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Molecular characterization of a voltage-gated calcium channel and its potential role in the acaricidal action of scopoletin against Tetranychus cinnabarinus.
Ma, Xiao-Feng; Zhang, Yuan-Yuan; Guo, Fu-You; Luo, Jin-Xiang; Ding, Wei; Zhang, Yong-Qiang.
Afiliação
  • Ma XF; College of Plant Protection, Southwest University, Chongqing 400715, China.
  • Zhang YY; College of Plant Protection, Southwest University, Chongqing 400715, China.
  • Guo FY; College of Plant Protection, Southwest University, Chongqing 400715, China.
  • Luo JX; College of Plant Protection, Southwest University, Chongqing 400715, China.
  • Ding W; College of Plant Protection, Southwest University, Chongqing 400715, China; State Cultivation Base of Crop Stress Biology for Southern Mountainous Land Southwest University, Chongqing 400715, China.
  • Zhang YQ; College of Plant Protection, Southwest University, Chongqing 400715, China; State Cultivation Base of Crop Stress Biology for Southern Mountainous Land Southwest University, Chongqing 400715, China; Chongqing Key Laboratory of Soft-Matter Material Chemistry and Function Manufacturing, Southwest Univ
Pestic Biochem Physiol ; 168: 104618, 2020 Sep.
Article em En | MEDLINE | ID: mdl-32711759
The carmine spider mite, Tetranychus cinnabarinus (Boisduval), is a polyphagous agricultural pest with an extensive host plant range. Scopoletin is a promising acaricidal compound whose acaricidal mechanism may occur by disrupting intracellular Ca2+ homeostasis and calcium signaling pathways. However, the underlying mechanism of scopoletin for specific target locations of T. cinnabarinus remains unclear. In this study, a full-length cDNA of the L-type voltage-gated calcium channel (TcLTCC) subunit gene from T. cinnabarinus was cloned and characterized. The expression pattern of the TcLTCC gene in all developmental stages of T. cinnabarinus was analyzed. The gene was highly expressed in larval and nymphal stages and was significantly upregulated after treatment with scopoletin. Knocking down the TcLTCC transcript reduced the sensitivity of T. cinnabarinus to scopoletin. Homology modeling and molecular docking were also conducted. The interaction between scopoletin and TcLTCC showed that scopoletin inserted into the cavity bound to the site of the TcLTCC protein by the driving force of hydrogen bonding. This study provides insights into the mechanism by which scopoletin interacts with TcLTCC. Results can improve the understanding of the toxicity of scopoletin to T. cinnabarinus and provide valuable information for the design of new LTCC inhibitors.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Tetranychidae / Acaricidas Tipo de estudo: Prognostic_studies Limite: Animals Idioma: En Ano de publicação: 2020 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Tetranychidae / Acaricidas Tipo de estudo: Prognostic_studies Limite: Animals Idioma: En Ano de publicação: 2020 Tipo de documento: Article