Identification of an interaction between calcium-dependent protein kinase 4 (EtCDPK4) and serine protease inhibitor (EtSerpin) in Eimeria tenella

文献类型: 外文期刊

第一作者: Lv, Ling

作者: Lv, Ling;Huang, Bing;Yan, Ming;Lv, Ling;Huang, Bing;Zhao, Qiping;Zhao, Zongping;Dong, Hui;Zhu, Shunhai;Chen, Ting;Yan, Ming;Han, Hongyu

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关键词: Eimeria tenella; Calcium-dependent protein kinases; Serpin; Yeast two-hybrid; Bimolecular fluorescence complementation; Co-immunoprecipitation

期刊名称:PARASITES & VECTORS ( 影响因子:3.876; 五年影响因子:3.959 )

ISSN: 1756-3305

年卷期: 2018 年 11 卷

页码:

收录情况: SCI

摘要: Background: Eimeria tenella is an obligate intracellular apicomplexan protozoan parasite that has a complex life-cycle. Calcium ions, through various calcium-dependent protein kinases (CDPKs), regulate key events in parasite growth and development, including protein secretion, movement, differentiation, and invasion of and escape from host cells. In this study, we identified proteins that interact with EtCDPK4 to lay a foundation for clarifying the role of CDPKs in calcium channels. Methods: Eimeria tenella merozoites were collected to construct a yeast two-hybrid (Y2H) cDNA library. The Y2H system was used to identify proteins that interact with EtCDPK4. One of interacting proteins was confirmed using bimolecular fluorescence complementation and co-immunoprecipitation in vivo. Co-localization of proteins was performed using immunofluorescence assays. Results: Eight proteins that interact with EtCDPK4 were identified using the Y2H system. One of the proteins, E. tenella serine protease inhibitor 1 (EtSerpin), was further confirmed. Conclusion: In this study, we screened for proteins that interact with EtCDPK4. An interaction between EtSerpin and EtCDPK4 was identified that may contribute to the invasion and development of E. tenella in host cells.

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