Interaction of 65- and 62-kD proteins from the apical membranes of the Aedes aegypti larvae midgut epithelium with Cry4B and Cry11A endotoxins of Bacillus thuringiensis
Interaction of 65- and 62-kD proteins from the apical membranes of the Aedes aegypti larvae midgut epithelium with Cry4B and Cry11A endotoxins of Bacillus thuringiensis
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DOI：
10.1023/a:1015594127636
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发表时间：
2002-05-01
影响因子：
2.8
通讯作者：
Chestukhina, GG
中科院分区：
文献类型：
--
作者：
Buzdin, AA;Revina, LP;Chestukhina, GG
分子量为65 kD的蛋白质是埃及伊蚊幼虫BBM中唯一能够特异性结合苏云金芽孢杆菌杀蚊毒素Cry4B和Cry11A的成分。该蛋白缺乏亮氨酸氨肽酶活性，而亮氨酸氨肽酶活性是毛毛虫膜上毒素结合蛋白的特征。对埃及伊蚊幼虫无活性的 Cry 毒素要么无法与 65 kD 蛋白及其分子量为 62 W 的蛋白水解推定产物 (Cry 1Ab) 结合，要么与杀蚊蛋白 (Cry9A) 结合但不竞争这种结合。 Cry4B 毒素分子中前 5 个 α 螺旋的蛋白水解分裂不会影响其与 65-和 62-kD 蛋白质的结合，但从分子 C 末端额外去除 20-30 个氨基酸会严重破坏这种结合。单糖残基不参与 65-和 62-kD 蛋白质与 Cry4B、Cry11A 和 Cry9A 的结合。
A protein with the molecular weight of 65 kD is the only component of Aedesaegypti larvae BBM capable to specifically bind mosquitocidal toxins Cry4B and Cry11A of Bacillus thuringiensis. This protein lacks the leucine aminopeptidase activity which is characteristic for the toxin-binding proteins from the membranes of caterpillars. Cry-toxins inactive against A. aegypti larvae either fail to bind to the 65-kD protein and to a putative product of its proteolysis with the molecular weight of 62 W (Cry 1Ab), or bind but do not compete for this binding with mosquitocidal proteins (Cry9A). The proteolytic splitting out of the first five alpha-helices in the Cry4B toxin molecule does not affect its binding to the 65- and 62-kD proteins, but an additional removal of 20-30 amino acids from the C-terminal of the molecule sharply spoils this binding. Monosaccharide residues are not involved in the binding of the 65- and 62-kD proteins with Cry4B, Cry11A, and Cry9A.