The Crystal Structure of Bacillus thuringiensis Tpp80Aa1 and Its Interaction with Galactose-Containing Glycolipids.

The Crystal Structure of Bacillus thuringiensis Tpp80Aa1 and Its Interaction with Galactose-Containing Glycolipids.
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DOI:
10.3390/toxins14120863
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发表时间:
2022-12-08
期刊:
影响因子:
4.2
通讯作者:
Berry C
Berry C
中科院分区:
医学2区
文献类型:
--
作者:
Best HL;Williamson LJ;Lipka-Lloyd M;Waller-Evans H;Lloyd-Evans E;Rizkallah PJ;Berry C

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苏云金芽孢杆菌Tpp80Aa1是一种毒素_10家族蛋白(Toxin_10 family protein,Tpp),对库蚊有明显的杀虫作用。在这里,我们展示了一个扩大的目标范围,显示Tpp80Aa1也对冈比亚按蚊和埃及伊蚊的幼虫有效。我们首次报道了Tpp 80 Aa 1的晶体结构,其分辨率为1.8 μ m,表明Tpp 80 Aa 1由两个结构域组成:N端的β三叶结构域类似于蓖麻毒素B凝集素,C端的孔形成结构域与气溶素家族具有结构相似性。与其他Tpp家族成员相似,我们观察到Tpp80Aa1与蚊子中肠结合,特别是后中肠和胃盲囊。我们还确定Tpp80Aa1可以与含半乳糖的糖脂和半乳糖相互作用,这种相互作用对于对蚊子靶细胞系发挥充分的杀虫作用至关重要。
Tpp80Aa1 from Bacillus thuringiensis is a Toxin_10 family protein (Tpp) with reported action against Culex mosquitoes. Here, we demonstrate an expanded target range, showing Tpp80Aa1 is also active against the larvae of Anopheles gambiae and Aedes aegypti mosquitoes. We report the first crystal structure of Tpp80Aa1 at a resolution of 1.8 Å, which shows Tpp80Aa1 consists of two domains: an N-terminal β-trefoil domain resembling a ricin B lectin and a C-terminal putative pore-forming domain sharing structural similarity with the aerolysin family. Similar to other Tpp family members, we observe Tpp80Aa1 binds to the mosquito midgut, specifically the posterior midgut and the gastric caecum. We also identify that Tpp80Aa1 can interact with galactose-containing glycolipids and galactose, and this interaction is critical for exerting full insecticidal action against mosquito target cell lines.
DOI: 10.1038/nature19825
发表时间: 2016-11-03
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