Genome- and proteome-wide analysis of lysine acetylation in Vibrio vulnificus Vv180806 reveals its regulatory roles in virulence and antibiotic resistance

V. vulnificus is an emergent pathogen and causes deadly septicemia in human. Protein acetylation regulates many important biological processes in bacteria. In this study, we identified the first lysine acetylome of V. vulnificus based on the whole-genome sequence of a cefoxitin-resistant strain isolated from a mortality case in China. A total of 6,626 acetylation sites at 1,924 acetylated proteins were uncovered, which to our knowledge represented the largest acetylated protein number that has been identified in bacteria. The presence of acetylation sites in virulence- and antibiotic resistance-related proteins further indicated the important role of acetylated modification on bacterial virulence and antibiotic resistance. Further investigation on the regulatory mechanisms will provide a better understanding of pathogen-host interactions in this increasingly pathogen.