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First comprehensive proteome analysis of lysine crotonylation in Streptococcus agalactiae, a pathogen causing meningoencephalitis in teleosts
BACKGROUD: Streptococcus agalactiae is a common colonizer of the rectovaginal tract and lead to infectious diseases of neonatal and non-pregnant adults, which also causes infectious disease in fish and a zoonotic risk as well. Lysine crotonylation (Kcr) is a kind of histone post-translational modifi...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8580364/ https://www.ncbi.nlm.nih.gov/pubmed/34758830 http://dx.doi.org/10.1186/s12953-021-00182-y |
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author | Chen, Xinjin Fan, Bolin Fan, Chenlong Wang, Zhongliang Wangkahart, Eakapol Huang, Yucong Huang, Yu Jian, Jichang Wang, Bei |
author_facet | Chen, Xinjin Fan, Bolin Fan, Chenlong Wang, Zhongliang Wangkahart, Eakapol Huang, Yucong Huang, Yu Jian, Jichang Wang, Bei |
author_sort | Chen, Xinjin |
collection | PubMed |
description | BACKGROUD: Streptococcus agalactiae is a common colonizer of the rectovaginal tract and lead to infectious diseases of neonatal and non-pregnant adults, which also causes infectious disease in fish and a zoonotic risk as well. Lysine crotonylation (Kcr) is a kind of histone post-translational modifications discovered in 2011. In yeast and mammals, Kcr function as potential enhancers and promote gene expression. However, lysine crotonylation in S. agalactiae has not been studied yet. METHODS: In this study, the crotonylation profiling of fish pathogen, S. agalactiae was investigated by combining affinity enrichment with LC MS/MS. The Kcr modification of several selected proteins were further validated by Western blotting. RESULTS: In the present study, we conducted the proteome-wide profiling of Kcr in S. agalactiae and identified 241 Kcr sites from 675 screened proteins for the first time. Bioinformatics analysis showed that 164 sequences were matched to a total of six definitively conserved motifs, and many of them were significantly enriched in metabolic processes, cellular process, and single-organism processes. Moreover, four crotonylation modified proteins were predicted as virulence factors or to being part of the quorum sensing system PTMs on bacteria. The data are available via ProteomeXchange with identifier PXD026445. CONCLUSIONS: These data provide a promising starting point for further functional research of crotonylation in bacterial virulence in S. agalactiae. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12953-021-00182-y. |
format | Online Article Text |
id | pubmed-8580364 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-85803642021-11-12 First comprehensive proteome analysis of lysine crotonylation in Streptococcus agalactiae, a pathogen causing meningoencephalitis in teleosts Chen, Xinjin Fan, Bolin Fan, Chenlong Wang, Zhongliang Wangkahart, Eakapol Huang, Yucong Huang, Yu Jian, Jichang Wang, Bei Proteome Sci Research BACKGROUD: Streptococcus agalactiae is a common colonizer of the rectovaginal tract and lead to infectious diseases of neonatal and non-pregnant adults, which also causes infectious disease in fish and a zoonotic risk as well. Lysine crotonylation (Kcr) is a kind of histone post-translational modifications discovered in 2011. In yeast and mammals, Kcr function as potential enhancers and promote gene expression. However, lysine crotonylation in S. agalactiae has not been studied yet. METHODS: In this study, the crotonylation profiling of fish pathogen, S. agalactiae was investigated by combining affinity enrichment with LC MS/MS. The Kcr modification of several selected proteins were further validated by Western blotting. RESULTS: In the present study, we conducted the proteome-wide profiling of Kcr in S. agalactiae and identified 241 Kcr sites from 675 screened proteins for the first time. Bioinformatics analysis showed that 164 sequences were matched to a total of six definitively conserved motifs, and many of them were significantly enriched in metabolic processes, cellular process, and single-organism processes. Moreover, four crotonylation modified proteins were predicted as virulence factors or to being part of the quorum sensing system PTMs on bacteria. The data are available via ProteomeXchange with identifier PXD026445. CONCLUSIONS: These data provide a promising starting point for further functional research of crotonylation in bacterial virulence in S. agalactiae. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12953-021-00182-y. BioMed Central 2021-11-10 /pmc/articles/PMC8580364/ /pubmed/34758830 http://dx.doi.org/10.1186/s12953-021-00182-y 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 Chen, Xinjin Fan, Bolin Fan, Chenlong Wang, Zhongliang Wangkahart, Eakapol Huang, Yucong Huang, Yu Jian, Jichang Wang, Bei First comprehensive proteome analysis of lysine crotonylation in Streptococcus agalactiae, a pathogen causing meningoencephalitis in teleosts |
title | First comprehensive proteome analysis of lysine crotonylation in Streptococcus agalactiae, a pathogen causing meningoencephalitis in teleosts |
title_full | First comprehensive proteome analysis of lysine crotonylation in Streptococcus agalactiae, a pathogen causing meningoencephalitis in teleosts |
title_fullStr | First comprehensive proteome analysis of lysine crotonylation in Streptococcus agalactiae, a pathogen causing meningoencephalitis in teleosts |
title_full_unstemmed | First comprehensive proteome analysis of lysine crotonylation in Streptococcus agalactiae, a pathogen causing meningoencephalitis in teleosts |
title_short | First comprehensive proteome analysis of lysine crotonylation in Streptococcus agalactiae, a pathogen causing meningoencephalitis in teleosts |
title_sort | first comprehensive proteome analysis of lysine crotonylation in streptococcus agalactiae, a pathogen causing meningoencephalitis in teleosts |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8580364/ https://www.ncbi.nlm.nih.gov/pubmed/34758830 http://dx.doi.org/10.1186/s12953-021-00182-y |
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