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Title | High-resolution cryo-EM structures of outbreak strain human norovirus shells reveal size variations. |
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Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 116, Issue 26, Page 12828-12832, Year 2019 |
Publish date | Jun 25, 2019 |
![]() | James Jung / Timothy Grant / Dennis R Thomas / Chris W Diehnelt / Nikolaus Grigorieff / Leemor Joshua-Tor / ![]() |
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 ...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. |
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Methods | EM (single particle) |
Resolution | 2.6 - 4.1 Å |
Structure data | EMDB-20195, PDB-6otf: ![]() EMDB-20197: EMDB-20198, PDB-6ou9: ![]() EMDB-20199: ![]() EMDB-20201: EMDB-20202, PDB-6ouc: EMDB-20205, PDB-6out: EMDB-20206, PDB-6ouu: |
Chemicals | ![]() ChemComp-ZN: ![]() ChemComp-HOH: |
Source |
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![]() | VIRUS LIKE PARTICLE / Caliciviridae / Norovirus / GII.2 / Snow Mountain Virus / Calicivirus / GI.7 / GI.1 / Norwalk / GII.4 |