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Proc Natl Acad Sci U S A. 2019 Jun 10. pii: 201903562. doi: 10.1073/pnas.1903562116. [Epub ahead of print]

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

Author information

1
W. M. Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724.
2
Howard Hughes Medical Institute, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724.
3
Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, VA 20147.
4
Biodesign Institute Center for Innovations in Medicine, Arizona State University, Tempe, AZ 85281.
5
RNA Therapeutics Institute, University of Massachusetts Medical School, Worcester, MA 01605.
6
Howard Hughes Medical Institute, University of Massachusetts Medical School, Worcester, MA 01605.
7
W. M. Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724; leemor@cshl.edu.

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.

KEYWORDS:

cryo-EM; foodborne illnesses; norovirus

PMID:
31182604
DOI:
10.1073/pnas.1903562116
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