Acetylome Analysis in Vibrio vulnificus MO6-24/O Reveals Extensive Lysine Acetylation in Carbon Metabolism and Protein Synthesis Pathways: A Pilot Study.

Vibrio vulnificus (V. vulnificus) is a type of bacterium commonly found in estuarine environments. It can cause necrotizing wound infections and sepsis, both of which are associated with high mortality rates. Protein lysine acetylation is a widespread post-translational modification (PTM) of proteins, and it participates in numerous cellular processes, including regulation, in bacteria. However, the finer landscape of lysine acetylation in V. vulnificus remains unexplored. In this study, acetylated proteins with low cellular abundance were enriched from V. vulnificus MO6-24/O using anti-acetyl-lysine immunoprecipitation and identified using LC-MS/MS, and the acetylation was further confirmed by Western blot analysis. We mapped 2035 lysine acetylation sites to 841 proteins, accounting for approximately 18.5% of the entire protein sequence of V. vulnificus MO6-24/O. Comprehensive bioinformatic characterization of the acetylome indicated that lysine acetylation is associated with metabolic regulation, particularly targeting enzymes regulating carbon metabolic functions and biosynthesis. In addition, sequence motif analysis identified two conserved patterns surrounding acetylated lysines: enrichment of lysine or arginine residues at the +4/+5 positions, and a preference for tyrosine, histidine, or phenylalanine residues at the -1/+1 positions. Furthermore, analysis of the protein-protein interaction network indicated that lysine acetylation influences numerous molecular interactions among proteins. Collectively, this acetylome investigation establishes a foundation for future studies aimed at elucidating physiological functions of protein lysine acetylation in V. vulnificus.