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- PDB-9e89: CPV2a capsid complexed with scFv2 -

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Basic information

Entry
Database: PDB / ID: 9.0E+89
TitleCPV2a capsid complexed with scFv2
Components
  • Capsid protein
  • Heavy-chain of scFv clone 2
  • Light-chain of scFv clone 2
KeywordsVIRUS/IMMUNE SYSTEM / Virus / Antibody / Complex / VIRUS-IMMUNE SYSTEM complex
Function / homology
Function and homology information


symbiont entry into host cell via permeabilization of host membrane / T=1 icosahedral viral capsid / clathrin-dependent endocytosis of virus by host cell / virion attachment to host cell / structural molecule activity
Similarity search - Function
Parvovirus coat protein VP2 / Parvovirus coat protein VP1/VP2 / Parvovirus coat protein VP2 / Capsid/spike protein, ssDNA virus
Similarity search - Domain/homology
Biological speciesCanine parvovirus 2b
Canis lupus familiaris (dog)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsLee, H. / Hafenstein, S.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: Proc Natl Acad Sci U S A / Year: 2025
Title: Structures and functions of the limited natural polyclonal antibody response to parvovirus infection.
Authors: Oluwafemi F Adu / Hyunwook Lee / Simon P Früh / Marta V Schoenle / Wendy S Weichert / Andrew I Flyak / Susan L Hafenstein / Colin R Parrish /
Abstract: Host antibody responses are key components in the protection of animals against pathogens, yet the defining properties of viral antigens and induction of B cell responses that result in varied ...Host antibody responses are key components in the protection of animals against pathogens, yet the defining properties of viral antigens and induction of B cell responses that result in varied protection are still poorly understood. Parvoviruses are simple molecular structures that display 60 repeated motifs on their capsid surface, and rapidly induce strong antibody responses that protect animals from infection. We recently showed that following canine parvovirus infection of its natural host, the polyclonal response in the sera contained only two or three dominant antibodies that bound two epitopes on the capsid. Here, we characterize key antibodies present in that immune response, identifying their sequences, defining their binding properties on the capsid by cryoelectron microscopic (cryoEM) analysis, and testing their effects on viral infectivity. Two antibodies sharing the same heavy chain bound to the side of the capsid threefold spike (B-site), while another distinct antibody bound close to the threefold axis (A-site). The epitopes of these antibodies overlapped the binding site of the host receptor, the transferrin receptor type-1, but to varying degrees. The antibodies varied widely in their neutralization efficiencies as either immunoglobulins (IgGs) or monomeric antigen-binding fragments (Fabs), which was consistent with their ability to compete for the receptor. The monoclonal antibodies characterized here matched the structures from the cryoEM analysis of polyclonal sera, including those present in a different dog than the monoclonal source. This shows that after infection, a focused response to the viral antigen is produced that protects against infection.
History
DepositionNov 5, 2024Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 29, 2025Provider: repository / Type: Initial release
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Capsid protein
L: Light-chain of scFv clone 2
H: Heavy-chain of scFv clone 2


Theoretical massNumber of molelcules
Total (without water)90,0323
Polymers90,0323
Non-polymers00
Water00
1
A: Capsid protein
L: Light-chain of scFv clone 2
H: Heavy-chain of scFv clone 2
x 60


Theoretical massNumber of molelcules
Total (without water)5,401,943180
Polymers5,401,943180
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation59
2


  • Idetical with deposited unit
  • icosahedral asymmetric unit
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
A: Capsid protein
L: Light-chain of scFv clone 2
H: Heavy-chain of scFv clone 2
x 5


  • icosahedral pentamer
  • 450 kDa, 15 polymers
Theoretical massNumber of molelcules
Total (without water)450,16215
Polymers450,16215
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation4
4
A: Capsid protein
L: Light-chain of scFv clone 2
H: Heavy-chain of scFv clone 2
x 6


  • icosahedral 23 hexamer
  • 540 kDa, 18 polymers
Theoretical massNumber of molelcules
Total (without water)540,19418
Polymers540,19418
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation5
5


  • Idetical with deposited unit in distinct coordinate
  • icosahedral asymmetric unit, std point frame
TypeNameSymmetry operationNumber
transform to point frame1
SymmetryPoint symmetry: (Schoenflies symbol: I (icosahedral))

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Components

#1: Protein Capsid protein / Viral protein 2


Mass: 64745.559 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Canine parvovirus 2b / Gene: VP2 / Production host: Felis catus (domestic cat) / References: UniProt: B8X1I1
#2: Antibody Light-chain of scFv clone 2


Mass: 11121.105 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Canis lupus familiaris (dog) / Cell line (production host): High Five / Production host: Trichoplusia ni (cabbage looper)
#3: Antibody Heavy-chain of scFv clone 2


Mass: 14165.727 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Canis lupus familiaris (dog) / Cell line (production host): High Five / Production host: Trichoplusia ni (cabbage looper)
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: Canine parvovirus 2a / Type: VIRUS / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Canine parvovirus 2a
Source (recombinant)Organism: Felis catus (domestic cat)
Details of virusEmpty: YES / Enveloped: NO / Isolate: STRAIN / Type: VIRION
Buffer solutionpH: 7
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: Talos Arctica / Image courtesy: FEI Company
MicroscopyModel: FEI TALOS ARCTICA
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2250 nm / Nominal defocus min: 750 nm
Image recordingElectron dose: 40 e/Å2 / Film or detector model: FEI FALCON III (4k x 4k)

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Processing

EM softwareName: PHENIX / Category: model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 5253 / Symmetry type: POINT
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0046290
ELECTRON MICROSCOPYf_angle_d0.5098591
ELECTRON MICROSCOPYf_dihedral_angle_d4.701853
ELECTRON MICROSCOPYf_chiral_restr0.042934
ELECTRON MICROSCOPYf_plane_restr0.0041132

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