Antigen self-anchoring onto bacteriophage T5 capsid-like particles for vaccine design

Emeline Vernhes, Linda Larbi Chérif, Nicolas Ducrot, Clément Vanbergue, Malika Ouldali, Lena Zig, N’diaye Sidibe, Sylviane Hoos, Luis Ramirez-Chamorro, Madalena Renouard, Ombeline Rossier, Patrick England, Guy Schoehn, Pascale Boulanger, Karim Benihoud

    Résultats de recherche: Contribution à un journalArticleRevue par des pairs

    Résumé

    The promises of vaccines based on virus-like particles stimulate demand for universal non-infectious virus-like platforms that can be efficiently grafted with large antigens. Here, we harnessed the modularity and extreme affinity of the decoration protein pb10 for the capsid of bacteriophage T5. SPR experiments demonstrated that pb10 fused to mCherry or to the model antigen ovalbumin (Ova) retained picomolar affinity for DNA-free T5 capsid-like particles (T5-CLPs), while cryo-EM studies attested to the full occupancy of the 120 capsid binding sites. Mice immunization with CLP-bound pb10-Ova chimeras elicited strong long-lasting anti-Ova humoral responses involving a large panel of isotypes, as well as CD8+ T cell responses, without any extrinsic adjuvant. Therefore, T5-CLP constitutes a unique DNA-free bacteriophage capsid able to display a regular array of large antigens through highly efficient chemical-free anchoring. Its ability to elicit robust immune responses paves the way for further development of this novel vaccination platform.

    langue originaleAnglais
    Numéro d'article6
    journalnpj Vaccines
    Volume9
    Numéro de publication1
    Les DOIs
    étatPublié - 1 déc. 2024

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