In silico design of ferritin-EBV gp۳۵۰ nanoparticle vaccine

BACKGROUND AND OBJECTIVESThe Epstein-Barr virus (EBV) is related to the emergence of different malignancies such as Infectious Mononucleosis (IM) and epithelial cell malignancies. The prevention of EBV infection and the management of EBV-related diseases have been proposed to be achievable through prophylactic and therapeutic vaccination. For the past two decades, researchers have studied the major envelope protein gp۳۵۰ in EBV vaccinations. This protein attaches to B cells through complement receptor ۲ (CR۲/CD۲۱). Despite years of research, there is no available licensed vaccine for EBV, one of the latest attempts in this field is the ferritin nanoparticle vaccine designed by Kanekiyo et al. In this study, a ferritin-based nanoparticle vaccine that represents gp۳۵۰ was computationally designed.MATERIALS AND METHODSThe structure of gp۳۵۰ protein “۲h۶o” was selected from PDB, and the structure of ferritin protein is sourced from Masoomi et al. HADDOCK ۲.۴ server was employed for the molecular docking of ferritin-gp۳۵۰. PyMol molecular viewer was used to examine the clusters.RESULTS AND DISCUSSIONMolecular docking results are shown in ۱۰ clusters. The cluster that had the best positioning of gp۳۵۰ on ferritin, along with a low RMSD (۰.۷ +/- ۰.۵) and HADDOCK score (-۱۴.۱ +/- ۱۸.۸), Electrostatic energy (-۴۸۸.۷ +/- ۶۷.۲), Z- score (-۲.۴) is presented here as the top molecular docking outcome.CONCLUSION In this study, a structure was chosen, which is the best molecular docking structure of the gp۳۵۰ protein, which is located in the vertical position of ferritin and has better accessibility for CR۲. The binding sites of gp۳۵۰ to ferritin were investigated and it was shown that the sites required for binding of gp۳۵۰ to CR۲ protein are free for binding, which facilitates antigen presentation and self-assembly of ferritin nanocages.