Analyses of α-amylase and α-glucosidase in the malaria vector mosquito, Anopheles gambiae, as receptors of Cry11Ba toxin of Bacillus thuringiensis subsp. jegathesan.
Analyses of α-amylase and α-glucosidase in the malaria vector mosquito, Anopheles gambiae, as receptors of Cry11Ba toxin of Bacillus thuringiensis subsp. jegathesan.
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DOI：
10.1016/j.ibmb.2013.07.003
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发表时间：
2013-10
影响因子：
3.8
通讯作者：
Qi Zhang;G. Hua;Krishnareddy Bayyareddy;M. Adang
中科院分区：
文献类型：
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作者：
Qi Zhang;G. Hua;Krishnareddy Bayyareddy;M. Adang
苏云金芽孢杆菌亚种jegathes3产生对蚊子幼虫具有高毒性的Cry11Ba晶体蛋白。Cry11Ba的毒性依赖于其在蚊子幼虫中肠上皮细胞上的受体。此前有报道称，钙粘蛋白样蛋白（AgCad2）、氨基肽酶（AgAPN2）和碱性磷酸酶（AgALP1）参与了Cry11Ba对冈比亚按蚊幼虫毒性的调控。本文从ma中克隆了编码α-淀粉酶（AgAmy1）和α-葡萄糖苷酶（Agm3）的cdna。gambiaelarva中肠。两者都是糖磷脂酰肌醇（GPI）锚定在刷状边界膜（BBMV）上的蛋白质。免疫组化显示它们在幼虫中肠不同部位的定位。AgAmy1和Agm3结合Cry11Ba具有较高的亲和力，分别为37.6 nM和21.1 nM。Cry11Ba对sta的毒性。AgAmy1和Agm3对冈比亚幼虫均有中和作用。结果证明AgAmy1和Agm3都是Cry11Ba - inA的受体。冈比亚按蚊。
Bacillus thuringiensis subsp.jegathesanproduces Cry11Ba crystal protein with high toxicity to mosquito larvae. The Cry11Ba toxicity is dependent on its receptors on mosquito larval midgut epithelial cells. Previously, a cadherin-like protein (AgCad2), aminopeptidase (AgAPN2) and alkaline phosphatase (AgALP1) were reported to be involved in regulation of Cry11Ba toxicity on Anopheles gambiae larvae. Here, the cDNAs encoding α-amylase (AgAmy1) and α-glucosidase (Agm3) were cloned fromA. gambiaelarva midgut. Both are glycophosphatidylinositol (GPI) anchored proteins on brush border membranes (BBMV). Immunohistochemistry revealed their localization on different regions of the larval midgut. AgAmy1 and Agm3 bound Cry11Ba with high affinity, 37.6 nM and 21.1 nM respectively. Cry11Ba toxicity againstA. gambiaelarvae was neutralized by both AgAmy1 and Agm3. The results provide evidence that both AgAmy1 and Agm3 function as receptors of Cry11Ba inA. gambiae.