{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Borgini S"],"funding":["National Institute of Allergy and Infectious Diseases","French National Research Agency","Federation of Wallonia and Brussels","National Institutes of Health","Fund for Scientific Research","Research Foundation Flanders"],"pagination":["111113"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12853789"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["302(2)"],"pubmed_abstract":["Bacteroidales are abundant Gram-negative bacteria present in the gut microbiota of most animals, including humans, where they carry out vital functions for host health. To thrive in this competitive environment, Bacteroidales use sophisticated weapons to outmatch competitors. Among these, Bacteroidales secreted antimicrobial proteins (BSAPs) represent a novel class of bactericidal pore-forming toxins that are highly specific to their receptor, typically targeting only a single membrane protein or lipopolysaccharide. The molecular determinants conferring this high selectivity remain unknown. In this study, we therefore investigated the model protein BSAP-1 and determined which of its domains is involved in providing receptor specificity. We demonstrate that receptor recognition is entirely "],"journal":["The Journal of biological chemistry"],"pubmed_title":["Identification of receptor-binding domains of Bacteroidales antibacterial pore-forming toxins."],"pmcid":["PMC12853789"],"funding_grant_id":["R01-GM129325","1B.274.22F","ANR-20-PAMR-0010","WELBIO-CR-2019C-03","O008818F"],"pubmed_authors":["Lauber F","Petre C","Vertommen D","Iorga BI","Remaut H","Collet JF","Borgini S","Pasveer E"],"additional_accession":[]},"is_claimable":false,"name":"Identification of receptor-binding domains of Bacteroidales antibacterial pore-forming toxins.","description":"Bacteroidales are abundant Gram-negative bacteria present in the gut microbiota of most animals, including humans, where they carry out vital functions for host health. To thrive in this competitive environment, Bacteroidales use sophisticated weapons to outmatch competitors. Among these, Bacteroidales secreted antimicrobial proteins (BSAPs) represent a novel class of bactericidal pore-forming toxins that are highly specific to their receptor, typically targeting only a single membrane protein or lipopolysaccharide. The molecular determinants conferring this high selectivity remain unknown. In this study, we therefore investigated the model protein BSAP-1 and determined which of its domains is involved in providing receptor specificity. We demonstrate that receptor recognition is entirely ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Dec","modification":"2026-06-15T04:59:26.123Z","creation":"2026-06-15T03:08:34.09Z"},"accession":"S-EPMC12853789","cross_references":{"pubmed":["41475548"],"doi":["10.1016/j.jbc.2025.111113"]}}