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 and Thomas Peters ()
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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
Esben Trabjerg: University of Copenhagen
Thilo Stehle: University of Tübingen
Kasper D. Rand: University of Copenhagen
Bärbel S. Blaum: University of Tübingen
Charlotte Uetrecht: Leibniz Institute for Experimental Virology
Thomas Peters: University of Lübeck

Nature Communications, 2019, vol. 10, issue 1, 1-14

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-09251-5

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