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

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, differentiat...

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Autores principales: Lv, Ling, Huang, Bing, Zhao, Qiping, Zhao, Zongping, Dong, Hui, Zhu, Shunhai, Chen, Ting, Yan, Ming, Han, Hongyu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5913893/
https://www.ncbi.nlm.nih.gov/pubmed/29688868
http://dx.doi.org/10.1186/s13071-018-2848-y
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author Lv, Ling
Huang, Bing
Zhao, Qiping
Zhao, Zongping
Dong, Hui
Zhu, Shunhai
Chen, Ting
Yan, Ming
Han, Hongyu
author_facet Lv, Ling
Huang, Bing
Zhao, Qiping
Zhao, Zongping
Dong, Hui
Zhu, Shunhai
Chen, Ting
Yan, Ming
Han, Hongyu
author_sort Lv, Ling
collection PubMed
description 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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spelling pubmed-59138932018-04-30 Identification of an interaction between calcium-dependent protein kinase 4 (EtCDPK4) and serine protease inhibitor (EtSerpin) in Eimeria tenella Lv, Ling Huang, Bing Zhao, Qiping Zhao, Zongping Dong, Hui Zhu, Shunhai Chen, Ting Yan, Ming Han, Hongyu Parasit Vectors Research 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. BioMed Central 2018-04-23 /pmc/articles/PMC5913893/ /pubmed/29688868 http://dx.doi.org/10.1186/s13071-018-2848-y Text en © The Author(s). 2018 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research
Lv, Ling
Huang, Bing
Zhao, Qiping
Zhao, Zongping
Dong, Hui
Zhu, Shunhai
Chen, Ting
Yan, Ming
Han, Hongyu
Identification of an interaction between calcium-dependent protein kinase 4 (EtCDPK4) and serine protease inhibitor (EtSerpin) in Eimeria tenella
title Identification of an interaction between calcium-dependent protein kinase 4 (EtCDPK4) and serine protease inhibitor (EtSerpin) in Eimeria tenella
title_full Identification of an interaction between calcium-dependent protein kinase 4 (EtCDPK4) and serine protease inhibitor (EtSerpin) in Eimeria tenella
title_fullStr Identification of an interaction between calcium-dependent protein kinase 4 (EtCDPK4) and serine protease inhibitor (EtSerpin) in Eimeria tenella
title_full_unstemmed Identification of an interaction between calcium-dependent protein kinase 4 (EtCDPK4) and serine protease inhibitor (EtSerpin) in Eimeria tenella
title_short Identification of an interaction between calcium-dependent protein kinase 4 (EtCDPK4) and serine protease inhibitor (EtSerpin) in Eimeria tenella
title_sort identification of an interaction between calcium-dependent protein kinase 4 (etcdpk4) and serine protease inhibitor (etserpin) in eimeria tenella
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5913893/
https://www.ncbi.nlm.nih.gov/pubmed/29688868
http://dx.doi.org/10.1186/s13071-018-2848-y
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