Background. Worldwide, Neisseria gonorrhoeae-related sexually transmitted infections (STIs) continue to be of significant public health concern. This obligate-human pathogen has developed a number of defenses against both innate and adaptive immune responses during infection, some of which are mediated by the pathogen’s proteins. Hence, the uncharacterized proteins of N. gonorrhoeae can be annotated to get insight into the unique functions of this organism related to its pathogenicity and to find a more efficient therapeutic target. Methods. In this study, a hypothetical protein (HP) of N. gonorrhoeae was chosen for analysis and an in-silico approach was used to explore various properties such as physicochemical characteristics, subcellular localization, secondary structure, 3D structures, and functional annotation of that HP. Finally, a molecular docking analysis was performed to design an epitope-based vaccine against that HP. Results. This study has identified the potential role of the chosen HP of N. gonorrhoeae 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 have 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 leukocyte antigen HLA-B ∗ 15 : 01. Conclusions. The in-silico characterization of this protein will help us understand molecular mechanism of action of N. gonorrhoeae 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.

Background. Although the monkeypox virus-associated illness was previously confined to Africa, recently, it has started to spread across the globe and become a significant threat to human lives. Hence, this study was designed to identify the B and T cell epitopes and develop an epitope-based peptide vaccine against this virus’s cell surface binding protein through an in silico approach to combat monkeypox-associated diseases. Results. The analysis revealed that the cell surface binding protein of the monkeypox virus contains 30 B cell and 19 T cell epitopes within the given parameter. Among the T cell epitopes, epitope “ILFLMSQRY” was found to be one of the most potential peptide vaccine candidates. The docking analysis revealed an excellent binding affinity of this epitope with the human receptor HLA-B ∗ 15:01 with a very low binding energy (-7.5 kcal/mol). Conclusion. The outcome of this research will aid the development of a T cell epitope-based peptide vaccine, and the discovered B and T cell epitopes will facilitate the creation of other epitope and multi-epitope-based vaccines in the future. This research will also serve as a basis for further in vitro and in vivo analysis to develop a vaccine that is effective against the monkeypox virus.

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.