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@ARTICLE{Mallagaray:224307,
      author       = {Mallagaray, Alvaro and Lockhauserbäumer, Julia and
                      Hansman, Grant and Uetrecht, Charlotte and Peters, Thomas},
      title        = {{A}ttachment of {N}orovirus to {H}isto {B}lood {G}roup
                      {A}ntigens: {A} {C}ooperative {M}ultistep {P}rocess},
      journal      = {Angewandte Chemie / International edition},
      volume       = {54},
      number       = {41},
      issn         = {1433-7851},
      address      = {Weinheim},
      publisher    = {Wiley-VCH},
      reportid     = {PUBDB-2015-03498},
      pages        = {12014 – 12019},
      year         = {2015},
      abstract     = {Human noroviruses recognize histo blood group antigens
                      (HBGAs) as cellular attachment factors. Recently, it has
                      been discovered that norovirus infection can be
                      significantly enhanced by HBGA binding. Yet the attachment
                      process and how it promotes host-cell entry is only poorly
                      understood. The binding of a norovirus protruding (P) domain
                      of a predominant GII.4 Saga strain to HBGAs at atomic
                      resolution was studied. So far, independent and equivalent
                      multiple binding sites were held responsible for attachment.
                      Using NMR experiments we show that norovirus-HBGA binding is
                      a cooperative multi-step process, and native mass
                      spectrometry reveals four instead of two HBGA binding sites
                      per P-dimer. An accompanying crystallographic study has
                      disclosed four instead of two l-fucose binding sites per
                      P-dimer of a related GII.10 strain1 further supporting our
                      findings. We have uncovered a novel paradigm for
                      norovirus-HBGA recognition that will inspire further studies
                      into norovirus–host interactions.},
      cin          = {Eur.XFEL},
      ddc          = {540},
      cid          = {$I:(DE-H253)Eur_XFEL-20120731$},
      pnm          = {6G13 - XFEL (POF3-622)},
      pid          = {G:(DE-HGF)POF3-6G13},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000363396000020},
      pubmed       = {pmid:26329854},
      doi          = {10.1002/anie.201505672},
      url          = {https://bib-pubdb1.desy.de/record/224307},
}