RNA Therapeutics Institute
Biophysics | Computational Biology | Microbiology | Structural Biology | Viruses
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.
cryo-EM, foodborne illnesses, norovirus
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Copyright © 2019 the Author(s). Published by PNAS. This open access article is distributed under Creative Commons Attribution-NonCommercial- NoDerivatives License 4.0 (CC BY-NC-ND).
DOI of Published Version
Proc Natl Acad Sci U S A. 2019 Jun 25;116(26):12828-12832. doi: 10.1073/pnas.1903562116. Epub 2019 Jun 10. Link to article on publisher's site
Proceedings of the National Academy of Sciences of the United States of America
Jung, James; Grant, Timothy; Thomas, Dennis R.; Diehnelt, Chris W.; Grigorieff, Nikolaus; and Joshua-Tor, Leemor, "High-resolution cryo-EM structures of outbreak strain human norovirus shells reveal size variations" (2019). Open Access Articles. 3901.
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.