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@ARTICLE{Vollmer:637726,
      author       = {Vollmer, Benjamin and Ebel, Henriette and Rees, Renate and
                      Nentwig, Julia and Mulvaney, Thomas and Schünemann, Jürgen
                      and Krull, Jens and Topf, Maya and Görlich, Dirk and
                      Gruenewald, Kay},
      title        = {{A} nanobody specific to prefusion glycoprotein {B}
                      neutralizes {HSV}-1 and {HSV}-2},
      journal      = {Nature},
      volume       = {646},
      number       = {8084},
      issn         = {0028-0836},
      address      = {London [u.a.]},
      publisher    = {Nature Publ. Group},
      reportid     = {PUBDB-2025-03899},
      pages        = {433 - 441},
      year         = {2025},
      abstract     = {The nine human herpesviruses, including herpes simplex
                      virus 1 and 2, human cytomegalovirus and Epstein–Barr
                      virus, present a significant burden to global public
                      health1. Their envelopes contain at least ten different
                      glycoproteins, which are necessary for host cell tropism,
                      attachment and entry2. The best conserved among them,
                      glycoprotein B (gB), is essential as it performs membrane
                      fusion by undergoing extensive rearrangements from a
                      prefusion to postfusion conformation. At present, there are
                      no antiviral drugs targeting gB or neutralizing antibodies
                      directed against its prefusion form, because of the
                      difficulty in structurally determining and using this
                      metastable conformation. Here we show the isolation of
                      prefusion-specific nanobodies, one of which exhibits strong
                      neutralizing and cross-species activity. By mutational
                      stabilization we solved the herpes simplex virus 1 gB
                      full-length prefusion structure, which allowed the bound
                      epitope to be determined. Our analyses show the
                      membrane-embedded regions of gB and previously unresolved
                      structural features3,4, including a new fusion loop
                      arrangement, providing insights into the initial
                      conformational changes required for membrane fusion. Binding
                      an epitope spanning three domains, proximal only in the
                      prefusion state, the nanobody keeps wild-type HSV-2 gB in
                      this conformation and enabled its native prefusion structure
                      to be determined. This also indicates the mode of
                      neutralization and an attractive avenue for antiviral
                      interventions.},
      cin          = {CSSB-LIV-KG / CSSB-LIV/UKE-MT},
      ddc          = {500},
      cid          = {I:(DE-H253)CSSB-LIV-KG-20220525 /
                      $I:(DE-H253)CSSB-LIV_UKE-MT-20220525$},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633)},
      pid          = {G:(DE-HGF)POF4-633},
      experiment   = {EXP:(DE-H253)ALFM-20250101 / EXP:(DE-H253)cryo-EM-20250101
                      / EXP:(DE-H253)SPC-20250101},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1038/s41586-025-09438-5},
      url          = {https://bib-pubdb1.desy.de/record/637726},
}