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

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作者
Maëlle Robin
Manon Chassaing
Julie Loutreul
Alexis de Rougemont
Gaël Belliot
Didier Majou
Christophe Gantzer
Nicolas Boudaud
机构
[1] Actalia,National Reference Center for Gastroenteritis Viruses, Laboratory of Virology
[2] Food Safety Department,UMR PAM A 02.102 Food and Microbiological Processes
[3] LCPME,undefined
[4] UMR 7564 CNRS,undefined
[5] University of Lorraine,undefined
[6] University Hospital of Dijon,undefined
[7] University of Bourgogne Franche-Comté/AgroSup Dijon,undefined
[8] ACTIA,undefined
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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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