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-Structure paper
Title | Structural heterogeneity of a human norovirus vaccine candidate. |
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Journal, issue, pages | Virology, Vol. 553, Page 23-34, Year 2021 |
Publish date | Jan 15, 2021 |
Authors | Jessica M Devant / Grant S Hansman / |
PubMed Abstract | 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 ...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. |
External links | Virology / PubMed:33202318 |
Methods | EM (single particle) |
Resolution | 4.17 - 8.05 Å |
Structure data | EMDB-10755: EMDB-10756: EMDB-10757: EMDB-10758: EMDB-10759: |