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Structure paper

TitlePrefusion structure, evasion and neutralization of HSV-1 glycoprotein B.
Journal, issue, pagesNat Microbiol, Vol. 10, Issue 11, Page 2966-2980, Year 2025
Publish dateOct 31, 2025
AuthorsRyan S Roark / Andrew J Schaub / Wei Shi / Maple Wang / Fabiana A Bahna / Jordan E Becker / Andrea Biju / Sue Chong / Haijuan Du / Yicheng Guo / Hsiang Hong / Phinikoula S Katsamba / Seetha M Mannepalli / Adam S Olia / Li Ou / Sarah K Rubin / Yosef Sabo / Mehin Suleiman / Malcolm L Wells / Baoshan Zhang / Cheng Cheng / Anum Glasgow / David D Ho / Yaoxing Huang / Theodore C Pierson / Reda Rawi / Tongqing Zhou / Lawrence Shapiro / Peter D Kwong /
PubMed AbstractGlycoprotein B (gB) refolds between prefusion and postfusion conformations to facilitate herpesvirus entry into host cells. However, the isolation of prefusion-specific neutralizing antibodies, ...Glycoprotein B (gB) refolds between prefusion and postfusion conformations to facilitate herpesvirus entry into host cells. However, the isolation of prefusion-specific neutralizing antibodies, effective against other viral entry machines, has been challenging. Here we describe stabilization of the prefusion gB ectodomain from herpes simplex virus 1 (HSV-1), determine ectodomain structures at 2.9- to 4.1-Å resolution using cryogenic electron microscopy (cryo-EM) and isolate a prefusion-specific gB-neutralizing antibody termed WS.HSV-1.24. Murine immunization with gB stabilized in the prefusion conformation induced high titres of antibodies binding to both prefusion and postfusion gB, but-most notably-without measurable serum neutralization. Accessibility analysis revealed iso-surface exposure, with accessible surfaces on prefusion HSV-1 gB also exposed on postfusion gB. Structural analysis suggested substantial plasticity, with regions that refolded between pre- and postfusion conformations relegated to domain interfaces with limited accessibility; indeed, WS.HSV-1.24 recognized a domain-interface refolding region to facilitate neutralization. We propose that prefusion HSV-1 gB evades neutralization by most antibodies through an iso-surface display that is coupled to structural plasticity.
External linksNat Microbiol / PubMed:41174178 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 4.1 Å
Structure data

46758

9dd6

EMDB-46758, PDB-9dd6:
Cryo-EM structure of neutralizing murine antibody WS.HSV-1.24 in complex with HSV-1 glycoprotein B trimer gB-Ecto.516P.531E
Method: EM (single particle) / Resolution: 3.1 Å

46759

9dd7

EMDB-46759, PDB-9dd7:
Cryo-EM structure of neutralizing human antibody D48 in complex with HSV-1 glycoprotein B trimer gB-Ecto.516P.531E.DS
Method: EM (single particle) / Resolution: 4.1 Å

46760

9dd8

EMDB-46760, PDB-9dd8:
Cryo-EM structure of neutralizing human antibody D48 in complex with HSV-1 glycoprotein B trimer gB-Ecto.516P
Method: EM (single particle) / Resolution: 3.08 Å

46761

9dd9

EMDB-46761, PDB-9dd9:
Cryo-EM structure of neutralizing human antibody D48 in complex with HSV-1 glycoprotein B trimer gB-Ecto.516P.531E
Method: EM (single particle) / Resolution: 3.77 Å

46762

9dda

EMDB-46762, PDB-9dda:
Cryo-EM structure of gB-Ecto.516P.531E.DS, a prefusion-stabilized HSV-1 glycoprotein B extracellular domain
Method: EM (single particle) / Resolution: 2.99 Å

46765

9ddc

EMDB-46765, PDB-9ddc:
Cryo-EM structure of gB-Ecto.516P, an HSV-1 glycoprotein B extracellular domain
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • mus musculus (house mouse)
  • human alphaherpesvirus 1 (Herpes simplex virus type 1)
  • homo sapiens (human)
KeywordsVIRAL PROTEIN / immune complex / neutralization / herpes fusogen / gB trimer / fusogen / postfusion-destabilization / neo-disulfide bond / trimer / postfusion

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