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- PDB-9kyz: A35 of MPXV in complex with mAb975 -

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Basic information

Entry
Database: PDB / ID: 9kyz
TitleA35 of MPXV in complex with mAb975
Components
  • Protein OPG161
  • mab975HC
  • mab975KC
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / envelope glycoprotein / VIRAL PROTEIN-IMMUNE SYSTEM complex
Function / homologyChordopoxvirus A33R / Chordopoxvirus A33R protein / C-type lectin-like/link domain superfamily / C-type lectin fold / host cell membrane / virion membrane / membrane / Protein OPG161
Function and homology information
Biological speciesMonkeypox virus
Homo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å
AuthorsYan, R.H. / Yang, H.N.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: Cell / Year: 2025
Title: Structurally conserved human anti-A35 antibodies protect mice and macaques from mpox virus infection.
Authors: Bin Ju / Congcong Liu / Jingjing Zhang / Yaning Li / Haonan Yang / Bing Zhou / Baoying Huang / Jianrong Ma / Jiahan Lu / Lin Cheng / Zhe Cong / Lin Zhu / Tianhao Shi / Yuehong Sun / Na Li / ...Authors: Bin Ju / Congcong Liu / Jingjing Zhang / Yaning Li / Haonan Yang / Bing Zhou / Baoying Huang / Jianrong Ma / Jiahan Lu / Lin Cheng / Zhe Cong / Lin Zhu / Tianhao Shi / Yuehong Sun / Na Li / Ting Chen / Miao Wang / Shilong Tang / Xiangyang Ge / Juanjuan Zhao / Wen-Jie Tan / Renhong Yan / Jing Xue / Zheng Zhang /
Abstract: The A35 protein, expressed on the enveloped virion of monkeypox (mpox) virus (MPXV), is essential for viral infection and spread within the host, making it an effective antiviral target. In this ...The A35 protein, expressed on the enveloped virion of monkeypox (mpox) virus (MPXV), is essential for viral infection and spread within the host, making it an effective antiviral target. In this study, we demonstrated two human anti-A35 monoclonal antibodies (mAbs) displayed potential protection against MPXV in CAST/EiJ mice and rhesus macaques. Using cryo-electron microscopy, we determined two high-resolution structures of the A35 dimer in complex with the fragment of antigen binding of mAb 975 or mAb 981, revealing detailed interactions at the antigen-antibody interfaces. Structural analysis showed that these structurally conserved mAbs bind to a groove region at the interface of A35 dimer. Overall, we provided a proof of concept for a single administration of anti-A35 mAbs mitigating the pathogenic effects of MPXV infection in rhesus macaques. These human-derived mAbs could be served as antibody drug candidates, and their binding models to the A35 dimer will provide valuable insights for future vaccine design.
History
DepositionDec 9, 2024Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Aug 13, 2025Provider: repository / Type: Initial release
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Revision 1.0Aug 13, 2025Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
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Revision 1.0Aug 13, 2025Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
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Revision 1.1Dec 24, 2025Group: Data collection / Database references / Category: citation / citation_author / em_admin
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Revision 2.0Dec 24, 2025Data content type: EM metadata / Data content type: EM metadata / EM metadata / Group: Database references / Experimental summary / Data content type: EM metadata / EM metadata / EM metadata / Category: citation / citation_author / em_admin
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
C: Protein OPG161
D: Protein OPG161
A: mab975HC
B: mab975KC


Theoretical massNumber of molelcules
Total (without water)42,9324
Polymers42,9324
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein Protein OPG161


Mass: 9261.993 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Monkeypox virus / Gene: OPG161, MPXVgp145 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: A0A7H0DND2
#2: Antibody mab975HC


Mass: 13109.636 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human)
#3: Antibody mab975KC


Mass: 11298.476 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / 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: A35 of MPXV in complex with mAb975 / Type: COMPLEX / Entity ID: #2-#3 / Source: MULTIPLE SOURCES
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 7.5
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 defocus max: 1500 nm / Nominal defocus min: 800 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM softwareName: PHENIX / Category: model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 180429 / Symmetry type: POINT
RefinementHighest resolution: 3.2 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0033039
ELECTRON MICROSCOPYf_angle_d0.5234133
ELECTRON MICROSCOPYf_dihedral_angle_d4.578418
ELECTRON MICROSCOPYf_chiral_restr0.038449
ELECTRON MICROSCOPYf_plane_restr0.003528

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