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Glycoprotein B (gB), the primary mediator of membrane fusion during viral entry, is a key target for neutralizing antibody (nAb) and vaccine development. In this study, we determined a 2.8 \u00c5 cryo-EM structure of the HHV-6B gB ectodomain in its postfusion conformation, unveiling unique N-terminal features and resolving the furin site for the first time in herpesviruses. Comparative analyses highlighted similarities between HHV-6B gB and gB from human cytomegalovirus (HCMV) and Epstein-Barr virus (EBV), mapping conserved residues across herpesviruses. Cross-binding assays indicated minimal cross-epitope recognition by nAbs from other herpesviruses, while several potential vulnerable sites on HHV-6B gB were identified. These insights advance our understanding of HHV-6B infection mechanisms and support future development of antibodies or vaccines targeting gB.<\/jats:p>","DOI":"10.1371\/journal.ppat.1013300","type":"journal-article","created":{"date-parts":[[2025,7,9]],"date-time":"2025-07-09T17:39:43Z","timestamp":1752082783000},"page":"e1013300","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":3,"title":["Human herpesvirus 6B glycoprotein B postfusion structure, vulnerability mapping, and receptor 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