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

IF 1.6 3区生物学 Q3 BIOCHEMICAL RESEARCH METHODS

Proteome Science Pub Date : 2021-11-10 DOI:10.1186/s12953-021-00182-y

Xinjin Chen, Bolin Fan, Chenlong Fan, Zhongliang Wang, Eakapol Wangkahart, Yucong Huang, Yu Huang, Jichang Jian, Bei Wang

{"title":"First comprehensive proteome analysis of lysine crotonylation in Streptococcus agalactiae, a pathogen causing meningoencephalitis in teleosts.","authors":"Xinjin Chen, Bolin Fan, Chenlong Fan, Zhongliang Wang, Eakapol Wangkahart, Yucong Huang, Yu Huang, Jichang Jian, Bei Wang","doi":"10.1186/s12953-021-00182-y","DOIUrl":null,"url":null,"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.","PeriodicalId":20857,"journal":{"name":"Proteome Science","volume":"19 1","pages":"14"},"PeriodicalIF":1.6000,"publicationDate":"2021-11-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8580364/pdf/","citationCount":"4","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Proteome Science","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1186/s12953-021-00182-y","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOCHEMICAL RESEARCH METHODS","Score":null,"Total":0}

引用次数: 4

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.

Abstract Image

查看原文本刊更多论文

首次全面的蛋白质组学分析在无乳链球菌，一种病原体引起硬骨鱼脑膜脑炎赖氨酸巴丁酰化。

背景:无乳链球菌是一种常见的直肠阴道定殖菌，可导致新生儿和非怀孕成人的传染病，也可引起鱼类传染病和人畜共患风险。赖氨酸巴豆酰化(Lysine crotonylation, Kcr)是2011年发现的一种组蛋白翻译后修饰。在酵母和哺乳动物中，Kcr作为潜在的增强子和促进基因表达。然而，目前尚无对无乳链球菌中赖氨酸巴豆酰化的研究。方法:采用亲和富集与LC - MS/MS相结合的方法对鱼类致病菌S. agalactiae进行巴豆酰化分析。Western blotting进一步验证了选定蛋白的Kcr修饰。结果:在本研究中，我们进行了S. agalactiae中Kcr的蛋白质组全谱分析，并首次从筛选的675个蛋白中鉴定出241个Kcr位点。生物信息学分析表明，164个序列与6个明确保守的基序相匹配，其中许多基序在代谢过程、细胞过程和单生物过程中显著富集。此外，四种巴豆酰化修饰蛋白被预测为细菌的毒力因子或群体感应系统ptm的一部分。数据可通过ProteomeXchange获得，标识符为PXD026445。结论:这些数据为进一步研究巴豆酰化在无乳链球菌毒力中的功能提供了一个有希望的起点。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文求助全文

来源期刊

Proteome Science 生物-生化研究方法

CiteScore

2.90

自引率

0.00%

发文量

审稿时长

4.5 months

期刊介绍： Proteome Science is an open access journal publishing research in the area of systems studies. Proteome Science considers manuscripts based on all aspects of functional and structural proteomics, genomics, metabolomics, systems analysis and metabiome analysis. It encourages the submissions of studies that use large-scale or systems analysis of biomolecules in a cellular, organismal and/or environmental context. Studies that describe novel biological or clinical insights as well as methods-focused studies that describe novel methods for the large-scale study of any and all biomolecules in cells and tissues, such as mass spectrometry, protein and nucleic acid microarrays, genomics, next-generation sequencing and computational algorithms and methods are all within the scope of Proteome Science, as are electron topography, structural methods, proteogenomics, chemical proteomics, stem cell proteomics, organelle proteomics, plant and microbial proteomics. In spite of its name, Proteome Science considers all aspects of large-scale and systems studies because ultimately any mechanism that results in genomic and metabolomic changes will affect or be affected by the proteome. To reflect this intrinsic relationship of biological systems, Proteome Science will consider all such articles.