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  1. Article

    Open Access

    Sialoglycan binding triggers spike opening in a human coronavirus

    Coronavirus spike proteins mediate receptor binding and membrane fusion, making them prime targets for neutralizing antibodies. In the cases of severe acute respiratory syndrome coronavirus, severe acute respi...

    Matti F. Pronker, Robert Creutznacher, Ieva Drulyte, Ruben J. G. Hulswit in Nature (2023)

  2. Article

    Open Access

    Distinct dissociation rates of murine and human norovirus P-domain dimers suggest a role of dimer stability in virus-host interactions

    Norovirus capsids are icosahedral particles composed of 90 dimers of the major capsid protein VP1. The C-terminus of the VP1 proteins forms a protruding (P)-domain, mediating receptor attachment, and providing...

    Robert Creutznacher, Thorben Maass, Jasmin Dülfer, Clara Feldmann in Communications Biology (2022)

  3. Article

    Open Access

    Ligand-induced structural transitions combined with paramagnetic ions facilitate unambiguous NMR assignments of methyl groups in large proteins

    NMR spectroscopy allows the study of biomolecules in close-to-native conditions. Structural information can be inferred from the NMR spectra when an assignment is available. Protein assignment is usually a tim...

    Lars Mühlberg, Tuncay Alarcin, Thorben Maass in Journal of Biomolecular NMR (2022)

  4. Article

    Open Access

    Assignment of Ala, Ile, LeuproS, Met, and ValproS methyl groups of the protruding domain of murine norovirus capsid protein VP1 using methyl–methyl NOEs, site directed mutagenesis, and pseudocontact shifts

    The protruding domain (P-domain) of the murine norovirus (MNV) capsid protein VP1 is essential for infection. It mediates receptor binding and attachment of neutralizing antibodies. Protein NMR studies into in...

    Thorben Maass, Leon Torben Westermann, Robert Creutznacher in Biomolecular NMR Assignments (2022)

  5. Article

    Open Access

    Complete assignment of Ala, Ile, LeuProS, Met and ValProS methyl groups of the protruding domain from human norovirus GII.4 Saga

    Attachment of human noroviruses to histo blood group antigens (HBGAs) is thought to be essential for infection, although how this binding event promotes infection is unknown. Recent studies have shown that 60%...

    Christoph Müller-Hermes, Robert Creutznacher in Biomolecular NMR Assignments (2020)

  6. Article

    Open Access

    A post-translational modification of human Norovirus capsid protein attenuates glycan binding

    Attachment of human noroviruses to histo blood group antigens (HBGAs) is essential for infection, but how this binding event promotes the infection of host cells is unknown. Here, we employ protein NMR experim...

    Alvaro Mallagaray, Robert Creutznacher, Jasmin Dülfer in Nature Communications (2019)