ArticlePLoS pathogens2025
Human herpesvirus 6B glycoprotein B postfusion structure, vulnerability mapping, and receptor recognition.
Article in PLoS pathogens, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
1 citing paper in PubMed.
- Progress and prospects for herpesvirus vaccination using gB antigens.Frontiers in immunology · 2026Review
Corrections and comments
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Authors and funding
14 authors.
Funding
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 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.
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Registered trials
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