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

Jung, J., Grant, T., Thomas, D. R., Diehnelt, C. W., Grigorieff, N., Joshua-Tor, L. (June 2019) High-resolution cryo-EM structures of outbreak strain human norovirus shells reveal size variations. Proc Natl Acad Sci U S A, 116 (26). pp. 12828-12832. ISSN 0027-8424

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URL: https://www.ncbi.nlm.nih.gov/pubmed/31182604
DOI: 10.1073/pnas.1903562116

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-A) 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 Zn(2+) 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.

Item Type: Paper
Subjects: Investigative techniques and equipment > microscopy > Cryo-electron microscopy
CSHL Authors:
Communities: CSHL labs > Joshua-Tor lab
Depositing User: Matthew Dunn
Date: 25 June 2019
Date Deposited: 08 Aug 2019 14:22
Last Modified: 08 Aug 2019 14:22
Related URLs:
URI: http://repository.cshl.edu/id/eprint/38140

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