Analysis of binding properties of VP2 protein of Human parvovirus B19 through in silico molecular docking

Human parvovirus B19, a member of the Parvoviridae family, is a pathogen associated with a wide variety of diseases. Most commonly, it causes childhood rash erythema infectiosum, but in some cases more serious symptoms such as persistent arthropathy, critical failures of red cell production causing transient aplastic crisis, this infection in pregnancy causes hydrops fetalis and myocarditis. Traditional immunosuppressive therapy being unsuccessful, anti-viral therapy might be worthy of consideration. Functional annotation would provide role of viral proteome in its survival and pathogenic mechanisms. SVMProt functional family annotations of VP2 protein had deciphered its zinc-binding, coat protein, outer membrane, chlorophyll biosynthesis, DNA repair and calcium-binding nature. VP2 protein is having a key role in viral assembly of B19 virus and being non-homologous to human proteome, it was identified as an attractive molecular target for structure based drug discovery. The VP2 protein crystal structure was energy minimized using CHARMM. A structure based virtual screening method was applied using LigandFit to identify potential inhibitors of VP2 protein from ChemBank database and ten potential Human parvovirus B19 VP2 inhibitors were proposed.