Loading…

Biological and physico-chemical characterization of human norovirus-like particles under various environmental conditions

Human noroviruses (HuNoVs) are the predominant etiological agent of viral gastroenteritis in all age groups worldwide. Mutations over the years have affected noroviruses' responses to environmental conditions due to the arrangement of amino acid residues exposed on the VP1 capsid surface of eac...

Full description

Saved in:
Bibliographic Details
Published in:Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2023-11, Vol.231, p.113545-113545, Article 113545
Main Authors: Abou-Hamad, Nicole, Estienney, Marie, Chassagnon, Rémi, Bon, Marjorie, Daval-Frerot, Philippe, de Rougemont, Alexis, Guyot, Stéphane, Bouyer, Frédéric, Belliot, Gaël
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Human noroviruses (HuNoVs) are the predominant etiological agent of viral gastroenteritis in all age groups worldwide. Mutations over the years have affected noroviruses' responses to environmental conditions due to the arrangement of amino acid residues exposed on the VP1 capsid surface of each strain. The GII.4 HuNoV genotype has been the predominant variant for decades, while the GII.17 genotype has often been detected in East Asia since 2014. Here, GII.17 and GII.4 baculovirus-expressed VLPs (virus-like particles) were used to study the biological (binding to HuNoV ligand, namely the ABO and Lewis antigens) and physicochemical properties (size, morphology, and charge) of the HuNoV capsid under different conditions (temperature, pH, and ionic strength). GII.17 showed stability at low and high ionic strength, while GII.4 aggregated at an ionic strength of 10 mM. The nature of the buffers influences the morphology and stability of the VLPs. Here, both VLPs were highly stable from pH 7–8.5 at 25 °C. VLPs retained HBGA binding capability for the pH, ionic strength and temperature encountered in the stomach (fed state) and the small intestine. Increasing the temperature to above 65 °C altered the morphology of VLPs, causing aggregation, and decreased their affinity to HBGAs. Comparing both isolates, GII.17 showed a better stability profile and higher affinity to HBGAs than GII.4, making them interesting candidate particles for a future norovirus vaccine. Biological and physicochemical studies of VLPs are as pertinent as ever in view of the future arrival of VLP-based HuNoV vaccines. [Display omitted] •pH and temperature affect human norovirus structure and biological properties.•Ionic strength doesn’t affect VLP structure and receptor binding capacity.•VLPs are active during gastric fed state but not in the fasted state.•Aggregated VLP is associated with loss of activity.
ISSN:0927-7765
1873-4367
DOI:10.1016/j.colsurfb.2023.113545