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| Title | Human herpesvirus 6B glycoprotein B postfusion structure, vulnerability mapping, and receptor recognition. |
|---|---|
| Journal, issue, pages | PLoS Pathog, Vol. 21, Issue 7, Page e1013300, Year 2025 |
| Publish date | Jul 9, 2025 |
Authors | Chu Xie / Xin-Yan Fang / Yuan-Tao Liu / Xian-Shu Tian / Lan-Yi Zhong / Pei-Huang Wu / Hang Zhou / Peng-Lin Li / Yan-Lin Yang / Zi-Ying Jiang / Sen-Fang Sui / Zheng Liu / Mu-Sheng Zeng / Cong Sun / ![]() |
| PubMed Abstract | Human herpesvirus 6B (HHV-6B), a β-herpesvirus that significantly threatens immunocompromised individuals, currently lacks targeted antiviral therapies or vaccines. Glycoprotein B (gB), the primary ...Human herpesvirus 6B (HHV-6B), a β-herpesvirus that significantly threatens immunocompromised individuals, currently lacks targeted antiviral therapies or vaccines. 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 Å 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. |
External links | PLoS Pathog / PubMed:40632757 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 2.84 Å |
| Structure data | EMDB-61589, PDB-9jli: |
| Chemicals | ![]() ChemComp-NAG: |
| Source |
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Keywords | VIRAL PROTEIN / HHV6B / gB |
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Human gammaherpesvirus 8
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