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Comparative proteomics reveals Cryptosporidium parvum manipulation of the host cell molecular expression and immune response
Cryptosporidium is a life-threating protozoan parasite belonging to the phylum Apicomplexa, which mainly causes gastroenteritis in a variety of vertebrate hosts. Currently, there is a re-emergence of Cryptosporidium infection; however, no fully effective drug or vaccine is available to treat Cryptos...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8612570/ https://www.ncbi.nlm.nih.gov/pubmed/34818332 http://dx.doi.org/10.1371/journal.pntd.0009949 |
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author | Li, Teng Liu, Hua Jiang, Nan Wang, Yiluo Wang, Ying Zhang, Jing Shen, Yujuan Cao, Jianping |
author_facet | Li, Teng Liu, Hua Jiang, Nan Wang, Yiluo Wang, Ying Zhang, Jing Shen, Yujuan Cao, Jianping |
author_sort | Li, Teng |
collection | PubMed |
description | Cryptosporidium is a life-threating protozoan parasite belonging to the phylum Apicomplexa, which mainly causes gastroenteritis in a variety of vertebrate hosts. Currently, there is a re-emergence of Cryptosporidium infection; however, no fully effective drug or vaccine is available to treat Cryptosporidiosis. In the present study, to better understand the detailed interaction between the host and Cryptosporidium parvum, a large-scale label-free proteomics study was conducted to characterize the changes to the proteome induced by C. parvum infection. Among 4406 proteins identified, 121 proteins were identified as differentially abundant (> 1.5-fold cutoff, P < 0.05) in C. parvum infected HCT-8 cells compared with uninfected cells. Among them, 67 proteins were upregulated, and 54 proteins were downregulated at 36 h post infection. Analysis of the differentially abundant proteins revealed an interferon-centered immune response of the host cells against C. parvum infection and extensive inhibition of metabolism-related enzymes in the host cells caused by infection. Several proteins were further verified using quantitative real-time reverse transcription polymerase chain reaction and western blotting. This systematic analysis of the proteomics of C. parvum-infected HCT-8 cells identified a wide range of functional proteins that participate in host anti-parasite immunity or act as potential targets during infection, providing new insights into the molecular mechanism of C. parvum infection. |
format | Online Article Text |
id | pubmed-8612570 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-86125702021-11-25 Comparative proteomics reveals Cryptosporidium parvum manipulation of the host cell molecular expression and immune response Li, Teng Liu, Hua Jiang, Nan Wang, Yiluo Wang, Ying Zhang, Jing Shen, Yujuan Cao, Jianping PLoS Negl Trop Dis Research Article Cryptosporidium is a life-threating protozoan parasite belonging to the phylum Apicomplexa, which mainly causes gastroenteritis in a variety of vertebrate hosts. Currently, there is a re-emergence of Cryptosporidium infection; however, no fully effective drug or vaccine is available to treat Cryptosporidiosis. In the present study, to better understand the detailed interaction between the host and Cryptosporidium parvum, a large-scale label-free proteomics study was conducted to characterize the changes to the proteome induced by C. parvum infection. Among 4406 proteins identified, 121 proteins were identified as differentially abundant (> 1.5-fold cutoff, P < 0.05) in C. parvum infected HCT-8 cells compared with uninfected cells. Among them, 67 proteins were upregulated, and 54 proteins were downregulated at 36 h post infection. Analysis of the differentially abundant proteins revealed an interferon-centered immune response of the host cells against C. parvum infection and extensive inhibition of metabolism-related enzymes in the host cells caused by infection. Several proteins were further verified using quantitative real-time reverse transcription polymerase chain reaction and western blotting. This systematic analysis of the proteomics of C. parvum-infected HCT-8 cells identified a wide range of functional proteins that participate in host anti-parasite immunity or act as potential targets during infection, providing new insights into the molecular mechanism of C. parvum infection. Public Library of Science 2021-11-24 /pmc/articles/PMC8612570/ /pubmed/34818332 http://dx.doi.org/10.1371/journal.pntd.0009949 Text en © 2021 Li et al https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Li, Teng Liu, Hua Jiang, Nan Wang, Yiluo Wang, Ying Zhang, Jing Shen, Yujuan Cao, Jianping Comparative proteomics reveals Cryptosporidium parvum manipulation of the host cell molecular expression and immune response |
title | Comparative proteomics reveals Cryptosporidium parvum manipulation of the host cell molecular expression and immune response |
title_full | Comparative proteomics reveals Cryptosporidium parvum manipulation of the host cell molecular expression and immune response |
title_fullStr | Comparative proteomics reveals Cryptosporidium parvum manipulation of the host cell molecular expression and immune response |
title_full_unstemmed | Comparative proteomics reveals Cryptosporidium parvum manipulation of the host cell molecular expression and immune response |
title_short | Comparative proteomics reveals Cryptosporidium parvum manipulation of the host cell molecular expression and immune response |
title_sort | comparative proteomics reveals cryptosporidium parvum manipulation of the host cell molecular expression and immune response |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8612570/ https://www.ncbi.nlm.nih.gov/pubmed/34818332 http://dx.doi.org/10.1371/journal.pntd.0009949 |
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