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Our study panned and screened the phage\u2010display antibody library constructed from the peripheral blood mononuclear cell (PBMC) from three SFTSV\u2010infected convalescent patients. Human monoclonal antibodies (hmAbs) targeting SFTSV glycoprotein N (Gn) were isolated from the library and evaluated for binding, affinity, and neutralizing activities in vitro. Epitope identification was performed by structural model analysis, immunofluorescence and RT\u2010qPCR. The results showed that hmAb B36 is a Gn\u2010binding, moderately high affinity, neutralizing antibody. Moreover, hmAb B36 recognizes a conformational epitope formed by six residues on the domain\u2160of the SFTSV Gn, which differs from the epitope previously reported. Among these residues, G114, L155, and S158 were identified as key sites for hmAb B36\u2010mediated recognition. This study performed isolation and identification of a novel neutralizing antibody, offering insights for the future development of therapeutic antibody cocktails and vaccines against SFTSV.<\/jats:p>","DOI":"10.1002\/jmv.71111","type":"journal-article","created":{"date-parts":[[2026,8,21]],"date-time":"2026-08-21T11:44:08Z","timestamp":1787312648000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Discovery and Identification of a Novel Human Monoclonal Neutralizing Antibody Targeting Domain \u2160 of Severe Fever With Thrombocytopenia Syndrome Virus Gn"],"prefix":"10.1002","volume":"98","author":[{"given":"Lin","family":"Wang","sequence":"first","affiliation":[{"name":"Shandong Medical and Pharmaceutical University Yantai China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuanni","family":"Liu","sequence":"additional","affiliation":[{"name":"Yantai Qishan Hospital Yantai 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