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© Ahmed Haouz
Cristaux d'une protéine de Mycobacterium tuberculosis produits dans le cadre du Grand Programme Horizontal sur la Tuberculose à l'Institut Pasteur. La caractérisation structurale de protéines mycobactériennes aide à une meilleure compréhension de la physiologie et de la pathogénicité des mycobactéries et fournit un point de départ pour la conception de nouveaux agents antibactériens.
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Cell - 18 Aug 2025

Meola A, Vernuccio R, Battini L, Albericio G, Delgado P, Bamford R, Pokorny L, Broutin M, Martínez León A, Gallien S, Gil M, Noriega MA, Guivel-Benhassine F, Porrot F, Postal J, Buchrieser J, Hubert M, Haouz A, Lafaye P, Esteban M, Hub JS, Mahévas M, Chappert P, Mercer J, Garcia-Arriaza J, Schwartz O, Guardado-Calvo P

Link to Pubmed [PMID] – 40865523

Link to DOI – 10.1016/j.cell.2025.07.040

Cell 2025 Aug; ():

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.