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- PDB-12tz: M6 bound to C-C VP1 dimer of GII.4 Syd VLP (C1 side) -

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Basic information

Entry
Database: PDB / ID: 12tz
TitleM6 bound to C-C VP1 dimer of GII.4 Syd VLP (C1 side)
Components
  • M6
  • VP1
KeywordsVIRAL PROTEIN / VP1 / M6 / Norovirus
Function / homologyCalicivirus coat protein C-terminal / Calicivirus coat protein C-terminal / Calicivirus coat protein / Calicivirus coat protein / Picornavirus/Calicivirus coat protein / Viral coat protein subunit / host cell cytoplasm / VP1
Function and homology information
Biological speciesNorovirus Hu/GII.4/Sydney/NSW0514/2012/AU
Lama glama (llama)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsApostol, C. / Anish, R. / Pham, S. / Prasad, B.V.V.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)P01 AI057788 United States
CitationJournal: Res Sq / Year: 2026
Title: Symmetry-breaking antibody binding reveals extensive capsid malleability in pandemic human norovirus.
Authors: Carmen V Apostol / Ramakrishnan Anish / Son Pham / Khalil Ettayebi / Janam Dave / Frederick H Neill / Marina Bok / Banumathi Sankaran / Sue Crawford / Robert L Atmar / James E Crowe / ...Authors: Carmen V Apostol / Ramakrishnan Anish / Son Pham / Khalil Ettayebi / Janam Dave / Frederick H Neill / Marina Bok / Banumathi Sankaran / Sue Crawford / Robert L Atmar / James E Crowe / Viviana Parreño / Mary K Estes / B V Venkataram Prasad /
Abstract: Virus capsids are metastable assemblies with an exquisite balance between stability and flexibility, obligatory for entry, infectivity, and immune escape. Yet, the extent to which human viruses ...Virus capsids are metastable assemblies with an exquisite balance between stability and flexibility, obligatory for entry, infectivity, and immune escape. Yet, the extent to which human viruses exploit capsid plasticity and how that consequently shapes antigenic landscapes remains poorly understood. Human noroviruses (HuNoVs) are the leading cause of acute viral gastroenteritis worldwide. GII.4 HuNoVs have been evolving epochally, driving most global pandemics, and since 2012, GII.4 Sydney has been the dominant variant. The major capsid protein VP1 is central to infectivity and immune recognition, and VP1-based virus-like particles (VLPs) are considered promising vaccine candidates. Yet, how the icosahedral HuNoV capsid responds to antibody pressure at the atomic level is still unclear. Here, we present the first atomic structure of GII.4 Sydney capsid determined by cryo-EM, revealing the structural features that likely contribute to its sustained dominance. Using focused refinement, we uncovered the remarkable capsid plasticity in response to symmetry-breaking binding of neutralizing and non-neutralizing antibodies. VP1 adopts 11 distinct conformational modalities to accommodate asymmetric antibody binding, and antibody-disrupted VLPs reassemble into smaller particles with five additional VP1 states. This previously unrecognized extent of conformational adaptability provides key insights for designing next-generation VLP- or mRNA-based vaccines targeting HuNoV infections.
History
DepositionApr 18, 2026Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 28, 2026Provider: repository / Type: Initial release
Revision 1.0Oct 28, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
C: VP1
B: VP1
D: M6


Theoretical massNumber of molelcules
Total (without water)125,1043
Polymers125,1043
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein VP1


Mass: 55897.645 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Norovirus Hu/GII.4/Sydney/NSW0514/2012/AU
Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: K4LM89
#2: Antibody M6


Mass: 13308.611 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lama glama (llama)
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Norovirus Hu/GII.4/Sydney/NSW0514/2012/AU / Type: VIRUS / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Norovirus Hu/GII.4/Sydney/NSW0514/2012/AU
Source (recombinant)Organism: Spodoptera frugiperda (fall armyworm)
Details of virusEmpty: YES / Enveloped: YES / Isolate: STRAIN / Type: VIRUS-LIKE PARTICLE
Buffer solutionpH: 6
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 130000 X / Nominal defocus max: 2500 nm / Nominal defocus min: 500 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)
EM imaging opticsEnergyfilter name: GIF Bioquantum

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Processing

EM software
IDNameVersionCategory
1cryoSPARCparticle selection
2PHENIX1.21.2_5419model refinement
13cryoSPARC3D reconstruction
CTF correctionType: NONE
3D reconstructionResolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 78998 / Symmetry type: POINT
RefinementHighest resolution: 3.5 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0039062
ELECTRON MICROSCOPYf_angle_d0.49312409
ELECTRON MICROSCOPYf_dihedral_angle_d5.71245
ELECTRON MICROSCOPYf_chiral_restr0.0411369
ELECTRON MICROSCOPYf_plane_restr0.0041657

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