Staphylococcus saprophyticus is a uropathogenic bacteria responsible for acute urinary tract infections (UTIs) mainly in young female patients. Patients suffering from urinary catheterization, pregnant patients, the elderly as well as those with nosocomial UTIs are at greater risk of the colonizing S. saprophyticus infection. The causative factors include benign prostatic hyperplasia, indwelling catheter, neurogenic bladder, pregnancy, and history of frequent UTIs. Recent findings have exhibited that S. saprophyticus is resistant to several antimicrobial agents. Moreover, there is a global concern regarding the increasing level of antimicrobial resistance, which leads to treatment failure and reduced effectiveness of broad-spectrum antimicrobials. Therefore, a novel approach is being utilized to combat resistant microbes since the past few years. Subtractive proteome analysis has been performed with the entire proteome of S. saprophyticus strain American Type Culture Collection (ATCC) 15305 using several bioinformatics servers and software. The proteins that were non-homologous to humans and bacteria were identified for metabolic pathway analysis. Only four cytoplasmic proteins were found possessing the potential of novel drug target candidates. The development of innovative therapeutic agents by targeting the inhibition of any essential proteins may disrupt the metabolic pathways specific to the pathogen, thus causing destruction as well as eradication of the pathogen from a particular host. The identified targets can facilitate in designing novel and potent drugs against S. saprophyticus strain ATCC 15305.

Coronavirus disease 2019 (COVID-19) associated pneumonia caused by severe acute respiratory coronavirus 2 (SARS-COV-2) was first reported in Wuhan, China in December 2019. Till date, no vaccine or completely effective drug is available to cure COVID-19. Therefore, an effective vaccine against SARS-COV-2 is crucially needed. This study was conducted to design an effective multiepitope based vaccine (MEV) against SARS-COV-2. Seven antigenic proteins were taken as targets and different epitopes (B-cell, T-cell and IFN-γ inducing) were predicted. Highly antigenic and overlapping epitopes were shortlisted. Selected epitopes indicated significant interactions with the HLA-binding alleles and 99.29% coverage of the world’s population. Finally, 505 amino acids long MEV was designed by connecting sixteen MHC class I and eleven MHC class II epitopes with suitable linkers and adjuvant. Linkers and adjuvant were added to enhance the immunogenicity response of the MEV. The antigenicity, allergenicity, physiochemical properties and structural details of MEV were analyzed in order to ensure safety and immunogenicity. MEV construct was non-allergenic, antigenic, stable and flexible. Molecular docking followed by molecular dynamics (MD) simulation analysis, demonstrated a stable and strong binding affinity of MEV with human pathogenic toll-like receptors (TLR), TLR3 and TLR8. Codon optimization and in silico cloning of MEV ensured increased expression in the Escherichia coli K-12 system. Designed MEV in present study could be a potential candidate for further vaccine production process against COVID-19. However, to ensure its safety and immunogenic profile, the proposed MEV needs to be experimentally validated.

Purpose: Crimean-Congo hemorrhagic fever virus (CCHFV), a single-stranded RNA (ssRNA) virus that spreads via tick bites. For the treatment of CCHFV, there is still a lack of vaccine or any antiviral medicine. For this purpose, a study was performed to design a multiepitope based subunit vaccine (MESV) for effective prevention against CCHFV infection. Methodology: The study contains immunoinformatic and docking methodologies to obtain a MESV by choosing highly antigenic and overlapping epitopes comprising of 8 epitopes of both MHC class I and II from viral proteins. Epitopes were chosen which were conserved within the epitopes of IFN- gamma, T-cell and B-cell. Then these epitopes were joined to final peptide by GPGPG and AAY linkers. An adjuvant was added at N terminal of vaccine via EAAAK linker for the improvement of vaccine’s immunogenicity. Findings: Our final construct was comprised of 278 amino acids. To validate the vaccine’s immunogenicity and safety, its physiochemical properties, allergenicity as well as antigenicity were checked and it was predicted to be non-allergenic and antigenic. The construct was further analyzed by molecular docking within vaccine and TLR3 receptor to assure its molecular interaction and binding affinity. In the end, In-silico cloning was also carried out for ensuring its expression efficiency. Recommendations: Nonetheless, the designed construct is proposed to be tested in laboratory settings to confirm its immunogenicity and safety.