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TitleTargeted mutagenesis of the herpesvirus fusogen central helix captures transition states.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 7958, Year 2023
Publish dateDec 2, 2023
AuthorsMomei Zhou / Benjamin Vollmer / Emily Machala / Muyuan Chen / Kay Grünewald / Ann M Arvin / Wah Chiu / Stefan L Oliver /
PubMed AbstractHerpesviruses remain a burden for animal and human health, including the medically important varicella-zoster virus (VZV). Membrane fusion mediated by conserved core glycoproteins, the fusogen gB and ...Herpesviruses remain a burden for animal and human health, including the medically important varicella-zoster virus (VZV). Membrane fusion mediated by conserved core glycoproteins, the fusogen gB and the heterodimer gH-gL, enables herpesvirus cell entry. The ectodomain of gB orthologs has five domains and is proposed to transition from a prefusion to postfusion conformation but the functional relevance of the domains for this transition remains poorly defined. Here we describe structure-function studies of the VZV gB DIII central helix targeting residues EHV. Critically, a H527P mutation captures gB in a prefusion conformation as determined by cryo-EM, a loss of membrane fusion in a virus free assay, and failure of recombinant VZV to spread in cell monolayers. Importantly, two predominant cryo-EM structures of gB[H527P] are identified by 3D classification and focused refinement, suggesting they represented gB conformations in transition. These studies reveal gB DIII as a critical element for herpesvirus gB fusion function.
External linksNat Commun / PubMed:38042814 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution9.8 - 12.4 Å
Structure data

EMDB-42250: Varicella-zoster virus glycoprotein B; H527P prefusion class I.
Method: EM (subtomogram averaging) / Resolution: 9.8 Å

EMDB-42251: Varicella-zoster virus glycoprotein B; H527P prefusion mutant class II.
Method: EM (subtomogram averaging) / Resolution: 12.4 Å

Source
  • Human alphaherpesvirus 3 (Varicella-zoster virus)

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