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

doi:10.1038/s41467-019-09251-5

Nature Communications (Mar 2019)

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

Affiliations

Alvaro Mallagaray: Institute of Chemistry and Metabolomics, Center of Structural and Cell Biology in Medicine (CSCM), University of Lübeck
Robert Creutznacher: Institute of Chemistry and Metabolomics, Center of Structural and Cell Biology in Medicine (CSCM), University of Lübeck
Jasmin Dülfer: Heinrich Pette Institute, Leibniz Institute for Experimental Virology
Philipp H. O. Mayer: Interfaculty Institute of BiochemistryUniversity of Tübingen, University of Tübingen
Lena Lisbeth Grimm: Institute of Chemistry and Metabolomics, Center of Structural and Cell Biology in Medicine (CSCM), University of Lübeck
Jose Maria Orduña: Institute of Chemistry and Metabolomics, Center of Structural and Cell Biology in Medicine (CSCM), University of Lübeck
Esben Trabjerg: Department of Pharmacy, University of Copenhagen
Thilo Stehle: Interfaculty Institute of BiochemistryUniversity of Tübingen, University of Tübingen
Kasper D. Rand: Department of Pharmacy, University of Copenhagen
Bärbel S. Blaum: Interfaculty Institute of BiochemistryUniversity of Tübingen, University of Tübingen
Charlotte Uetrecht: Heinrich Pette Institute, Leibniz Institute for Experimental Virology
Thomas Peters: Institute of Chemistry and Metabolomics, Center of Structural and Cell Biology in Medicine (CSCM), University of Lübeck

DOI: https://doi.org/10.1038/s41467-019-09251-5
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 14

Abstract

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Attachment of human noroviruses to histo blood group antigens (HBGAs) is essential for infection. Here the authors report that an asparagine residue located near the HBGA-attachment site can convert into an iso-aspartate residue through spontaneous deamidation and influence HBGA recognition.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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