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Fucose Binding Cancels out Mechanical Differences between Distinct Human Noroviruses

The majority of nonbacterial gastroenteritis in humans and livestock is caused by noroviruses. Like most RNA viruses, frequent mutations result in various norovirus variants. The strain-dependent binding profiles of noroviruses to fucose are supposed to facilitate norovirus infection. It remains unc...

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Autores principales: Feng, Yuzhen, Pogan, Ronja, Thiede, Lars, Müller-Guhl, Jürgen, Uetrecht, Charlotte, Roos, Wouter H.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10383637/
https://www.ncbi.nlm.nih.gov/pubmed/37515170
http://dx.doi.org/10.3390/v15071482
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author Feng, Yuzhen
Pogan, Ronja
Thiede, Lars
Müller-Guhl, Jürgen
Uetrecht, Charlotte
Roos, Wouter H.
author_facet Feng, Yuzhen
Pogan, Ronja
Thiede, Lars
Müller-Guhl, Jürgen
Uetrecht, Charlotte
Roos, Wouter H.
author_sort Feng, Yuzhen
collection PubMed
description The majority of nonbacterial gastroenteritis in humans and livestock is caused by noroviruses. Like most RNA viruses, frequent mutations result in various norovirus variants. The strain-dependent binding profiles of noroviruses to fucose are supposed to facilitate norovirus infection. It remains unclear, however, what the molecular mechanism behind strain-dependent functioning is. In this study, by applying atomic force microscopy (AFM) nanoindentation technology, we studied norovirus-like particles (noroVLPs) of three distinct human norovirus variants. We found differences in viral mechanical properties even between the norovirus variants from the same genogroup. The noroVLPs were then subjected to fucose treatment. Surprisingly, after fucose treatment, the previously found considerable differences in viral mechanical properties among these variants were diminished. We attribute a dynamic switch of the norovirus P domain upon fucose binding to the reduced differences in viral mechanical properties across the tested norovirus variants. These findings shed light on the mechanisms used by norovirus capsids to adapt to environmental changes and, possibly, increase cell infection. Hereby, a new step towards connecting viral mechanical properties to viral prevalence is taken.
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spelling pubmed-103836372023-07-30 Fucose Binding Cancels out Mechanical Differences between Distinct Human Noroviruses Feng, Yuzhen Pogan, Ronja Thiede, Lars Müller-Guhl, Jürgen Uetrecht, Charlotte Roos, Wouter H. Viruses Article The majority of nonbacterial gastroenteritis in humans and livestock is caused by noroviruses. Like most RNA viruses, frequent mutations result in various norovirus variants. The strain-dependent binding profiles of noroviruses to fucose are supposed to facilitate norovirus infection. It remains unclear, however, what the molecular mechanism behind strain-dependent functioning is. In this study, by applying atomic force microscopy (AFM) nanoindentation technology, we studied norovirus-like particles (noroVLPs) of three distinct human norovirus variants. We found differences in viral mechanical properties even between the norovirus variants from the same genogroup. The noroVLPs were then subjected to fucose treatment. Surprisingly, after fucose treatment, the previously found considerable differences in viral mechanical properties among these variants were diminished. We attribute a dynamic switch of the norovirus P domain upon fucose binding to the reduced differences in viral mechanical properties across the tested norovirus variants. These findings shed light on the mechanisms used by norovirus capsids to adapt to environmental changes and, possibly, increase cell infection. Hereby, a new step towards connecting viral mechanical properties to viral prevalence is taken. MDPI 2023-06-30 /pmc/articles/PMC10383637/ /pubmed/37515170 http://dx.doi.org/10.3390/v15071482 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Feng, Yuzhen
Pogan, Ronja
Thiede, Lars
Müller-Guhl, Jürgen
Uetrecht, Charlotte
Roos, Wouter H.
Fucose Binding Cancels out Mechanical Differences between Distinct Human Noroviruses
title Fucose Binding Cancels out Mechanical Differences between Distinct Human Noroviruses
title_full Fucose Binding Cancels out Mechanical Differences between Distinct Human Noroviruses
title_fullStr Fucose Binding Cancels out Mechanical Differences between Distinct Human Noroviruses
title_full_unstemmed Fucose Binding Cancels out Mechanical Differences between Distinct Human Noroviruses
title_short Fucose Binding Cancels out Mechanical Differences between Distinct Human Noroviruses
title_sort fucose binding cancels out mechanical differences between distinct human noroviruses
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10383637/
https://www.ncbi.nlm.nih.gov/pubmed/37515170
http://dx.doi.org/10.3390/v15071482
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