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Significance Despite being a leading cause of foodborne illnesses, accounting for 58% of all outbreaks and over 96% of nonbacterial outbreaks, there are no approved treatments available for norovirus infections. Assembled shells of the viruses without genetic materials enclosed are currently being used as candidates for vaccine trials. Although the virus shells have been thought to exist in a single-sized assembly, our structures in near-atomic detail reveal clear variations in size between different outbreak strains, and in spatial and angular arrangements of the antigenic surface spikes. The structures we present serve as valuable templates for facilitating vaccine formulations. Noroviruses are a leading cause of foodborne illnesses worldwide. Although GII.4 strains have been responsible for most norovirus outbreaks, the assembled virus shell structures have been available in detail for only a single strain (GI.1). We present high-resolution (2.6- to 4.1-Å) cryoelectron microscopy (cryo-EM) structures of GII.4, GII.2, GI.7, and GI.1 human norovirus outbreak strain virus-like particles (VLPs). Although norovirus VLPs have been thought to exist in a single-sized assembly, our structures reveal polymorphism between and within genogroups, with small, medium, and large particle sizes observed. Using asymmetric reconstruction, we were able to resolve a Zn2+ metal ion adjacent to the coreceptor binding site, which affected the structural stability of the shell. Our structures serve as valuable templates for facilitating vaccine formulations.

High-resolution cryo-EM structures of outbreak strain human norovirus shells reveal size variations