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

Jung, James, Grant, Timothy, Thomas, Dennis, Diehnelt, Chris, Grigorieff, Nikolaus, Joshua-Tor, Leemor (March 2019) High-resolution cryo-EM structures of outbreak strain human norovirus shells reveal size variations. BioRxiv. (Unpublished)

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Abstract

Abstract Noroviruses are a leading cause of food-borne 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 (2.6-4.1 Å) cryo-electron 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. We developed a new asymmetric reconstruction method and resolved a metal ion adjacent to the co-receptor 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 diseases & disorders > viral diseases
CSHL Authors:	Jung, James Thomas, Dennis R Joshua-Tor, Leemor
Communities:	CSHL labs > Joshua-Tor lab
SWORD Depositor:	CSHL Elements
Depositing User:	CSHL Elements
Date:	16 March 2019
Date Deposited:	21 May 2021 20:18
Last Modified:	21 May 2021 20:18
URI:	https://repository.cshl.edu/id/eprint/40124

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