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*

*Korrespondierende/r Autor/-in für diese Arbeit
21 Zitate (Scopus)

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.

OriginalspracheEnglisch
Aufsatznummer1320
ZeitschriftNature Communications
Jahrgang10
Ausgabenummer1
ISSN1751-8628
DOIs
PublikationsstatusVeröffentlicht - 01.12.2019

Strategische Forschungsbereiche und Zentren

  • Forschungsschwerpunkt: Infektion und Entzündung - Zentrum für Infektions- und Entzündungsforschung Lübeck (ZIEL)

DFG-Fachsystematik

  • 204-04 Virologie

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