Structural heterogeneity of a human norovirus vaccine candidate

• Verfasst von: Devant, Jessica [VerfasserIn]
• Verfasst von: Hansman, Grant S. [VerfasserIn]
• Titel: Structural heterogeneity of a human norovirus vaccine candidate
• Verf.angabe: Jessica M. Devant, Grant S. Hansman
• Jahr: 2021
• Jahr des Originals: 2020
• Umfang: 12 S.
• Fussnoten: Available online 28 October 2020 ; Gesehen am 08.02.2021
• Titel Quelle: Enthalten in: Virology
• Ort Quelle: San Diego, Calif. [u.a.] : Elsevier, 1955
• Jahr Quelle: 2021
• Band/Heft Quelle: 553(2021), Seite 23-34
• ISSN Quelle: 1096-0341
• DOI: doi:10.1016/j.virol.2020.10.005
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: Cryo-EM
• Sach-SW: Norovirus
• Sach-SW: Vaccine
• K10plus-PPN: 1747719099

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 (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.