9JLI

Structure of HHV6B glycoprotein B

Summary for 9JLI

• Entry DOI: 10.2210/pdb9jli/pdb
• EMDB information: 61589
• Descriptor: Envelope glycoprotein B, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• Functional Keywords: hhv6b, gb, viral protein
• Biological source: Human herpesvirus 6 strain Z29
• Total number of polymer chains: 3
• Total formula weight: 218954.21

Authors

Fang, X.Y.,Xie, C.,Sun, C.,Zeng, M.S.,Liu, Z. (deposition date: 2024-09-19, release date: 2025-06-25, Last modification date: 2026-01-21)

Primary citation

Xie, C.,Fang, X.Y.,Liu, Y.T.,Tian, X.S.,Zhong, L.Y.,Wu, P.H.,Zhou, H.,Li, P.L.,Yang, Y.L.,Jiang, Z.Y.,Sui, S.F.,Liu, Z.,Zeng, M.S.,Sun, C.
Human herpesvirus 6B glycoprotein B postfusion structure, vulnerability mapping, and receptor recognition.
Plos Pathog., 21:e1013300-e1013300, 2025

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 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.

PubMed: 40632757
DOI: 10.1371/journal.ppat.1013300

Experimental method

ELECTRON MICROSCOPY (2.84 Å)