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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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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spelling	oai:doaj.org-article:c8982557c21047d891ebe906ae91a8ed2021-12-02T16:57:20ZA post-translational modification of human Norovirus capsid protein attenuates glycan binding10.1038/s41467-019-09251-52041-1723https://doaj.org/article/c8982557c21047d891ebe906ae91a8ed2019-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-09251-5https://doaj.org/toc/2041-1723Attachment 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.Alvaro MallagarayRobert CreutznacherJasmin DülferPhilipp H. O. MayerLena Lisbeth GrimmJose Maria OrduñaEsben TrabjergThilo StehleKasper D. RandBärbel S. BlaumCharlotte UetrechtThomas PetersNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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 A post-translational modification of human Norovirus capsid protein attenuates glycan binding
description	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.
format	article
author	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
author_facet	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
author_sort	Alvaro Mallagaray
title	A post-translational modification of human Norovirus capsid protein attenuates glycan binding
title_short	A post-translational modification of human Norovirus capsid protein attenuates glycan binding
title_full	A post-translational modification of human Norovirus capsid protein attenuates glycan binding
title_fullStr	A post-translational modification of human Norovirus capsid protein attenuates glycan binding
title_full_unstemmed	A post-translational modification of human Norovirus capsid protein attenuates glycan binding
title_sort	post-translational modification of human norovirus capsid protein attenuates glycan binding
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/c8982557c21047d891ebe906ae91a8ed
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A post-translational modification of human Norovirus capsid protein attenuates glycan binding

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