{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Scharnow AM"],"funding":["Division of Chemistry","NIDCR NIH HHS","NIAID NIH HHS","National Institute of Dental and Craniofacial Research","Division of Microbiology and Infectious Diseases","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["23449-23456"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11345752"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["146(33)"],"pubmed_abstract":["Natural products are important precursors for antibiotic drug design. These chemical scaffolds serve as synthetic inspiration for chemists who leverage their structures to develop novel antibacterials and chemical probes. We have previously studied carolacton, a natural product macrolactone from<i>Sorangium cellulosum</i>, and discovered a simplified derivative, <b>A2</b>, that maintained apparent biofilm inhibitory activity, although the biological target was unknown. Herein, we utilize affinity-based protein profiling (AfBPP) <i>in situ</i> during biofilm formation to identify the protein target using a photoexcitable cross-linking derivative of <b>A2</b>. From these studies, we identified glucan binding protein B (GbpB), a peptidoglycan hydrolase, as the primary target of <b>A2</b>. Fur"],"journal":["Journal of the American Chemical Society"],"pubmed_title":["In Situ Biofilm Affinity-Based Protein Profiling Identifies the Streptococcal Hydrolase GbpB as the Target of a Carolacton-Inspired Chemical Probe."],"pmcid":["PMC11345752"],"funding_grant_id":["AI148752","DE022350","AI149778","CHE1531620","R35 GM119426","T32 GM007753","DE025837","R01 DE022350","T90 DE030859","R01 DE025837","CHE1755698","R01 AI148752","GM119426","R01 AI149778","DE030859","GM007753"],"pubmed_authors":["Drechsel I","Sieber SA","Scharnow AM","Zhang H","Shaw E","Wuest WM","Page JE","Solinski AE","Rowe S","Wu H"],"additional_accession":[]},"is_claimable":false,"name":"In Situ Biofilm Affinity-Based Protein Profiling Identifies the Streptococcal Hydrolase GbpB as the Target of a Carolacton-Inspired Chemical Probe.","description":"Natural products are important precursors for antibiotic drug design. These chemical scaffolds serve as synthetic inspiration for chemists who leverage their structures to develop novel antibacterials and chemical probes. We have previously studied carolacton, a natural product macrolactone from<i>Sorangium cellulosum</i>, and discovered a simplified derivative, <b>A2</b>, that maintained apparent biofilm inhibitory activity, although the biological target was unknown. Herein, we utilize affinity-based protein profiling (AfBPP) <i>in situ</i> during biofilm formation to identify the protein target using a photoexcitable cross-linking derivative of <b>A2</b>. From these studies, we identified glucan binding protein B (GbpB), a peptidoglycan hydrolase, as the primary target of <b>A2</b>. Fur","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Aug","modification":"2026-06-03T03:46:32.198Z","creation":"2024-11-21T10:56:17.83Z"},"accession":"S-EPMC11345752","cross_references":{"pubmed":["39133525"],"doi":["10.1021/jacs.4c06658"]}}