Unveiling a Novel Barstar Protein: In Silico Analysis of Hypothetical Protein WP_۳۱۱۰۰۸۵۳۳.۱ from Shigella boydii Reveals Its Role as an Intracellular Inhibitor of Barnase

Shigella boydii, a major cause of shigellosis, poses significant health risks in regions like Asia and Africa. Hypothetical proteins in this pathogen, such as WP_۳۱۱۰۰۸۵۳۳.۱, are poorly characterized but may serve as potential therapeutic targets. This study aims to annotate and characterize the structural and functional properties of WP_۳۱۱۰۰۸۵۳۳.۱ from S. boydii. The protein was analyzed using bioinformatics tools, including CELLO, PSORTb, and SOSUIGramN for subcellular localization, and domain and motif analysis for functional annotation. Secondary structure analysis and ۳D structure prediction were performed using AlphaFold۲, followed by quality evaluation with PROCHECK, ERRAT, VERIFY۳D, and QMEAN. Energy minimization was conducted using YASARA, and the active site was identified with CASTp. The protein was identified as a cytoplasmic Barstar, an intracellular inhibitor of Barnase, with a secondary structure dominated by α-helices. The ۳D structure, predicted at ۹۹% sequence identity to a Barnase inhibitor (PDB ID: AF-A۰A۸۲۹A۹B۴-F۱-v۴), showed high stability and a validated active site suitable for drug targeting. The findings suggest that WP_۳۱۱۰۰۸۵۳۳.۱ plays a critical role in bacterial survival by inhibiting Barnase. Disrupting this function could weaken the bacterium’s defense mechanisms, potentially enhancing endotoxin efficacy. The annotation and structural characterization of WP_۳۱۱۰۰۸۵۳۳.۱ as a Barstar inhibitor provide insights into its role in S. boydii. Targeting its function may enable novel therapeutic strategies to combat shigellosis by enhancing endotoxin activity.

کلیدواژه ها:

Food-borne diseases ، Bioinformatics tools ، Functional annotation ، Antimicrobial interventions ، Gastrointestinal infections