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.
Guardado en:
Autores principales: | 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 |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2019
|
Materias: | |
Acceso en línea: | https://doaj.org/article/c8982557c21047d891ebe906ae91a8ed |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Glycan Engagement Dictates Hydrocephalus Induction by Serotype 1 Reovirus
por: Jennifer Stencel-Baerenwald, et al.
Publicado: (2015) -
Structural Basis and Evolution of Glycan Receptor Specificities within the Polyomavirus Family
por: Luisa J. Ströh, et al.
Publicado: (2020) -
Mass Spectrometry-Based System for Identifying and Typing Norovirus Major Capsid Protein VP1
por: Pei-Yu Chu, et al.
Publicado: (2021) -
Norovirus evolution in immunodeficient mice reveals potentiated pathogenicity via a single nucleotide change in the viral capsid.
por: Forrest C Walker, et al.
Publicado: (2021) -
Phylogenetic Analyses Suggest that Factors Other Than the Capsid Protein Play a Role in the Epidemic Potential of GII.2 Norovirus
por: Kentaro Tohma, et al.
Publicado: (2017)