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

James Jung, Timothy Grant, Dennis R. Thomas, Chris W. Diehnelt, Nikolaus Grigorieff, Leemor Joshua-Tor

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)12828-12832
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume116
Issue number26
DOIs
StatePublished - 2019

Keywords

  • Cryo-EM
  • Foodborne illnesses
  • Norovirus

ASJC Scopus subject areas

  • General

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