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Urine proteomics for profiling of mouse toxoplasmosis using liquid chromatography tandem mass spectrometry analysis
BACKGROUND: Toxoplasma gondii is an obligate intracellular parasite that causes toxoplasmosis. Urine is an easily obtained clinical sample that has been widely applied for diagnostic purposes. However, changes in the urinary proteome during T. gondii infection have never been investigated. METHODS:...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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BioMed Central
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8056516/ https://www.ncbi.nlm.nih.gov/pubmed/33879238 http://dx.doi.org/10.1186/s13071-021-04713-6 |
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author | Cui, Lin-Lin Zhou, Chun-Xue Han, Bing Wang, Sha-Sha Li, Si-Ying Xie, Shi-Chen Zhou, Dong-Hui |
author_facet | Cui, Lin-Lin Zhou, Chun-Xue Han, Bing Wang, Sha-Sha Li, Si-Ying Xie, Shi-Chen Zhou, Dong-Hui |
author_sort | Cui, Lin-Lin |
collection | PubMed |
description | BACKGROUND: Toxoplasma gondii is an obligate intracellular parasite that causes toxoplasmosis. Urine is an easily obtained clinical sample that has been widely applied for diagnostic purposes. However, changes in the urinary proteome during T. gondii infection have never been investigated. METHODS: Twenty four-hour urine samples were obtained from BALB/c mice with acute infection [11 days post infection (DPI)], mice with chronic infection (35 DPI) and healthy controls, and were analyzed using a label-free liquid chromatography tandem mass spectrometry analysis. RESULTS: We identified a total of 13,414 peptides on 1802 proteins, of which 169 and 47 proteins were significantly differentially expressed at acute and chronic infection phases, respectively. Clustering analysis revealed obvious differences in proteome profiles among all groups. Gene ontology analysis showed that a large number of differentially expressed proteins (DEPs) detected in acute infection were associated with biological binding activity and single-organism processes. KEGG pathway enrichment analysis showed that the majority of these DEPs were involved in disease-related and metabolic pathways. CONCLUSIONS: Our findings revealed global reprogramming of the urine proteome following T. gondii infection, and data obtained in this study will enhance our understanding of the host responses to T. gondii infection and lead to the identification of new diagnostic biomarkers. GRAPHIC ABSTRACT: [Image: see text] SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s13071-021-04713-6. |
format | Online Article Text |
id | pubmed-8056516 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-80565162021-04-20 Urine proteomics for profiling of mouse toxoplasmosis using liquid chromatography tandem mass spectrometry analysis Cui, Lin-Lin Zhou, Chun-Xue Han, Bing Wang, Sha-Sha Li, Si-Ying Xie, Shi-Chen Zhou, Dong-Hui Parasit Vectors Research BACKGROUND: Toxoplasma gondii is an obligate intracellular parasite that causes toxoplasmosis. Urine is an easily obtained clinical sample that has been widely applied for diagnostic purposes. However, changes in the urinary proteome during T. gondii infection have never been investigated. METHODS: Twenty four-hour urine samples were obtained from BALB/c mice with acute infection [11 days post infection (DPI)], mice with chronic infection (35 DPI) and healthy controls, and were analyzed using a label-free liquid chromatography tandem mass spectrometry analysis. RESULTS: We identified a total of 13,414 peptides on 1802 proteins, of which 169 and 47 proteins were significantly differentially expressed at acute and chronic infection phases, respectively. Clustering analysis revealed obvious differences in proteome profiles among all groups. Gene ontology analysis showed that a large number of differentially expressed proteins (DEPs) detected in acute infection were associated with biological binding activity and single-organism processes. KEGG pathway enrichment analysis showed that the majority of these DEPs were involved in disease-related and metabolic pathways. CONCLUSIONS: Our findings revealed global reprogramming of the urine proteome following T. gondii infection, and data obtained in this study will enhance our understanding of the host responses to T. gondii infection and lead to the identification of new diagnostic biomarkers. GRAPHIC ABSTRACT: [Image: see text] SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s13071-021-04713-6. BioMed Central 2021-04-20 /pmc/articles/PMC8056516/ /pubmed/33879238 http://dx.doi.org/10.1186/s13071-021-04713-6 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://creativecommons.org/publicdomain/zero/1.0/) ) applies to the data made available in this article, unless otherwise stated in a credit line to the data. |
spellingShingle | Research Cui, Lin-Lin Zhou, Chun-Xue Han, Bing Wang, Sha-Sha Li, Si-Ying Xie, Shi-Chen Zhou, Dong-Hui Urine proteomics for profiling of mouse toxoplasmosis using liquid chromatography tandem mass spectrometry analysis |
title | Urine proteomics for profiling of mouse toxoplasmosis using liquid chromatography tandem mass spectrometry analysis |
title_full | Urine proteomics for profiling of mouse toxoplasmosis using liquid chromatography tandem mass spectrometry analysis |
title_fullStr | Urine proteomics for profiling of mouse toxoplasmosis using liquid chromatography tandem mass spectrometry analysis |
title_full_unstemmed | Urine proteomics for profiling of mouse toxoplasmosis using liquid chromatography tandem mass spectrometry analysis |
title_short | Urine proteomics for profiling of mouse toxoplasmosis using liquid chromatography tandem mass spectrometry analysis |
title_sort | urine proteomics for profiling of mouse toxoplasmosis using liquid chromatography tandem mass spectrometry analysis |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8056516/ https://www.ncbi.nlm.nih.gov/pubmed/33879238 http://dx.doi.org/10.1186/s13071-021-04713-6 |
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