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


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2019-12

AUTHORS

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

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. More... »

PAGES

1320

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41467-019-09251-5

DOI

http://dx.doi.org/10.1038/s41467-019-09251-5

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1112896034

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30899001


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