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

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.

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Detalles Bibliográficos
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:
Science
Q
Acceso en línea:https://doaj.org/article/c8982557c21047d891ebe906ae91a8ed
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Descripción
Sumario: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.

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