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Effects of Yersinia ruckeri invasion on the proteome of the Chinook salmon cell line CHSE-214
Yersinia ruckeri is an important bacterial pathogen of fish, in particular salmonids, it has been associated with systemic infections worldwide and, like many enteric bacteria, it is a facultative intracellular pathogen. However, the effect of Y. ruckeri’s interactions with the host at the cellular...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7366648/ https://www.ncbi.nlm.nih.gov/pubmed/32678312 http://dx.doi.org/10.1038/s41598-020-68903-5 |
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author | Menanteau-Ledouble, Simon Nöbauer, Katharina Razzazi-Fazeli, Ebrahim El-Matbouli, Mansour |
author_facet | Menanteau-Ledouble, Simon Nöbauer, Katharina Razzazi-Fazeli, Ebrahim El-Matbouli, Mansour |
author_sort | Menanteau-Ledouble, Simon |
collection | PubMed |
description | Yersinia ruckeri is an important bacterial pathogen of fish, in particular salmonids, it has been associated with systemic infections worldwide and, like many enteric bacteria, it is a facultative intracellular pathogen. However, the effect of Y. ruckeri’s interactions with the host at the cellular level have received little investigation. In the present study, a culture of Chinook Salmon Embryo (CHSE) cell line was exposed to Y. ruckeri. Afterwards, the proteins were investigated and identified by mass spectrometry and compared to the content of unexposed cultures. The results of this comparison showed that 4.7% of the identified proteins were found at significantly altered concentrations following infection. Interestingly, infection with Y. ruckeri was associated with significant changes in the concentration of surface adhesion proteins, including a significantly decreased presence of β-integrins. These surface adhesion molecules are known to be the target for several adhesion molecules of Yersiniaceae. The concentration of several anti-apoptotic regulators (HSP90 and two DNAj molecules) appeared similarly downregulated. Taken together, these findings suggest that Y. ruckeri affects the proteome of infected cells in a notable manner and our results shed some light on the interaction between this important bacterial pathogen and its host. |
format | Online Article Text |
id | pubmed-7366648 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-73666482020-07-17 Effects of Yersinia ruckeri invasion on the proteome of the Chinook salmon cell line CHSE-214 Menanteau-Ledouble, Simon Nöbauer, Katharina Razzazi-Fazeli, Ebrahim El-Matbouli, Mansour Sci Rep Article Yersinia ruckeri is an important bacterial pathogen of fish, in particular salmonids, it has been associated with systemic infections worldwide and, like many enteric bacteria, it is a facultative intracellular pathogen. However, the effect of Y. ruckeri’s interactions with the host at the cellular level have received little investigation. In the present study, a culture of Chinook Salmon Embryo (CHSE) cell line was exposed to Y. ruckeri. Afterwards, the proteins were investigated and identified by mass spectrometry and compared to the content of unexposed cultures. The results of this comparison showed that 4.7% of the identified proteins were found at significantly altered concentrations following infection. Interestingly, infection with Y. ruckeri was associated with significant changes in the concentration of surface adhesion proteins, including a significantly decreased presence of β-integrins. These surface adhesion molecules are known to be the target for several adhesion molecules of Yersiniaceae. The concentration of several anti-apoptotic regulators (HSP90 and two DNAj molecules) appeared similarly downregulated. Taken together, these findings suggest that Y. ruckeri affects the proteome of infected cells in a notable manner and our results shed some light on the interaction between this important bacterial pathogen and its host. Nature Publishing Group UK 2020-07-16 /pmc/articles/PMC7366648/ /pubmed/32678312 http://dx.doi.org/10.1038/s41598-020-68903-5 Text en © The Author(s) 2020 Open Access This 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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Menanteau-Ledouble, Simon Nöbauer, Katharina Razzazi-Fazeli, Ebrahim El-Matbouli, Mansour Effects of Yersinia ruckeri invasion on the proteome of the Chinook salmon cell line CHSE-214 |
title | Effects of Yersinia ruckeri invasion on the proteome of the Chinook salmon cell line CHSE-214 |
title_full | Effects of Yersinia ruckeri invasion on the proteome of the Chinook salmon cell line CHSE-214 |
title_fullStr | Effects of Yersinia ruckeri invasion on the proteome of the Chinook salmon cell line CHSE-214 |
title_full_unstemmed | Effects of Yersinia ruckeri invasion on the proteome of the Chinook salmon cell line CHSE-214 |
title_short | Effects of Yersinia ruckeri invasion on the proteome of the Chinook salmon cell line CHSE-214 |
title_sort | effects of yersinia ruckeri invasion on the proteome of the chinook salmon cell line chse-214 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7366648/ https://www.ncbi.nlm.nih.gov/pubmed/32678312 http://dx.doi.org/10.1038/s41598-020-68903-5 |
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