A post-translational modification of human Norovirus capsid protein attenuates glycan binding
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.
Enregistré dans:
Auteurs principaux: | 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 |
---|---|
Format: | article |
Langue: | EN |
Publié: |
Nature Portfolio
2019
|
Sujets: | |
Accès en ligne: | https://doaj.org/article/c8982557c21047d891ebe906ae91a8ed |
Tags: |
Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!
|
Documents similaires
-
Glycan Engagement Dictates Hydrocephalus Induction by Serotype 1 Reovirus
par: Jennifer Stencel-Baerenwald, et autres
Publié: (2015) -
Structural Basis and Evolution of Glycan Receptor Specificities within the Polyomavirus Family
par: Luisa J. Ströh, et autres
Publié: (2020) -
Mass Spectrometry-Based System for Identifying and Typing Norovirus Major Capsid Protein VP1
par: Pei-Yu Chu, et autres
Publié: (2021) -
Norovirus evolution in immunodeficient mice reveals potentiated pathogenicity via a single nucleotide change in the viral capsid.
par: Forrest C Walker, et autres
Publié: (2021) -
Phylogenetic Analyses Suggest that Factors Other Than the Capsid Protein Play a Role in the Epidemic Potential of GII.2 Norovirus
par: Kentaro Tohma, et autres
Publié: (2017)