6OU9

Asymmetric focused reconstruction of human norovirus GI.7 Houston strain VLP asymmetric unit in T=3 symmetry

Summary for 6OU9

• Entry DOI: 10.2210/pdb6ou9/pdb
• Related: 6OTF
• EMDB information: 20195 20197 20198 20199 20201 20202 20205 20206
• Descriptor: Major capsid protein (1 entity in total)
• Functional Keywords: caliciviridae, calicivirus, norovirus, gi.7, virus like particle
• Biological source: Norovirus Hu/GI.7/TCH-060/USA/2003
• Total number of polymer chains: 3
• Total formula weight: 174302.19

Authors

Jung, J.,Grant, T.,Thomas, D.R.,Diehnelt, C.W.,Grigorieff, N.,Joshua-Tor, L. (deposition date: 2019-05-04, release date: 2019-06-26, Last modification date: 2024-03-20)

Primary citation

Jung, J.,Grant, T.,Thomas, D.R.,Diehnelt, C.W.,Grigorieff, N.,Joshua-Tor, L.
High-resolution cryo-EM structures of outbreak strain human norovirus shells reveal size variations.
Proc.Natl.Acad.Sci.USA, 116:12828-12832, 2019

PubMed 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-Å) 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 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.

PubMed: 31182604
DOI: 10.1073/pnas.1903562116

Experimental method

ELECTRON MICROSCOPY (3.2 Å)