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- PDB-26wc: Local refinement of the mpox virus A35R protein in complexed with... -

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Entry
Database: PDB / ID: 26wc
TitleLocal refinement of the mpox virus A35R protein in complexed with 17H1 Fab
Components
  • Protein OPG161
  • Variable domain of the 17H1 heavy chain
  • Variable domain of the 17H1 light chain
KeywordsVIRAL PROTEIN / Immune Complex
Function / homologyChordopoxvirus A33R / Chordopoxvirus A33R protein / C-type lectin-like/link domain superfamily / C-type lectin fold / host cell membrane / virion membrane / Protein OPG161
Function and homology information
Biological speciesMonkeypox virus
Mus musculus (house mouse)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.63 Å
AuthorsXiao, Y.X. / He, M.Z.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: MedComm (2020) / Year: 2026
Title: Discovery and Structural Characterization of a Highly Protective Neutralizing Antibody Targeting the Mpox Virus A35R Protein.
Authors: Shimeng Bai / Shuo Song / Xin Wang / Yuxin Xiao / Yun Long / Fenfang Wu / Fuxiang Wang / Zhongyi Fan / Jianqing Xu / Maozhou He / Hongzhou Lu /
Abstract: The recent resurgence of the mpox virus (MPXV) has raised global health concerns due to its potential to cause severe illness in vulnerable populations. Targeting the extracellular enveloped virus ...The recent resurgence of the mpox virus (MPXV) has raised global health concerns due to its potential to cause severe illness in vulnerable populations. Targeting the extracellular enveloped virus (EEV) protein A35R is a promising strategy to restrict viral dissemination within the host. In this study, we combined mRNA-LNP immunization with the Beacon Optofluidic system to rapidly screen and isolate high-affinity monoclonal antibodies. One of these antibodies, 17H1, exhibited exceptional neutralization against authentic MPXV. Cryo-electron microscopy (Cryo-EM) analysis revealed that 17H1 binds to a specific epitope at the distal ends of the A35R dimer. The interaction is stabilized by a unique network of hydrogen bonds and salt bridges, particularly involving residue E120, distinguishing its binding mode from previously reported A35R antibodies. Furthermore, 17H1 exhibited complete protective efficacy against MPXV infection in vivo and significantly reduced pulmonary viral load and lung pathogenesis. These findings highlight 17H1 as a promising therapeutic candidate for novel mpox interventions.
History
DepositionMay 18, 2026Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Jul 22, 2026Provider: repository / Type: Initial release
Revision 1.0Jul 22, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Jul 22, 2026Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jul 22, 2026Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jul 22, 2026Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Jul 22, 2026Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Protein OPG161
H: Variable domain of the 17H1 heavy chain
L: Variable domain of the 17H1 light chain
a: Protein OPG161
h: Variable domain of the 17H1 heavy chain
l: Variable domain of the 17H1 light chain


Theoretical massNumber of molelcules
Total (without water)91,3026
Polymers91,3026
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 Protein OPG161


Mass: 20900.422 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Monkeypox virus / Gene: OPG161, MPXVgp145 / Production host: Homo sapiens (human) / References: UniProt: A0A7H0DND2
#2: Antibody Variable domain of the 17H1 heavy chain


Mass: 12816.322 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Production host: Homo sapiens (human)
#3: Antibody Variable domain of the 17H1 light chain


Mass: 11934.276 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Production host: Homo sapiens (human)
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: Local refinement of the mpox virus A35R protein in complexed with 17H1 Fab
Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Monkeypox virus
Source (recombinant)Organism: Homo sapiens (human)
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

MicroscopyModel: TFS GLACIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k)

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Processing

EM software
IDNameVersionCategory
1cryoSPARCparticle selection
2RELION5particle selection
14cryoSPARC3D reconstruction
CTF correctionType: PHASE FLIPPING ONLY
SymmetryPoint symmetry: C2 (2 fold cyclic)
3D reconstructionResolution: 3.63 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 447301 / Symmetry type: POINT

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