Cargando…
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...
Autores principales: | , , , , , |
---|---|
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 |
_version_ | 1785080959495831552 |
---|---|
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. |
format | Online Article Text |
id | pubmed-10383637 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT fengyuzhen fucosebindingcancelsoutmechanicaldifferencesbetweendistincthumannoroviruses AT poganronja fucosebindingcancelsoutmechanicaldifferencesbetweendistincthumannoroviruses AT thiedelars fucosebindingcancelsoutmechanicaldifferencesbetweendistincthumannoroviruses AT mullerguhljurgen fucosebindingcancelsoutmechanicaldifferencesbetweendistincthumannoroviruses AT uetrechtcharlotte fucosebindingcancelsoutmechanicaldifferencesbetweendistincthumannoroviruses AT rooswouterh fucosebindingcancelsoutmechanicaldifferencesbetweendistincthumannoroviruses |