Glycan remodeled erythrocytes facilitate antigenic characterization of recent A/H3N2 influenza viruses

Here, Broszeit et al. show that circulating A/H3N2 viruses have evolved binding specificity to α2,6-sialosides on extended LacNAc moieties and therefore cannot agglutinate erythrocytes. Applying glycan remodeling allows to install functional receptors on erythrocytes and promotes identification of n...

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Autores principales:	Frederik Broszeit, Rosanne J. van Beek, Luca Unione, Theo M. Bestebroer, Digantkumar Chapla, Jeong-Yeh Yang, Kelley W. Moremen, Sander Herfst, Ron A. M. Fouchier, Robert P. de Vries, Geert-Jan Boons
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/5e15ec268a114eca8611ad0bb2edf018
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spelling	oai:doaj.org-article:5e15ec268a114eca8611ad0bb2edf0182021-12-02T18:50:53ZGlycan remodeled erythrocytes facilitate antigenic characterization of recent A/H3N2 influenza viruses10.1038/s41467-021-25713-12041-1723https://doaj.org/article/5e15ec268a114eca8611ad0bb2edf0182021-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-25713-1https://doaj.org/toc/2041-1723Here, Broszeit et al. show that circulating A/H3N2 viruses have evolved binding specificity to α2,6-sialosides on extended LacNAc moieties and therefore cannot agglutinate erythrocytes. Applying glycan remodeling allows to install functional receptors on erythrocytes and promotes identification of newly circulating variants to facilitate vaccine design.Frederik BroszeitRosanne J. van BeekLuca UnioneTheo M. BestebroerDigantkumar ChaplaJeong-Yeh YangKelley W. MoremenSander HerfstRon A. M. FouchierRobert P. de VriesGeert-Jan BoonsNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Frederik Broszeit Rosanne J. van Beek Luca Unione Theo M. Bestebroer Digantkumar Chapla Jeong-Yeh Yang Kelley W. Moremen Sander Herfst Ron A. M. Fouchier Robert P. de Vries Geert-Jan Boons Glycan remodeled erythrocytes facilitate antigenic characterization of recent A/H3N2 influenza viruses
description	Here, Broszeit et al. show that circulating A/H3N2 viruses have evolved binding specificity to α2,6-sialosides on extended LacNAc moieties and therefore cannot agglutinate erythrocytes. Applying glycan remodeling allows to install functional receptors on erythrocytes and promotes identification of newly circulating variants to facilitate vaccine design.
format	article
author	Frederik Broszeit Rosanne J. van Beek Luca Unione Theo M. Bestebroer Digantkumar Chapla Jeong-Yeh Yang Kelley W. Moremen Sander Herfst Ron A. M. Fouchier Robert P. de Vries Geert-Jan Boons
author_facet	Frederik Broszeit Rosanne J. van Beek Luca Unione Theo M. Bestebroer Digantkumar Chapla Jeong-Yeh Yang Kelley W. Moremen Sander Herfst Ron A. M. Fouchier Robert P. de Vries Geert-Jan Boons
author_sort	Frederik Broszeit
title	Glycan remodeled erythrocytes facilitate antigenic characterization of recent A/H3N2 influenza viruses
title_short	Glycan remodeled erythrocytes facilitate antigenic characterization of recent A/H3N2 influenza viruses
title_full	Glycan remodeled erythrocytes facilitate antigenic characterization of recent A/H3N2 influenza viruses
title_fullStr	Glycan remodeled erythrocytes facilitate antigenic characterization of recent A/H3N2 influenza viruses
title_full_unstemmed	Glycan remodeled erythrocytes facilitate antigenic characterization of recent A/H3N2 influenza viruses
title_sort	glycan remodeled erythrocytes facilitate antigenic characterization of recent a/h3n2 influenza viruses
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/5e15ec268a114eca8611ad0bb2edf018
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Glycan remodeled erythrocytes facilitate antigenic characterization of recent A/H3N2 influenza viruses

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