{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wang K"],"funding":["National Natural Science Foundation of China","National Natural Science Foundation of China (National Science Foundation of China)"],"pagination":["334"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12508477"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(1)"],"pubmed_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<sub>H35A</sub>) serves as a potent carrier protein for subunit vaccines, yet its immunomodulatory mechanisms remain incompletely understood. Here, we demonstrate that the Hla<sub>H35A</sub> 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<sub>H35A</sub>-PA0833 fusion protein (HPF) significantly augments antigen uptake, DC maturation, and Notch-dependent transcriptional programs, particularly in convent"],"journal":["Signal transduction and targeted therapy"],"pubmed_title":["Alpha hemolysin enhances the immune response by modulating dendritic cell differentiation via ADAM10-Notch signaling."],"pmcid":["PMC12508477"],"funding_grant_id":["32300778","32170938"],"pubmed_authors":["Jing H","Liao Y","Gou Q","Xia Z","Yan P","Zhang J","Sun T","Zhao Z","Wang K","Liao J","Chen Z","Zhang X","Zou Q","Liang M","Yu T","Zeng H","Tang Y","Yu X","Yuan Y"],"additional_accession":[]},"is_claimable":false,"name":"Alpha hemolysin enhances the immune response by modulating dendritic cell differentiation via ADAM10-Notch signaling.","description":"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<sub>H35A</sub>) serves as a potent carrier protein for subunit vaccines, yet its immunomodulatory mechanisms remain incompletely understood. Here, we demonstrate that the Hla<sub>H35A</sub> 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<sub>H35A</sub>-PA0833 fusion protein (HPF) significantly augments antigen uptake, DC maturation, and Notch-dependent transcriptional programs, particularly in convent","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Oct","modification":"2026-06-04T09:15:51.447Z","creation":"2026-06-01T03:06:44.801Z"},"accession":"S-EPMC12508477","cross_references":{"pubmed":["41062455"],"doi":["10.1038/s41392-025-02432-3"]}}