Antigen self-anchoring onto bacteriophage T5 capsid-like particles for vaccine design - Archive ouverte HAL Accéder directement au contenu
Pré-Publication, Document De Travail Année : 2022

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

Sylviane Hoos
Guy Schoehn

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 immunisation 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 the first DNA-free bacteriophage capsid able to irreversibly 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.

Dates et versions

hal-03870795 , version 1 (24-11-2022)

Identifiants

Citer

Emeline Vernhes, Linda Larbi Chérif, Nicolas Ducrot, Malika Ouldali, Lena Zig, et al.. Antigen self-anchoring onto bacteriophage T5 capsid-like particles for vaccine design. 2022. ⟨hal-03870795⟩
43 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More