Abstract
Bovine parainfluenza virus type 3 (BPIV3) is a significant pathogen implicated in bovine respiratory disease complex (BRDC), leading to lung tissue destruction, immunosuppression, and subsequent bacterial infections in cattle, hence incurring considerable economic losses globally. Notwithstanding its importance, a limited number of commercial vaccinations are presently accessible. The fusion (F) protein and hemagglutinin-neuraminidase (HN) protein, as protective antigens of the Paramyxoviridae family, can elicit neutralizing antibodies and are regarded as optimal candidates for the creation of genetically modified vaccines. A multi-epitope-based peptide vaccine (MEBPV) was developed by immunoinformatics methodologies by choosing epitopes from the F and HN proteins characterized by high antigenicity, moderate toxicity, and limited allergenic potential. The epitopes were combined with suitable linkers and adjuvants to produce the vaccine, whose physicochemical qualities, immunological attributes, solubility, and structural stability were improved and evaluated using computational methods. Molecular docking and molecular dynamics simulations demonstrated the strong potential binding affinity and stability of the vaccination with TLR2, TLR3, and especially TLR4 receptors. Immune simulations forecasted strong humoral and cellular responses, accompanied by a significant elevation in interferon-γ (IFN-γ) production. The vaccine sequence was later cloned into the pET-28a (+) vector for possible expression in Escherichia coli. Despite in silico predictions suggesting a favorable immunogenic potential, additional in vitro and in vivo studies are necessary to confirm its protective efficacy and safety. This research establishes a solid foundation for the creation of safe and efficacious subunit vaccines targeting BPIV3 and presents novel perspectives for the formulation of vaccinations against additional viral infections.