{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["301(7)"],"submitter":["Espinosa-Vinals C"],"pubmed_abstract":["Acylated domains (ADs), like that of the Bordetella pertussis adenylate cyclase toxin (CyaA), are structures found in all pore-forming toxins from the family of Repeat-in-ToXin (RTX) proteins. These AD segments are fatty-acylated on ε-amino groups of conserved lysine residues, such as the K860 and K983 residues of CyaA. The ε-amide-linked acyl chains are essential for toxin activity and promote irreversible membrane insertion of the CyaA molecule, thus enabling the toxin to translocate its N-terminal adenyl cyclase enzyme domain into the host cell cytoplasm. In parallel, the membrane-inserted CyaA molecules can oligomerize into cation-selective pores in the plasma membrane. Here, we show that the attached acyl chains are not only crucial for membrane insertion of the toxin but also play an"],"journal":["The Journal of biological chemistry"],"pagination":["110392"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12332401"],"repository":["biostudies-literature"],"pubmed_title":["Acyl chains stabilize the acylated domain and determine the receptor-mediated interaction of the Bordetella adenylate cyclase toxin with cell membrane."],"pmcid":["PMC12332401"],"pubmed_authors":["Sebo P","Espinosa-Vinals C","Bumba L","Osickova A","Jurnecka D","Stransky J","Osicka R"],"additional_accession":[]},"is_claimable":false,"name":"Acyl chains stabilize the acylated domain and determine the receptor-mediated interaction of the Bordetella adenylate cyclase toxin with cell membrane.","description":"Acylated domains (ADs), like that of the Bordetella pertussis adenylate cyclase toxin (CyaA), are structures found in all pore-forming toxins from the family of Repeat-in-ToXin (RTX) proteins. These AD segments are fatty-acylated on ε-amino groups of conserved lysine residues, such as the K860 and K983 residues of CyaA. The ε-amide-linked acyl chains are essential for toxin activity and promote irreversible membrane insertion of the CyaA molecule, thus enabling the toxin to translocate its N-terminal adenyl cyclase enzyme domain into the host cell cytoplasm. In parallel, the membrane-inserted CyaA molecules can oligomerize into cation-selective pores in the plasma membrane. Here, we show that the attached acyl chains are not only crucial for membrane insertion of the toxin but also play an","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jul","modification":"2026-04-15T19:07:11.132Z","creation":"2026-04-07T14:00:43.765Z"},"accession":"S-EPMC12332401","cross_references":{"pubmed":["40543585"],"doi":["10.1016/j.jbc.2025.110392"]}}