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

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 Uetrecht, Thomas Peters*

*Corresponding author for this work
21 Citations (Scopus)


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.

Original languageEnglish
Article number1320
JournalNature Communications
Issue number1
Publication statusPublished - 01.12.2019

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)

DFG Research Classification Scheme

  • 204-04 Virology


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