溶藻弧菌
毒力
乙酰化
赖氨酸
病菌
生物
微生物学
人类病原体
生物化学
氨基酸
细菌
弧菌
基因
遗传学
作者
Hongxi Pang,Wanxin Li,Weijie Zhang,Shujie Zhou,Rowena Hoare,Sean J. Monaghan,Jichang Jian,Xiangmin Lin
标识
DOI:10.1016/j.jprot.2019.103543
摘要
It is well known that lysine acetylation (Kace) modification is a common post-translational modification (PTM) that plays an important role in multiple biological and pathological functions in bacteria. However, few studies have focused on lysine acetylation modification in aquatic pathogens to date. In this study, the acetylome profiling of fish pathogen, Vibrio alginolyticus was investigated by combining affinity enrichment with LC MS/MS. A total of 2883 acetylation modification sites on 1178 proteins in this pathogen were identified. The Kace modification of several selected proteins were further validated by Co-immunocoprecipitation combined with Western blotting. Bioinformatics analysis showed that seven conserved motifs can be enriched among Kace peptides, and many of them were significantly enriched in metabolic processes such as biosynthesis of secondary metabolites, microbial metabolism in diverse environments, and biosynthesis of amino acids, which was similar to data previously published for V. parahaemolyticus. Moreover, we found at least 102 acetylation modified proteins predicted as virulence factors, which indicate the important role of PTM on bacterial virulence. In general, our results provide a promising starting point for further investigations of the biological role of lysine acetylation on bacterial virulence in V. alginolyticus. Lysine acetylation (Kace) modification, is well known to play important roles on diverse biological functions in prokaryotic cell, whereas few studies focused on aquatic pathogens to date. In this study, the acetylome profiling of fish pathogen, Vibrio alginolyticus was investigated by combining affinity enrichment with LC MS/MS. A total of 2883 acetylation modification sites on 1178 proteins in this pathogen were identified. The further bioinformatics analysis showed that seven conserved motifs can be enriched among Kace peptides, and many of them were significantly enriched in metabolic processes, which was similar to data previously published for V. parahemolyticus. Moreover, we found at least 102 acetylation modified proteins predicted as virulence factors, which indicate the important role of PTM on bacterial virulence. In general, our results provide a promising starting point for further investigations of the biological role of lysine acetylation on bacterial virulence in V. alginolyticus.
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