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

Authors :
Alexis de Rougemont
Manon Chassaing
Didier Majou
Christophe Gantzer
Nicolas Boudaud
Julie Loutreul
Maëlle Robin
Gaël Belliot
Actalia [Saint-Lô]
Laboratoire de Chimie Physique et Microbiologie pour les Matériaux et l'Environnement (LCPME)
Institut de Chimie du CNRS (INC)-Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS)
Centre National de Référence des virus entériques [CHU de Dijon] (CNR virus entériques)
Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand (CHU Dijon)
Laboratoire de sérologie-virologie (CHU de Dijon)
Procédés Alimentaires et Microbiologiques [Dijon] (PAM)
Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement
ACTIA
Source :
Scientific Reports, Scientific Reports, Nature Publishing Group, 2019, 9 (1), pp.15312. ⟨10.1038/s41598-019-51750-4⟩, Scientific Reports, Vol 9, Iss 1, Pp 1-11 (2019)
Publication Year :
2019
Publisher :
Springer Science and Business Media LLC, 2019.

Abstract

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.

Details

ISSN :
20452322
Volume :
9
Database :
OpenAIRE
Journal :
Scientific Reports
Accession number :
edsair.doi.dedup.....0e5cf91b06ea6f100a919b8266a97535
Full Text :
https://doi.org/10.1038/s41598-019-51750-4