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

Author

Listed:
  • Alvaro Mallagaray

    (University of Lübeck)

  • Robert Creutznacher

    (University of Lübeck)

  • Jasmin Dülfer

    (Leibniz Institute for Experimental Virology)

  • Philipp H. O. Mayer

    (University of Tübingen)

  • Lena Lisbeth Grimm

    (University of Lübeck)

  • Jose Maria Orduña

    (University of Lübeck
    San Pablo CEU University)

  • Esben Trabjerg

    (University of Copenhagen
    ETH Zürich)

  • Thilo Stehle

    (University of Tübingen)

  • Kasper D. Rand

    (University of Copenhagen)

  • Bärbel S. Blaum

    (University of Tübingen)

  • Charlotte Uetrecht

    (Leibniz Institute for Experimental Virology
    European XFEL GmbH)

  • Thomas Peters

    (University of Lübeck)

Abstract

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 experiments supported by mass spectrometry and crystallography to study HBGA binding to the P-domain of a prevalent virus strain (GII.4). We report a highly selective transformation of asparagine 373, located in an antigenic loop adjoining the HBGA binding site, into an iso-aspartate residue. This spontaneous post-translational modification (PTM) proceeds with an estimated half-life of a few days at physiological temperatures, independent of the presence of HBGAs but dramatically affecting HBGA recognition. Sequence conservation and the surface-exposed position of this PTM suggest an important role in infection and immune recognition for many norovirus strains.

Suggested Citation

  • Alvaro Mallagaray & Robert Creutznacher & Jasmin Dülfer & Philipp H. O. Mayer & Lena Lisbeth Grimm & Jose Maria Orduña & Esben Trabjerg & Thilo Stehle & Kasper D. Rand & Bärbel S. Blaum & Charlotte Ue, 2019. "A post-translational modification of human Norovirus capsid protein attenuates glycan binding," Nature Communications, Nature, vol. 10(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-09251-5
    DOI: 10.1038/s41467-019-09251-5
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