{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["72(7)"],"submitter":["Protze J"],"pubmed_abstract":["Clostridium perfringens enterotoxin (CPE) binds to distinct claudins (Clds), which regulate paracellular barrier functions in endo- and epithelia. The C-terminal domain (cCPE) has the potential for selective claudin modulation, since it only binds to a subset of claudins, e.g., Cld3 and Cld4 (cCPE receptors). Cld5 (non-CPE receptor) is a main constituent in tight junctions (TJ) of the blood-brain barrier. We aimed to reveal claudin recognition mechanisms of cCPE and to create a basis for a Cld5-binder. By utilizing structure-based interaction models, mutagenesis and assays of cCPE-binding to the TJ-free cell line HEK293, transfected with human Cld1 and murine Cld5, we showed how cCPE-binding to Cld1 and Cld5 is prevented by two residues in extracellular loop 2 of Cld1 (Asn(150) and Thr(153"],"journal":["Cellular and molecular life sciences : CMLS"],"pagination":["1417-32"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11113963"],"repository":["biostudies-literature"],"pubmed_title":["Directed structural modification of Clostridium perfringens enterotoxin to enhance binding to claudin-5."],"pmcid":["PMC11113963"],"pubmed_authors":["Blecharz KG","Eichner M","Protze J","Piontek J","Vajkoczy P","Piontek A","Rossa J","Dinter S","Krause G"],"additional_accession":[]},"is_claimable":false,"name":"Directed structural modification of Clostridium perfringens enterotoxin to enhance binding to claudin-5.","description":"Clostridium perfringens enterotoxin (CPE) binds to distinct claudins (Clds), which regulate paracellular barrier functions in endo- and epithelia. The C-terminal domain (cCPE) has the potential for selective claudin modulation, since it only binds to a subset of claudins, e.g., Cld3 and Cld4 (cCPE receptors). Cld5 (non-CPE receptor) is a main constituent in tight junctions (TJ) of the blood-brain barrier. We aimed to reveal claudin recognition mechanisms of cCPE and to create a basis for a Cld5-binder. By utilizing structure-based interaction models, mutagenesis and assays of cCPE-binding to the TJ-free cell line HEK293, transfected with human Cld1 and murine Cld5, we showed how cCPE-binding to Cld1 and Cld5 is prevented by two residues in extracellular loop 2 of Cld1 (Asn(150) and Thr(153","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Apr","modification":"2026-06-02T06:14:47.372Z","creation":"2026-04-15T03:14:52.562Z"},"accession":"S-EPMC11113963","cross_references":{"pubmed":["25342221"],"doi":["10.1007/s00018-014-1761-6"]}}