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最近很忙，几件事情凑到一起了，有篇文章需要翻译，没有时间做，并且自己的英语水平也有限。特在此请高手帮忙翻译成中文。我浏览了哈，除专业词汇外，不是很难的， 呵呵。如果有高手能做，请先回个帖子，最好在1.17号之前弄出来。 caodong023@163.com 文题是 ：Engineering Modified Bt Toxins to Counter Insect Resistance 这个是摘要：The evolution of insect resistance threatens the effectiveness of Bacillus thuringiensis (Bt) toxinsthat are widely used in sprays and transgenic crops. Resistance to Bt toxins in some insects is linked with mutations that disrupt a toxin-binding cadherin protein. We show that susceptibility to the Bttoxin Cry1Ab was reduced by cadherin gene silencing with RNA interference in Manduca sexta,confirming cadherin’s role in Bt toxicity. Native Cry1A toxins required cadherin to form oligomers, but modified Cry1A toxins lacking one a-helix did not. The modified toxins killed cadherin-silencedM. sexta and Bt-resistant Pectinophora gossypiella that had cadherin deletion mutations. Ourfindings suggest that cadherin promotes Bt toxicity by facilitating toxin oligomerization and demonstrate that the modified Bt toxins may be useful against pests resistant to standard Bt toxins. 纳米下载 http://www.namipan.com/d/f287b47 ... e2f4b4c24845c470300 Engineering Modified Bt Toxins to.pdf |
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caitikuan
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Two hypotheses proposed to explain how Cry1A toxins function are the pore-formation model and the signaling model. 两个提出解释Cry1A毒素功能的假设是孔隙形成模型和信号模型。 These theories share initial steps: Cry1A protoxins are ingested, solubilized in the gut, and cleaved by midgut proteases such as trypsin to yield activated 60-kD monomeric toxins that bind to cadherin with high affinity. 这些理论的共同初始步骤： Cry1A 前毒素蛋白的摄入， 在肠道中溶解，经中肠蛋白酶如胰蛋白酶的消化分裂产生和钙粘蛋白具有高亲和力生物活性的60-kD 单体毒素蛋白。 The signaling model, derived from studies of insect cell cultures, suggests that after protease-activated monomeric toxins bind to cadherin, initiation of a magnesium-dependent signaling pathway causes cell death. 信号模式：来自昆虫细胞培养的研究表明，蛋白酶激活单体毒素结合钙粘蛋白后，发起镁依赖的信号转导通路引起细胞死亡。 In contrast, on the basis of results from in vitro experiments and bioassays, the pore-formation model proposes that protease activated monomers bind to cadherin to facilitate protease cleavage of the N-terminus of the toxin, including helix a-1of domain. 与上面相反，在体外实验和生物测定结果的基础上，孔隙形成模型建议蛋白酶激活单体结合钙粘蛋白能促进裂解蛋白酶裂解毒素N -末端，包括α-1的螺旋结构域。 This cleavage induces the assembly of oligomeric forms of the toxin, which have increased binding affinity to secondary receptors,including glycosylphosphatidylinositol-anchored proteins, aminopeptidase N, and alkaline phosphatases. 这种分裂诱导毒素低聚体的装配，这种装配能提高二级受体的亲和力，包括糖基磷脂酰肌醇锚蛋白，氨肽酶N和碱性磷酸酶。 |
10楼2009-01-15 11:49:04
jianwu2691
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2楼2009-01-12 17:48:35
4楼2009-01-13 13:47:25
caitikuan
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The evolution of insect resistance threatens the effectiveness of Bacillus thuringiensis (Bt) toxinsthat are widely used in sprays and transgenic crops. 抗虫性演变威胁被广泛应用在喷雾剂和转基因作物的苏云金杆菌毒素的有效性。 Resistance to Bt toxins in some insects is linked with mutations that disrupt a toxin-binding cadherin protein. 一些抗苏云金杆菌毒素的昆虫的抗性是和毒素结合钙粘蛋白的断裂相关。 We show that susceptibility to the Bttoxin Cry1Ab was reduced by cadherin gene silencing with RNA interference in Manduca sexta, confirming cadherin’s role in Bt toxicity. 在烟草天蛾体内RNA干扰使钙粘蛋白基因沉默导致苏云金杆菌毒素的Cry1Ab蛋白的敏感性降低，证明了钙粘蛋白在苏云金杆菌毒素中的作用。 Native Cry1A toxins required cadherin to form oligomers, but modified Cry1A toxins lacking one a-helix did not. 天然的Cry1A毒素需要钙粘蛋白形成寡聚体，但是改变的Cry1A缺少一个α-螺旋不能形成寡聚体。 The modified toxins killed cadherin-silenced Manduca sexta and Bt-resistant Pectinophora gossypiella that had cadherin deletion mutations. 修饰后的毒素能杀死钙粘蛋白沉默的烟草天蛾和钙粘蛋白缺失突变造成苏云金杆菌毒素抵抗的棉红铃虫。 Our findings suggest that cadherin promotes Bt toxicity by facilitating toxin oligomerization and demonstrate that the modified Bt toxins may be useful against pests resistant to standard Bt toxins. 我们的研究结果表明，钙粘蛋白通过推动毒素寡聚化作用来促进苏云金杆菌毒素的作用，还表明修饰后的苏云金杆菌毒素可能是对害虫抗药性（抗标准的苏云金杆菌毒素）有用的。 [ Last edited by caitikuan on 2009-1-15 at 10:31 ] |
5楼2009-01-13 16:41:02
