Deciphering the lysine acetylation pattern of leptospiral strains by in silico approach

Leptospirosis, caused by the pathogenic Leptospira, is an emerging zoonotic disease affecting over one million people annually. The existence of a large number of serovars, different reservoir hosts, and common disease symptoms account for the difficulty in early diagnosis, prophylaxis, and treatment. Post-translational modification plays a significant regulatory role in both eukaryotic and prokaryotic organisms. Therefore, the study of post-translational modification may help in better understanding the pathogenesis of the bacterial disease. Acetylation at lysine residue was found to be involved in regulating bacterial pathogenesis. This study aims to identify protein lysine acetylation patterns among groups of pathogenic and saprophytic species of Leptospira, by screening the leptospiral proteome using a robust proteomics approach. In this study, a total of 15, 78,796 acetylated proteins with 83, 65,945 acetylation sites were identified among 469 strains of Leptospira to predict the pathogenesis pattern and signature peptide sequence, which was conserved among pathogenic Leptospira species, that can be used as a novel vaccine candidate. A similar pattern of acetylation was observed among the pathogenic and intermediate groups while different in the saprophytic group of Leptospira. Consequently, a common signature peptide was observed among pathogenic strains of Leptospira. Acetylated proteins were found to be primarily involved in metabolic processes. As a result, this is the first study to analyze proteome-wise strain specific lysine acetylation of Leptospiral proteins which may constitute a valuable resource for in-depth studies of the impact of lysine acetylation in the pathogenesis of Leptospira.