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@ARTICLE{Zhou:613890,
      author       = {Zhou, Momei and Vollmer, Benjamin and Machala, Emily and
                      Chen, Muyuan and Grünewald, Kay and Arvin, Ann M. and Chiu,
                      Wah and Oliver, Stefan L.},
      title        = {{T}argeted mutagenesis of the herpesvirus fusogen central
                      helix captures transition states},
      journal      = {Nature Communications},
      volume       = {14},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {PUBDB-2024-05669},
      pages        = {7958},
      year         = {2023},
      abstract     = {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
                      $^{526}$EHV$^{528}$. 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.},
      cin          = {CSSB-LIV-KG},
      ddc          = {500},
      cid          = {I:(DE-H253)CSSB-LIV-KG-20220525},
      pnm          = {899 - ohne Topic (POF4-899) / DFG project 390874280 - EXC
                      2155: RESIST - Resolving Infection Susceptibility
                      (390874280)},
      pid          = {G:(DE-HGF)POF4-899 / G:(GEPRIS)390874280},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:38042814},
      UT           = {WOS:001115563700027},
      doi          = {10.1038/s41467-023-43011-w},
      url          = {https://bib-pubdb1.desy.de/record/613890},
}