@article {64971,
	title = {High-resolution cryo-EM structures of outbreak strain human norovirus shells reveal size variations.},
	journal = {Proceedings of the National Academy of Sciences of the United States of America},
	volume = {116},
	year = {2019},
	month = {2019 Jun 25},
	pages = {12828-32},
	abstract = {<p>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-{\r 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 Zn2+\&nbsp;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.</p>
},
	doi = {10.1073/pnas.1903562116},
	author = {Jung, James and Grant, Timothy and Thomas, Dennis R. and Diehnelt, Chris W. and Grigorieff, Nikolaus and Leemor, Joshua-Tor}
}
