Data/hora: 10/06/2024 12:22:59

Provedor de dados: 	Obihiro University of Agriculture and Veterinary Medicine Academic Repository (OAK)	
País: 	Japan	
Título: 	Characterization of a Toxoplasma gondii calcium calmodulin-dependent protein kinase homolog	
Autores: 	Kato, Kentaro; Sugi, Tatsuki; Takemae, Hitoshi; Takano, Ryo; Gong, Haiyan; Ishiwa, Akiko; Horimoto, Taisuke; Akashi, Hiroomi.	
Data: 	2016-07-21	
Ano: 	2016	
Palavras-chave: 	Calcium calmodulin-dependent protein kinase homolog; GAP45; Phosphorylation; T. gondii CaMK-related kinase; Toxoplasma gondii.	
Resumo: 	Background: Toxoplasma gondii is an obligate intracellular parasite of the phylum Apicomplexa and a major pathogen of animals and immunocompromised humans, in whom it causes encephalitis. Understanding the mechanism of tachyzoite invasion is important for the discovery of new drug targets and may serve as a model for the study of other apicomplexan parasites. We previously showed that Plasmodium falciparum expresses a homolog of human calcium calmodulin-dependent protein kinase (CaMK) that is important for host cell invasion. In this study, to identify novel targets for the treatment of Toxoplasma gondii infection (another apicomplexan parasite), we sought to identify a CaMK-like protein in the T. gondii genome and to characterize its role in the life-cycle of this parasite. Methods: An in vitro kinase assay was performed to assess the phosphorylation activities of a novel CaMK-like protein in T. gondii by using purified proteins with various concentrations of calcium, calmodulin antagonists, or T. gondii glideosome proteins. Indirect immunofluorescence microscopy was performed to detect the localization of this protein kinase by using the antibodies against this protein and organellar maker proteins of T. gondii. Results: We identified a novel CaMK homolog in T. gondii, T. gondii CaMK-related kinase (TgCaMKrk), which exhibits calmodulin-independent autophosphorylation and substrate phosphorylation activity. However, calmodulin antagonists had no effect on its kinase activity. In T. gondii-infected cells, TgCaMKrk localized to the apical ends of extracellular and intracellular tachyzoites. TgCaMKrk phosphorylated TgGAP45 for phosphorylation in vitro. Conclusions: Our data improve our understanding of T. gondii motility and infection, the interaction between parasite protein kinases and glideosomes, and drug targets for protozoan diseases.	
Idioma: 	Inglês	
Identificador: 	http://ir.obihiro.ac.jp/dspace/handle/10322/4447

info:doi/10.1186/s13071-016-1676-1	
Editor: 	Biomed Central	
Fonte: 	This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/).