Dissecting post-translational modifications in Leptospira proteome to elucidate novel insights into pathogen-host interaction using bioinformatics approach

ABSTRACT: Leptospirosis is a zoonotic disease caused by Leptospira spp. that cause serious health burden. Humans are accidental host gets infected from water contaminated with Leptospira from urine of reservoir hosts like rodents and other mammals. Currently there is no effective vaccine available for leptospirosis. Investigations on post-translational modifications (PTMs) provide insights into the bacterial pathophysiology and functional consequences during bacterial infection and that can provide significant contribution in the search for better vaccine candidates. PTMs are decisive factors in the structure, function, and localization of proteins in both prokaryotic and eukaryotic organisms. In our previous investigations, we have identified PXD016204 (Thoduvayil et al., 2020) and PXD026044 (Sarma et al., 2021) from Leptospira interrogans serovar Copenhageni (strain Fiocruz L1-130). In this project, a systematic reanalysis of unassigned spectra were carried out from our previous total proteome data (PXD016204 and PXD026044) for multi-PTM analysis. We have identified a total of 3,693 unique high-confidence PTM sites corresponding to 1,266 proteins (PTM-Pro probability cut-off value is ≥75%). There were two objectives for the study. The first objective was the functional characterization of PTM proteins, through the identification of protein-protein interactions (PPI). This will enable us to understand the type and functions of PTMs. This analysis was supported by additional characteristics like gene ontology (GO), cluster of autologous groups (COG), other protein features and functions. The second objective was to find the relationship of PTMs with the subcellular localization of leptospiral proteins. We have analyzed the PTM containing proteins identified in Triton X-114 fractions and used the iBAQ values and number of PTM containing peptides that correlate with the sub-cellular localization of leptospiral proteins.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Leptospira Interrogans Serovar Copenhageni Str. Fiocruz L1-130

DISEASE(S): Leptospirosis

SUBMITTER: Madathiparambil G. Madanan  

LAB HEAD: Madathiparambil G. Madanan

PROVIDER: PXD030370 | Pride | 2022-08-12

REPOSITORIES: Pride