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@ARTICLE{Royet:292524,
      author       = {A. Royet and R. Ruedas and L. Gargowitsch and V. Gervais
                      and J. Habersetzer and L. Pieri and M. Ouldali and M.
                      Paternostre and I. Hofmann$^*$ and T. Tubiana and S.
                      Fieulaine and S. Bressanelli},
      title        = {{N}onstructural protein 4 of human norovirus self-assembles
                      into various membrane-bridging multimers.},
      journal      = {The journal of biological chemistry},
      volume       = {300},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {DKFZ-2024-01770},
      pages        = {107724},
      year         = {2024},
      note         = {Volume 300, Issue 9, September 2024, 107724 / Core Facility
                      Antibodies},
      abstract     = {Single-stranded, positive-sense RNA ((+)RNA) viruses
                      replicate their genomes in virus-induced intracellular
                      membrane compartments. (+)RNA viruses dedicate a significant
                      part of their small genomes (a few thousands to a few tens
                      of thousands of bases) to the generation of these
                      compartments by encoding membrane-interacting proteins
                      and/or protein domains. Noroviruses are a very diverse genus
                      of (+)RNA viruses including human and animal pathogens.
                      Human noroviruses are the major cause of acute
                      gastroenteritis worldwide, with genogroup II genotype 4
                      (GII.4) noroviruses accounting for the vast majority of
                      infections. Three viral proteins encoded in the N-terminus
                      of the viral replication polyprotein direct intracellular
                      membrane rearrangements associated with norovirus
                      replication. Of these three, nonstructural protein 4 (NS4)
                      seems to be the most important, although its exact functions
                      in replication organelle formation are unknown. Here we
                      produce, purify and characterize GII.4 NS4. AlphaFold
                      modeling combined with experimental data refine and correct
                      our previous crude structural model of NS4. Using simple
                      artificial liposomes, we report an extensive
                      characterization of the membrane properties of NS4. We find
                      that NS4 self-assembles and thereby bridges liposomes
                      together. Cryo-EM, NMR and membrane flotation show formation
                      of several distinct NS4 assemblies, at least two of them
                      bridging pairs of membranes together in different fashions.
                      Noroviruses belong to (+)RNA viruses whose replication
                      compartment is extruded from the target endomembrane and
                      generates double-membrane vesicles. Our data establish that
                      the 21-kDa GII.4 human norovirus NS4 can, in the absence of
                      any other factor, recapitulate in tubo several features,
                      including membrane apposition, that occur in such
                      processes.},
      keywords     = {Cryo-electron microscopy (Other) / Lipid-protein
                      interaction (Other) / Liposome (Other) / Membrane (Other) /
                      Nonstructural protein (Other) / Norovirus (Other) /
                      Plus-stranded RNA virus (Other) / Protein assembly (Other) /
                      Viral protein (Other) / Viral replication (Other)},
      cin          = {A190},
      ddc          = {540},
      cid          = {I:(DE-He78)A190-20160331},
      pnm          = {311 - Zellbiologie und Tumorbiologie (POF4-311)},
      pid          = {G:(DE-HGF)POF4-311},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39214299},
      doi          = {10.1016/j.jbc.2024.107724},
      url          = {https://inrepo02.dkfz.de/record/292524},
}