Alpha hemolysin enhances the immune response by modulating dendritic cell differentiation via ADAM10-Notch signaling.

ABSTRACT: Alpha hemolysin, a pore-forming toxin from Staphylococcus aureus, is a critical virulence factor for bacteria. Previous studies have demonstrated that the Hla mutant H35A (Hla_H35A) serves as a potent carrier protein for subunit vaccines, yet its immunomodulatory mechanisms remain incompletely understood. Here, we demonstrate that the Hla_H35A fusion enhances vaccine efficacy by targeting A Disintegrin and Metalloproteinase 10 (ADAM10) on dendritic cells (DCs), thereby activating the ADAM10-Notch signaling axis. Using the candidate antigen PA0833 from Pseudomonas aeruginosa as a model, we show that the Hla_H35A-PA0833 fusion protein (HPF) significantly augments antigen uptake, DC maturation, and Notch-dependent transcriptional programs, particularly in convent

SUBMITTER: Wang K 

PROVIDER: S-EPMC12508477 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature