First comprehensive proteome analysis of lysine crotonylation in Streptococcus agalactiae, a pathogen causing meningoencephalitis in teleosts

Abstract 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-translationa...

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Autores principales: Xinjin Chen, Bolin Fan, Chenlong Fan, Zhongliang Wang, Eakapol Wangkahart, Yucong Huang, Yu Huang, Jichang Jian, Bei Wang
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Publicado: BMC 2021
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spelling oai:doaj.org-article:3eddf54db52e44b2a8a6797de963b1022021-11-14T12:06:27ZFirst comprehensive proteome analysis of lysine crotonylation in Streptococcus agalactiae, a pathogen causing meningoencephalitis in teleosts10.1186/s12953-021-00182-y1477-5956https://doaj.org/article/3eddf54db52e44b2a8a6797de963b1022021-11-01T00:00:00Zhttps://doi.org/10.1186/s12953-021-00182-yhttps://doaj.org/toc/1477-5956Abstract 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.Xinjin ChenBolin FanChenlong FanZhongliang WangEakapol WangkahartYucong HuangYu HuangJichang JianBei WangBMCarticleStreptococcus agalactiaeCrotonylationVirulence factorsProteomicsCytologyQH573-671ENProteome Science, Vol 19, Iss 1, Pp 1-10 (2021)
institution DOAJ
collection DOAJ
language EN
topic Streptococcus agalactiae
Crotonylation
Virulence factors
Proteomics
Cytology
QH573-671
spellingShingle Streptococcus agalactiae
Crotonylation
Virulence factors
Proteomics
Cytology
QH573-671
Xinjin Chen
Bolin Fan
Chenlong Fan
Zhongliang Wang
Eakapol Wangkahart
Yucong Huang
Yu Huang
Jichang Jian
Bei Wang
First comprehensive proteome analysis of lysine crotonylation in Streptococcus agalactiae, a pathogen causing meningoencephalitis in teleosts
description Abstract 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.
format article
author Xinjin Chen
Bolin Fan
Chenlong Fan
Zhongliang Wang
Eakapol Wangkahart
Yucong Huang
Yu Huang
Jichang Jian
Bei Wang
author_facet Xinjin Chen
Bolin Fan
Chenlong Fan
Zhongliang Wang
Eakapol Wangkahart
Yucong Huang
Yu Huang
Jichang Jian
Bei Wang
author_sort Xinjin Chen
title 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_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_sort first comprehensive proteome analysis of lysine crotonylation in streptococcus agalactiae, a pathogen causing meningoencephalitis in teleosts
publisher BMC
publishDate 2021
url https://doaj.org/article/3eddf54db52e44b2a8a6797de963b102
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