Schaftoside Interacts With NlCDK1 Protein: A Mechanism of Rice Resistance to Brown Planthopper, Nilaparvata lugens.
Schaftoside Interacts With NlCDK1 Protein: A Mechanism of Rice Resistance to Brown Planthopper, Nilaparvata lugens.
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Schaftoside 与 NICDK1 蛋白相互作用：水稻抗褐飞虱的机制
DOI：
10.3389/fpls.2018.00710
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发表时间：
2018
影响因子：
5.6
通讯作者：
Yu XP
中科院分区：
文献类型：
--
作者：
Hao PY;Feng YL;Zhou YS;Song XM;Li HL;Ma Y;Ye CL;Yu XP
褐飞虱（Nilaparvata lugens Stål）是亚洲国家水稻的重要害虫。活性物质与水稻对褐飞虱的抗性密切相关。本研究采用高效液相色谱、质谱联用和核磁共振技术对大米总黄酮中的活性成分进行了鉴定。结果，从水稻黄酮类化合物中分离到一种抗褐飞虱相关化合物，即HPLC色谱图中的峰1，经鉴定为沙夫托苷。人工饲料饲养实验表明，沙夫托苷对BPH的抑制作用呈剂量依赖性，在0.10和0.15mg·mL ~（-1）浓度下，沙夫托苷对BPH的存活有显著抑制作用（p < 0.05）。荧光光谱显示沙夫托苷与BPH的CDK 1激酶NlCDK 1有很强的结合能力。NlCDK 1与沙夫托苷结合的表观结合常数KA为6.436 × 103 L/mol。对接模型表明，Schaftoside可能通过与ATP结合元件GXGXXGXV（Gly 11 to Val 18）中的氨基酸残基Glu 12，Thr 14和Val 17相互作用，影响NlCDK 1作为蛋白激酶的活化。用抗磷酸化CDK 1（pThr 14）抗体进行的Western blot证实，沙夫托苷处理抑制了NlCDK 1的Thr-14位点的磷酸化，从而抑制了其作为激酶的活化。因此，本研究揭示了Schaftoside与NlCDK 1的相互作用模式，揭示了水稻抗褐飞虱的新机制。
Brown planthopper (BPH) Nilaparvata lugens Stål is a serious insect pest of rice in Asian countries. Active compounds have close relationship with rice resistance against BPH. In this study, HPLC, MS/MS, and NMR techniques were used to identify active compounds in total flavonoids of rice. As a result, a BPH resistance-associated compound, Peak 1 in HPLC chromatogram of rice flavonoids, was isolated and identified as schaftoside. Feeding experiment with artificial diet indicated that schaftoside played its role in a dose dependent manner, under the concentration of 0.10 and 0.15 mg mL-1, schaftoside showed a significant inhibitory effect on BPH survival (p < 0.05), in comparison with the control. The fluorescent spectra showed that schaftoside has a strong ability to bind with NlCDK1, a CDK1 kinase of BPH. The apparent association constant KA for NlCDK1 binding with schaftoside is 6.436 × 103 L/mol. Docking model suggested that binding of schaftoside might affect the activation of NlCDK1 as a protein kinase, mainly through interacting with amino acid residues Glu12, Thr14 and Val17 in the ATP binding element GXGXXGXV (Gly11 to Val18). Western blot using anti-phospho-CDK1 (pThr14) antibody confirmed that schaftoside treatment suppressed the phosphorylation on Thr-14 site of NlCDK1, thus inhibited its activation as a kinase. Therefore, this study revealed the schaftoside-NlCDK1 interaction mode, and unraveled a novel mechanism of rice resistance against BPH.
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影响因子：
3.7
作者：
Navarro-Retamal C;Caballero J
通讯作者：
Caballero J
影响因子：
8.8
作者：
Qin L;Fan M;Candas D;Jiang G;Papadopoulos S;Tian L;Woloschak G;Grdina DJ;Li JJ
通讯作者：
Li JJ
影响因子：
5.6
作者：
Petrussa E;Braidot E;Zancani M;Peresson C;Bertolini A;Patui S;Vianello A
通讯作者：
Vianello A
影响因子：
4.1
作者：
Hu, Jie;Cheng, Mingxing;He, Yuqing
通讯作者：
He, Yuqing
影响因子：
2.3
作者：
Onyilagha, JC;Lazorko, J;Erlandson, MA
通讯作者：
Erlandson, MA