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@ARTICLE{Williams:602551,
      author       = {Williams, Harry and Thorkelsson, Sigurdur R and Vogel,
                      Dominik and Milewski, Morlin and Busch, Carola and Cusack,
                      Stephen and Gruenewald, Kay and Quemin, Emmanuelle and
                      Rosenthal, Maria},
      title        = {{S}tructural insights into viral genome replication by the
                      severe fever with thrombocytopenia syndrome virus {L}
                      protein},
      journal      = {Nucleic acids symposium series},
      volume       = {51},
      number       = {3},
      issn         = {0305-1048},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press},
      reportid     = {PUBDB-2024-00649},
      pages        = {1424 - 1442},
      year         = {2023},
      note         = {part of this work was performed at the Cryo-EM multi-user
                      Facility at CSSB, headed by K.G. and sup-ported by the UHH
                      and DFG [INST 152/772-1, 774-1, 775-1, 776-1];},
      abstract     = {Severe fever with thrombocytopenia syndrome virus (SFTSV)
                      is a phenuivirus that has rapidly become endemic in several
                      East Asian countries. The large (L) protein of SFTSV, which
                      includes the RNA-dependent RNA polymerase (RdRp), is
                      responsible for catalysing viral genome replication and
                      transcription. Here, we present 5 cryo-electron microscopy
                      (cryo-EM) structures of the L protein in several states of
                      the genome replication process, from pre-initiation to
                      late-stage elongation, at a resolution of up to 2.6 Å. We
                      identify how the L protein binds the 5′ viral RNA in a
                      hook-like conformation and show how the distal 5′ and 3′
                      RNA ends form a duplex positioning the 3′ RNA terminus in
                      the RdRp active site ready for initiation. We also observe
                      the L protein stalled in the early and late stages of
                      elongation with the RdRp core accommodating a 10-bp
                      product-template duplex. This duplex ultimately splits with
                      the template binding to a designated 3′ secondary binding
                      site. The structural data and observations are complemented
                      by in vitro biochemical and cell-based mini-replicon assays.
                      Altogether, our data provide novel key insights into the
                      mechanism of viral genome replication by the SFTSV L protein
                      and will aid drug development against segmented
                      negative-strand RNA viruses.},
      cin          = {CSSB-LIV-KG},
      ddc          = {540},
      cid          = {I:(DE-H253)CSSB-LIV-KG-20220525},
      pnm          = {899 - ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-899},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:36651274},
      UT           = {WOS:000914839600001},
      doi          = {10.1093/nar/gkac1249},
      url          = {https://bib-pubdb1.desy.de/record/602551},
}