Yang Yong, Tong Mingwei, Bai Xue, Liu Xiaolei, Cai Xuepeng, Luo Xuenong, Zhang Peihao, Cai Wei, Vallée Isabelle, Zhou Yonghua, Liu Mingyuan
Key Laboratory of Zoonosis Research, Ministry of Education, Institute of Zoonosis/College of Veterinary Medicine, Jilin University, Changchun, China.
Wu Xi Medical School, Jiangnan University, Affiliated Hospital of Jiangnan University, Wuxi, China.
Front Microbiol. 2018 Jan 11;8:2674. doi: 10.3389/fmicb.2017.02674. eCollection 2017.
Lysine acetylation is a dynamic and highly conserved post-translational modification that plays a critical role in regulating diverse cellular processes. is a foodborne parasite with a considerable socio-economic impact. However, to date, little is known regarding the role of lysine acetylation in this parasitic nematode. In this study, we utilized a proteomic approach involving anti-acetyl lysine-based enrichment and highly sensitive mass spectrometry to identify the global acetylated proteome and investigate lysine acetylation in . In total, 3872 lysine modification sites were identified in 1592 proteins that are involved in a wide variety of biological processes. Consistent with the results of previous studies, a large number of the acetylated proteins appear to be involved in metabolic and biosynthetic processes. Interestingly, according to the functional enrichment analysis, 29 acetylated proteins were associated with phagocytosis, suggesting an important role of lysine acetylation in this process. Among the identified proteins, 15 putative acetylation motifs were detected. The presence of serine downstream of the lysine acetylation site was commonly observed in the regions surrounding the sites. Moreover, protein interaction network analysis revealed that various interactions are regulated by protein acetylation. These data represent the first report of the acetylome of and provide an important resource for further explorations of the role of lysine acetylation in this foodborne pathogen.
赖氨酸乙酰化是一种动态且高度保守的翻译后修饰，在调节多种细胞过程中发挥关键作用。[某种寄生虫名称]是一种具有重大社会经济影响的食源性寄生虫。然而，迄今为止，关于赖氨酸乙酰化在这种寄生线虫中的作用知之甚少。在本研究中，我们采用了一种蛋白质组学方法，包括基于抗乙酰赖氨酸的富集和高灵敏度质谱分析，以鉴定整体乙酰化蛋白质组并研究[某种寄生虫名称]中的赖氨酸乙酰化。总共在1592种参与多种生物过程的蛋白质中鉴定出3872个赖氨酸修饰位点。与先前研究结果一致，大量乙酰化蛋白质似乎参与代谢和生物合成过程。有趣的是，根据功能富集分析，29种乙酰化蛋白质与吞噬作用相关，表明赖氨酸乙酰化在此过程中起重要作用。在鉴定出的蛋白质中，检测到15个假定的乙酰化基序。在赖氨酸乙酰化位点下游的丝氨酸存在情况在这些位点周围区域普遍可见。此外，蛋白质相互作用网络分析表明，各种相互作用受蛋白质乙酰化调节。这些数据代表了[某种寄生虫名称]乙酰化蛋白质组的首次报道，并为进一步探索赖氨酸乙酰化在这种食源性病原体中的作用提供了重要资源。
