Capsid assembly is regulated by amino acid residues asparagine 47 and 48 in the VP2 protein of porcine parvovirus

Porcine parvovirus (PPV) is a major cause of reproductive failure in swine and has caused substantial losses throughout the world. Viral protein 2 (VP2) PPV structural that can self-assemble into virus-like particles (VLP) with hemagglutination (HA) activity. In order to identify essential residues involved mechanism capsid assembly further understand function HA, we analyzed series deletion mutants site-directed mutations within N-terminal VP2 using Escherichia coli system. Our results showed first 47 amino acids from did not affect assembly, truncation residue 48 Asparagine (Asn, N) detrimental effects. Site-directed mutagenesis experiments demonstrated 47Asn reduced efficiency VLP, while 48Asn destroyed stability, hemagglutination, self-assembly characteristics protein. Results native PAGE inferred macromolecular polymers were critical intermediates during process. mutation at ability monomers form oligomers, but oligomers assemble particles, influencing both HA findings provide valuable information on mechanisms possibility chimeric VLP vaccine development by replacing