| Popis: |
Background The threat of sexually transmitted diseases (STDs) is a significant public health concern. Blood, sperm, vaginal, and other bodily fluids can transport bacteria, viruses, and parasites that cause sexually transmitted diseases from one person to another. Neisseria gonorrhoeae is one of the microorganisms responsible for sexually transmitted diseases (STDs). It is an aerobic gram-negative bacterium with a large genome that contains numerous proteins, some of which are considered hypothetical. Methods In this study, the hypothetical protein of Neisseria gonorrhoeae F0T10 13280 was chosen for analysis and used an in-silico approach to explore various properties such as physicochemical characteristics, subcellular localization, secondary structure, 3D structures, and functional annotation. Finally, a molecular docking analysis was performed to design an epitope-based vaccine against this protein. Results This study has identified the potential role of the HP in plasmid transfer, cell cycle control, cell division, and chromosome partitioning. Acidic nature, thermal stability, cytoplasmic localization of the protein and some of its other physicochemical properties has also been identified through this study. Molecular docking analysis has demonstrated that one of the T cell epitopes of the protein has a significant binding affinity with the human leucocyte antigen HLA-B*3501. Conclusions The in-silico characterization of this protein will help us understand its molecular mechanism of action and get an insight into novel therapeutic identification processes. This research will, therefore, enhance our knowledge to find new medications to tackle this potential threat to humankind. |
