bacteriology >Identification of amino acid residues of Bacillus thuringiensis delta-endotoxin CryIAa associated with membrane binding and toxicity to Bombyx mori.
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Identification of amino acid residues of Bacillus thuringiensis delta-endotoxin CryIAa associated with membrane binding and toxicity to Bombyx mori.

机译:苏云金芽孢杆菌δ-内毒素CryIAa氨基酸残基的鉴定与膜结合和对家蚕的毒性有关。

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摘要

Alanine substitution (A3) or deletion (D3) of residues 365 to 371 of Bacillus thuringiensis CryIAa insect toxin removed nearly all toxicity for Bombyx mori (> 1,000-fold less active than the wild type). The loss of larvicidal activity in the mutants was not caused by increased sensitivity to larval gut enzymes but could be attributed to significantly reduced binding to B. mori brush border membrane vesicles. Some or all of the affected amino acid residues may interact directly or indirectly with the B. mori membrane receptor(s). Such receptor binding appears to be directly correlated with insect toxicity.
机译:苏云金芽孢杆菌CryIAa昆虫毒素的残基365至371的丙氨酸取代(A3)或缺失(D3)消除了对家蚕的几乎所有毒性(活性比野生型低1,000倍)。突变体中杀幼虫活性的降低不是由于对幼虫肠道酶的敏感性提高,而是由于与蚕桑毛刷缘膜囊泡的结合明显减少。一些或全部受影响的氨基酸残基可与桑蚕芽孢杆菌膜受体直接或间接相互作用。这种受体结合似乎与昆虫毒性直接相关。

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