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TitleStructural basis of poxvirus fusion regulation and anti-A16/G9 antibody-mediated neutralization and protection.
Journal, issue, pagesCell, Vol. 188, Issue 22, Page 6266-6282.e18, Year 2025
Publish dateOct 30, 2025
AuthorsAnnalisa Meola / Riccardo Vernuccio / Leandro Battini / Guillermo Albericio / Pilar Delgado / Rebecca Bamford / Laura Pokorny / Manon Broutin / Alejandro Martínez León / Sébastien Gallien / María Gil / María A Noriega / Florence Guivel-Benhassine / Françoise Porrot / Jeanne Postal / Julian Buchrieser / Mathieu Hubert / Ahmed Haouz / Pierre Lafaye / Mariano Esteban / Jochen S Hub / Matthieu Mahévas / Pascal Chappert / Jason Mercer / Juan Garcia-Arriaza / Olivier Schwartz / Pablo Guardado-Calvo /
PubMed AbstractMonkeypox virus (MPXV) is a poxvirus endemic to Central and West Africa with high epidemic potential. Poxviruses enter host cells via a conserved entry-fusion complex (EFC), which mediates viral ...Monkeypox virus (MPXV) is a poxvirus endemic to Central and West Africa with high epidemic potential. Poxviruses enter host cells via a conserved entry-fusion complex (EFC), which mediates viral fusion to the cell membrane. The EFC is a promising therapeutic target, but the absence of structural data has limited the development of fusion-inhibiting treatments. Here, we investigated A16/G9, a subcomplex of the EFC that controls fusion timing. Using cryo-electron microscopy, we showed how A16/G9 interacts with A56/K2, a viral fusion suppressor that prevents superinfection. Immunization with A16/G9 elicited a protective immune response in mice. Using X-ray crystallography, we characterized two neutralizing antibodies and engineered a chimeric antibody that cross-neutralizes several poxviruses more efficiently than 7D11, the most potent antibody targeting the EFC described to date. These findings highlight the potential of A16/G9 as a candidate for subunit vaccines and identify regions of the EFC as targets for antiviral development.
External linksCell / PubMed:40865523
MethodsEM (single particle) / X-ray diffraction
Resolution2.45 - 4.0 Å
Structure data

52019

9hbk

EMDB-52019, PDB-9hbk:
Structure of A16/G9 in complex with A56/K2 (vaccinia virus)
Method: EM (single particle) / Resolution: 3.2 Å

53936

9rdh

EMDB-53936, PDB-9rdh:
Structure of A16/G9 in complex with A56/K2 at pH 5.5 (vaccinia virus)
Method: EM (single particle) / Resolution: 4.0 Å

PDB-9hl2:
Structure of A56/K2 (vaccinia virus)
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-9hls:
Structure of A16/G9 (vaccinia virus) in complex with VHH D07, VHH B01 and VHH C05
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

PDB-9hng:
Structure of A16/G9 (G9 mutant - H44Y) of Vaccinia virus in complex with VHH D07
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-9hpa:
Structure of A16/G9 (vaccinia virus) in complex with VHH D07 and VHH E12
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

PDB-9r09:
Structure of A16/G9 (vaccinia virus) in complex with VHH D07 at pH 5.7
Method: X-RAY DIFFRACTION / Resolution: 2.45 Å

PDB-9r0b:
Structure of A16/G9 (vaccinia virus) in complex with VHH D07 at pH 6.5
Method: X-RAY DIFFRACTION / Resolution: 2.45 Å

PDB-9r0j:
Structure of A16/G9 (vaccinia virus) in complex with VHH D07 at pH 7.2
Method: X-RAY DIFFRACTION / Resolution: 2.45 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

ChemComp-K:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

ChemComp-SO4:
SULFATE ION

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

ChemComp-GOL:
GLYCEROL

Source
  • Vaccinia virus
  • vaccinia virus western reserve
  • vicugna pacos (alpaca)
KeywordsVIRAL PROTEIN / poxvirus / viral fusion / vaccinia virus / mpox virus

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