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Changes in the proteomic profiles of mouse brain after infection with cyst-forming Toxoplasma gondii

BACKGROUND: Toxoplasma gondii is an opportunistic pathogenic protozoan parasite, which infects approximately one third of the human population worldwide, causing opportunistic zoonotic toxoplasmosis. The predilection of T. gondii for the central nervous system (CNS) causes behavioral disorders and f...

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Autores principales: Zhou, Dong-Hui, Zhao, Fu-Rong, Huang, Si-Yang, Xu, Min-Jun, Song, Hui-Qun, Su, Chunlei, Zhu, Xing-Quan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3660206/
https://www.ncbi.nlm.nih.gov/pubmed/23587304
http://dx.doi.org/10.1186/1756-3305-6-96
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author Zhou, Dong-Hui
Zhao, Fu-Rong
Huang, Si-Yang
Xu, Min-Jun
Song, Hui-Qun
Su, Chunlei
Zhu, Xing-Quan
author_facet Zhou, Dong-Hui
Zhao, Fu-Rong
Huang, Si-Yang
Xu, Min-Jun
Song, Hui-Qun
Su, Chunlei
Zhu, Xing-Quan
author_sort Zhou, Dong-Hui
collection PubMed
description BACKGROUND: Toxoplasma gondii is an opportunistic pathogenic protozoan parasite, which infects approximately one third of the human population worldwide, causing opportunistic zoonotic toxoplasmosis. The predilection of T. gondii for the central nervous system (CNS) causes behavioral disorders and fatal necrotizing encephalitis and thus constitutes a major threat especially to AIDS patients. METHODS: In the present study, we explored the proteomic profiles of brain tissues of the specific pathogen-free (SPF) Kunming mice at 7 d, 14 d and 21 d after infection with cysts of the Toxoplasma gondii Prugniaud (PRU) strain (Genotype II), by two-dimensional gel electrophoresis (2-DE) combined with MALDI-TOF/TOF tandem mass spectrometry (MS/MS). RESULTS: A total of 60 differentially expressed protein spots were selected. Fifty-six spots were successfully identified, which corresponded to 45 proteins of the mouse. Functional analysis using a Gene Ontology database showed that these proteins were mainly involved in metabolism, cell structure, signal transduction and immune responses, and will be beneficial for the understanding of molecular mechanisms of T. gondii pathogenesis. CONCLUSIONS: This study identified some mouse brain proteins involved in the response with cyst-forming T. gondii PRU strain. These results provided an insight into the responsive relationship between T. gondii and the host brain tissues, which will shed light on our understanding of the mechanisms of pathogenesis in toxoplasmic encephalitis, and facilitate the discovery of new methods of diagnosis, prevention, control and treatment of toxoplasmic encephalopathy.
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spelling pubmed-36602062013-05-22 Changes in the proteomic profiles of mouse brain after infection with cyst-forming Toxoplasma gondii Zhou, Dong-Hui Zhao, Fu-Rong Huang, Si-Yang Xu, Min-Jun Song, Hui-Qun Su, Chunlei Zhu, Xing-Quan Parasit Vectors Research BACKGROUND: Toxoplasma gondii is an opportunistic pathogenic protozoan parasite, which infects approximately one third of the human population worldwide, causing opportunistic zoonotic toxoplasmosis. The predilection of T. gondii for the central nervous system (CNS) causes behavioral disorders and fatal necrotizing encephalitis and thus constitutes a major threat especially to AIDS patients. METHODS: In the present study, we explored the proteomic profiles of brain tissues of the specific pathogen-free (SPF) Kunming mice at 7 d, 14 d and 21 d after infection with cysts of the Toxoplasma gondii Prugniaud (PRU) strain (Genotype II), by two-dimensional gel electrophoresis (2-DE) combined with MALDI-TOF/TOF tandem mass spectrometry (MS/MS). RESULTS: A total of 60 differentially expressed protein spots were selected. Fifty-six spots were successfully identified, which corresponded to 45 proteins of the mouse. Functional analysis using a Gene Ontology database showed that these proteins were mainly involved in metabolism, cell structure, signal transduction and immune responses, and will be beneficial for the understanding of molecular mechanisms of T. gondii pathogenesis. CONCLUSIONS: This study identified some mouse brain proteins involved in the response with cyst-forming T. gondii PRU strain. These results provided an insight into the responsive relationship between T. gondii and the host brain tissues, which will shed light on our understanding of the mechanisms of pathogenesis in toxoplasmic encephalitis, and facilitate the discovery of new methods of diagnosis, prevention, control and treatment of toxoplasmic encephalopathy. BioMed Central 2013-04-12 /pmc/articles/PMC3660206/ /pubmed/23587304 http://dx.doi.org/10.1186/1756-3305-6-96 Text en Copyright © 2013 Zhou et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research
Zhou, Dong-Hui
Zhao, Fu-Rong
Huang, Si-Yang
Xu, Min-Jun
Song, Hui-Qun
Su, Chunlei
Zhu, Xing-Quan
Changes in the proteomic profiles of mouse brain after infection with cyst-forming Toxoplasma gondii
title Changes in the proteomic profiles of mouse brain after infection with cyst-forming Toxoplasma gondii
title_full Changes in the proteomic profiles of mouse brain after infection with cyst-forming Toxoplasma gondii
title_fullStr Changes in the proteomic profiles of mouse brain after infection with cyst-forming Toxoplasma gondii
title_full_unstemmed Changes in the proteomic profiles of mouse brain after infection with cyst-forming Toxoplasma gondii
title_short Changes in the proteomic profiles of mouse brain after infection with cyst-forming Toxoplasma gondii
title_sort changes in the proteomic profiles of mouse brain after infection with cyst-forming toxoplasma gondii
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3660206/
https://www.ncbi.nlm.nih.gov/pubmed/23587304
http://dx.doi.org/10.1186/1756-3305-6-96
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