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

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Proceedings of the National Academy of Sciences of the United States of America. 2019 Jun 25;116(26):12828-32. doi: 10.1073/pnas.1903562116
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High-resolution cryo-EM structures of outbreak strain human norovirus shells reveal size variations. Grigorieff Lab
Jung J, Grant T, Thomas DR, Diehnelt CW, Grigorieff N, Leemor J
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Abstract

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.

PMID: 31182604 [PubMed - indexed for MEDLINE]

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Published as a preprint in bioRxiv on March 16. https://www.biorxiv.org/content/10.1101/580167v1

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