{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,21]],"date-time":"2026-10-21T21:38:50Z","timestamp":1792618730898,"version":"4.5.0"},"reference-count":23,"publisher":"Wiley","issue":"9","license":[{"start":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T00:00:00Z","timestamp":1788998400000},"content-version":"vor","delay-in-days":9,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Journal of Medical Virology"],"published-print":{"date-parts":[[2026,9]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Rabies is a fatal zoonotic disease caused by rabies virus (RABV), resulting in approximately 59,000 deaths annually worldwide and posing a serious threat to public health. The RABV phosphoprotein (P protein) plays crucial roles in viral replication, transcription, and immune antagonism; however, its immunogenic properties have not been fully characterized. In this study, the RABV P protein was expressed in an\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    expression system and used to immunize mice, resulting in the generation of six P protein\u2010specific monoclonal antibodies (mAbs). Using an overlapping peptide\u2010based truncation strategy, two linear B\u2010cell epitopes were identified:\n                    <jats:sup>52<\/jats:sup>\n                    DMKRLHLDDEKSSNL\n                    <jats:sup>66<\/jats:sup>\n                    and\n                    <jats:sup>177<\/jats:sup>\n                    VAPGPPALEWSATNE\n                    <jats:sup>191<\/jats:sup>\n                    . Alanine\u2010scanning mutagenesis revealed that residues D52, M53, R55, L56, and L58 were critical for the recognition of epitope\n                    <jats:sup>52<\/jats:sup>\n                    DMKRLHLDDEKSSNL\n                    <jats:sup>66<\/jats:sup>\n                    by mAbs 2D2 and 18G7. Residues G180, P181, and W186 were essential for recognition of epitope\n                    <jats:sup>177<\/jats:sup>\n                    VAPGPPALEWSATNE\n                    <jats:sup>191<\/jats:sup>\n                    by mAbs 3D7, 15D8, 16D3, and 16C6. Notably, although some amino acid residues within epitopes P1\u20105 and P4\u20102 exhibited high variability among representative RABV strains, the critical residues recognized by these monoclonal antibodies were highly conserved. These findings provide new insights into the antigenic structure of the RABV P protein and may contribute to future studies on its functional characterization, as well as the development of P protein\u2010based diagnostic reagents and subunit vaccines.\n                  <\/jats:p>","DOI":"10.1002\/jmv.71124","type":"journal-article","created":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T12:30:31Z","timestamp":1789043431000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Development and Epitope Characterization of Monoclonal Antibodies Targeting the Rabies Virus P Protein"],"prefix":"10.1002","volume":"98","author":[{"given":"Chao","family":"Liang","sequence":"first","affiliation":[{"name":"School of Life Sciences Zhengzhou University Zhengzhou Henan People's Republic of China"},{"name":"Longhu Laboratory of Advanced Immunology Zhengzhou Henan People's Republic of China"},{"name":"Henan Provincial Key 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