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Effect of natural ageing and heat treatments on GII.4 norovirus binding to Histo-Blood Group Antigens

Human noroviruses (HuNoVs) are the leading cause of viral foodborne outbreaks worldwide. To date, no available methods can be routinely used to detect infectious HuNoVs in foodstuffs. HuNoVs recognize Histo-Blood Group Antigens (HBGAs) through the binding pocket (BP) of capsid protein VP1, which pro...

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Autores principales: Robin, Maëlle, Chassaing, Manon, Loutreul, Julie, de Rougemont, Alexis, Belliot, Gaël, Majou, Didier, Gantzer, Christophe, Boudaud, Nicolas
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6814753/
https://www.ncbi.nlm.nih.gov/pubmed/31653918
http://dx.doi.org/10.1038/s41598-019-51750-4
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author Robin, Maëlle
Chassaing, Manon
Loutreul, Julie
de Rougemont, Alexis
Belliot, Gaël
Majou, Didier
Gantzer, Christophe
Boudaud, Nicolas
author_facet Robin, Maëlle
Chassaing, Manon
Loutreul, Julie
de Rougemont, Alexis
Belliot, Gaël
Majou, Didier
Gantzer, Christophe
Boudaud, Nicolas
author_sort Robin, Maëlle
collection PubMed
description Human noroviruses (HuNoVs) are the leading cause of viral foodborne outbreaks worldwide. To date, no available methods can be routinely used to detect infectious HuNoVs in foodstuffs. HuNoVs recognize Histo-Blood Group Antigens (HBGAs) through the binding pocket (BP) of capsid protein VP1, which promotes infection in the host cell. In this context, the suitability of human HBGA-binding assays to evaluate the BP integrity of HuNoVs was studied on GII.4 virus-like particles (VLPs) and GII.4 HuNoVs during natural ageing at 20 °C and heat treatments. Our results demonstrate that this approach may reduce the over-estimation of potential infectious HuNoVs resulting from solely using the genome detection, even though some limitations have been identified. The specificity of HBGA-binding to the BP is clearly dependent on the HGBA type (as previously evidenced) and the ionic strength of the media without disturbing such interactions. This study also provides new arguments regarding the ability of VLPs to mimic HuNoV behavior during inactivation treatments. The BP stability of VLPs was at least 4.3 fold lower than that of HuNoVs at 20 °C, whereas capsids of both particles were disrupted at 72 °C. Thus, VLPs are relevant surrogates of HuNoVs for inactivation treatments inducing significant changes in the capsid structure.
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spelling pubmed-68147532019-10-30 Effect of natural ageing and heat treatments on GII.4 norovirus binding to Histo-Blood Group Antigens Robin, Maëlle Chassaing, Manon Loutreul, Julie de Rougemont, Alexis Belliot, Gaël Majou, Didier Gantzer, Christophe Boudaud, Nicolas Sci Rep Article Human noroviruses (HuNoVs) are the leading cause of viral foodborne outbreaks worldwide. To date, no available methods can be routinely used to detect infectious HuNoVs in foodstuffs. HuNoVs recognize Histo-Blood Group Antigens (HBGAs) through the binding pocket (BP) of capsid protein VP1, which promotes infection in the host cell. In this context, the suitability of human HBGA-binding assays to evaluate the BP integrity of HuNoVs was studied on GII.4 virus-like particles (VLPs) and GII.4 HuNoVs during natural ageing at 20 °C and heat treatments. Our results demonstrate that this approach may reduce the over-estimation of potential infectious HuNoVs resulting from solely using the genome detection, even though some limitations have been identified. The specificity of HBGA-binding to the BP is clearly dependent on the HGBA type (as previously evidenced) and the ionic strength of the media without disturbing such interactions. This study also provides new arguments regarding the ability of VLPs to mimic HuNoV behavior during inactivation treatments. The BP stability of VLPs was at least 4.3 fold lower than that of HuNoVs at 20 °C, whereas capsids of both particles were disrupted at 72 °C. Thus, VLPs are relevant surrogates of HuNoVs for inactivation treatments inducing significant changes in the capsid structure. Nature Publishing Group UK 2019-10-25 /pmc/articles/PMC6814753/ /pubmed/31653918 http://dx.doi.org/10.1038/s41598-019-51750-4 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Robin, Maëlle
Chassaing, Manon
Loutreul, Julie
de Rougemont, Alexis
Belliot, Gaël
Majou, Didier
Gantzer, Christophe
Boudaud, Nicolas
Effect of natural ageing and heat treatments on GII.4 norovirus binding to Histo-Blood Group Antigens
title Effect of natural ageing and heat treatments on GII.4 norovirus binding to Histo-Blood Group Antigens
title_full Effect of natural ageing and heat treatments on GII.4 norovirus binding to Histo-Blood Group Antigens
title_fullStr Effect of natural ageing and heat treatments on GII.4 norovirus binding to Histo-Blood Group Antigens
title_full_unstemmed Effect of natural ageing and heat treatments on GII.4 norovirus binding to Histo-Blood Group Antigens
title_short Effect of natural ageing and heat treatments on GII.4 norovirus binding to Histo-Blood Group Antigens
title_sort effect of natural ageing and heat treatments on gii.4 norovirus binding to histo-blood group antigens
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6814753/
https://www.ncbi.nlm.nih.gov/pubmed/31653918
http://dx.doi.org/10.1038/s41598-019-51750-4
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