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TitleConformational Plasticity of the Human Norovirus GII.3 Capsid Reveals Alternative P Domain Interaction Networks.
Journal, issue, pagesInt J Mol Sci, Vol. 27, Issue 15, Year 2026
Publish dateJul 24, 2026
AuthorsChihong Song / Motohiro Miki / Reiko Takai-Todaka / Kosuke Murakami / Kazuhiko Katayama / Kazuyoshi Murata /
PubMed AbstractHuman noroviruses (HuNoVs) are a leading cause of acute gastroenteritis worldwide, yet no effective antiviral therapeutics are currently available. Although environmentally induced capsid ...Human noroviruses (HuNoVs) are a leading cause of acute gastroenteritis worldwide, yet no effective antiviral therapeutics are currently available. Although environmentally induced capsid conformational changes associated with infectivity have been reported in murine noroviruses (MNVs), comparable conformational switching has not been demonstrated in HuNoVs. In this study, we generated HuNoV GII.3 virus-like particles (VLPs) using a baculovirus expression system and identified two distinct T = 3 particle populations coexisting within VLP preparations derived from a single strain through cryo-electron microscopy single-particle analysis. Comparative structural analysis revealed that these two T = 3 capsid conformations correspond to the resting and rising states of the protruding (P) domain. Rearrangement of the P domain alters intermolecular interactions between adjacent capsid subunits, resulting in distinct capsid surface architectures. In the resting state, intermolecular contacts were mediated predominantly by the P2 subdomain, with limited contribution from the P1 subdomain. In contrast, the rising state exhibited a shift toward an alternative interaction interface primarily involving the P1 subdomain. The alteration of the capsid surface accompanying this conformational switching can influence biologically relevant intermolecular interactions with viral hosts and antibodies as demonstrated in murine norovirus. These findings demonstrate previously unrecognized structural polymorphism in the HuNoV capsid and provide evidence that conformational switching may occur in HuNoVs. Our results offer new insights into norovirus capsid dynamics and may inform future structure-based vaccine and antiviral drug development.
External linksInt J Mol Sci / PubMed:42589245 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 7.2 Å
Structure data

81556

27zd

EMDB-81556, PDB-27zd:
Human norovirus GII.3 TCH04-577 VP1
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-81567: Cryo-EM overall map of the GII.3 VLP in the resting state
Method: EM (single particle) / Resolution: 7.2 Å

EMDB-81571: Focused-refinement map of the AB dimer in the resting-state GII.3 human norovirus VLP
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-81575: Focused-refinement map of the CC dimer in the resting-state GII.3 human norovirus VLP
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-81576: Focused-refinement map of the CC dimer in the rising-state GII.3 human norovirus VLP
Method: EM (single particle) / Resolution: 4.7 Å

Source
  • norovirus hu/texas/tch04-577/2004/us
KeywordsVIRUS / Calicivirus / Molecular Interactions / Icosahedral Virus / Virus Like Particle

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