Structural heterogeneity of a human norovirus vaccine candidate

Human norovirus virus-like particles (VLPs) are assumed to be morphologically and antigenically similar to virion particles. The norovirus virion is assembled from 180 copies of the capsid protein (VP1) and exhibits T = 3 icosahedral symmetry. In this study, we showed that the vaccine candidate GII....

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Hauptverfasser: Devant, Jessica (VerfasserIn) , Hansman, Grant S. (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 2021
In: Virology
Year: 2020, Jahrgang: 553, Pages: 23-34
ISSN:1096-0341
DOI:10.1016/j.virol.2020.10.005
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.virol.2020.10.005
Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0042682220302063
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Verfasserangaben:Jessica M. Devant, Grant S. Hansman

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520 |a Human norovirus virus-like particles (VLPs) are assumed to be morphologically and antigenically similar to virion particles. The norovirus virion is assembled from 180 copies of the capsid protein (VP1) and exhibits T = 3 icosahedral symmetry. In this study, we showed that the vaccine candidate GII.4c VP1 formed T = 1 and T = 3 VLPs, but mainly assembled into T = 4 icosahedral particles that were composed of 240 VP1 copies. In contrast, another clinically important genotype, GII.17, almost exclusively folded into T = 3 VLPs. Interestingly, the GII.4c T = 1 particles had higher binding capacities to norovirus-specific Nanobodies than to GII.4c T = 3 and T = 4 particles. Our data indicated that the occluded Nanobody-binding epitopes on the T = 1 particles were more accessible compared to the larger T = 3 and T = 4 particles. Overall, this new data revealed that GII.4c VLPs had a preference for forming the T = 4 icosahedral symmetry and future studies with varied sized norovirus VLPs should take caution when examining antigenicity. 
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