ArticleProteome science2021
First comprehensive proteome analysis of lysine crotonylation in Streptococcus agalactiae, a pathogen causing meningoencephalitis in teleosts.
Article in Proteome science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Crotonylation driving Streptococcus pneumoniae adaption and virulence.Journal of advanced research · 2026Article
- Lysine crotonylation in disease: mechanisms, biological functions and therapeutic targets.Epigenetics & chromatin · 2025Review
- Protein lysine crotonylation in cellular processions and disease associations.Genes & diseases · 2024Review
- Systematic analysis of lysine crotonylation in human macrophages responding to MRSA infection.Frontiers in cellular and infection microbiology · 2023Article
- Glycine-rich RNA-binding cofactor RZ1AL is associated with tomato ripening and development.Horticulture research · 2022Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
backgroudStreptococcus 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.
methodsIn 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.
resultsIn 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.
conclusionsThese data provide a promising starting point for further functional research of crotonylation in bacterial virulence in S. agalactiae.
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