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Despite the significant impact of this virus, effective vaccines remain unclear. In this study, we successfully engineered B19V protein nanoparticles by fusing the N\u2010terminal receptor\u2010binding domain corresponding to 5\u201380 amino acids of VP1 with two distinct types of self\u2010assembling protein nanoparticles. Gel filtration and electron microscopic analysis confirmed the spherical assembly of the antigen\u2010fused nanoparticles. The purified nanoparticles are efficiently bound to the surface of UT7\/Epo\u2010S1 cells, which are semi\u2010permissive hosts for B19V infection. Immunization of BALB\/c mice with VP1u 5\u201380 nanoparticles elicited a robust production of B19V\u2010specific IgG antibodies compared to single VP1u 5\u201380 peptides. Moreover, a neutralization assay using B19V derived from a blood donor sample revealed that antibodies from mice immunized with VP1u 5\u201380 nanoparticles exhibited stronger infection\u2010neutralizing activity. These findings suggest that nanoparticle formation plays a crucial role in enhancing the immunogenicity of the B19V VP1u 5\u201380 amino acid peptide and that these nanoparticles could serve as promising vaccine candidates, effectively inducing immunity against B19V.<\/jats:p>","DOI":"10.1111\/1348-0421.13182","type":"journal-article","created":{"date-parts":[[2024,11,15]],"date-time":"2024-11-15T10:44:40Z","timestamp":1731667480000},"page":"35-42","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Efficient Neutralizing Antibodies Induction by Human Parvovirus B19 Epitope\u2010Presenting Protein Nanoparticles"],"prefix":"10.1111","volume":"69","author":[{"given":"Sakika","family":"Kimura","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, Faculty of Agriculture and Life Science Hirosaki University Hirosaki 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