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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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 Investigative techniques and equipment Investigative techniques and equipment > microscopy
CSHL Authors:	Joshua-Tor, Leemor Jung, James Thomas, Dennis R
Communities:	CSHL labs > Joshua-Tor lab CSHL Cancer Center Program > Gene Regulation and Inheritance Program
Depositing User:	Matthew Dunn
Date:	25 June 2019
Date Deposited:	08 Aug 2019 14:22
Last Modified:	02 Feb 2024 16:04
PMCID:	PMC6601263
Related URLs:	Publisher
URI:	https://repository.cshl.edu/id/eprint/38140

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