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 J, Grant T, Thomas DR, Diehnelt CW, Grigorieff N, Joshua-Tor L. (2019). High-resolution cryo-EM structures of outbreak strain human norovirus shells reveal size variations. Open Access Articles. https://doi.org/10.1073/pnas.1903562116. Retrieved from https://escholarship.umassmed.edu/oapubs/3901
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.