| Literature DB >> 27977118 |
Sabine Ottilie1, Gregory M Goldgof1,2, Claudia Magalhaes Calvet3,4, Gareth K Jennings3, Greg LaMonte1, Jake Schenken1, Edgar Vigil1, Prianka Kumar1, Laura-Isobel McCall3, Eduardo Soares Constantino Lopes1,5, Felicia Gunawan1, Jennifer Yang1, Yo Suzuki2, Jair L Siqueira-Neto3, James H McKerrow3, Rommie E Amaro6, Larissa M Podust3, Jacob D Durrant7, Elizabeth A Winzeler1.
Abstract
Recent advances in cell-based, high-throughput phenotypic screening have identified new chemical compounds that are active against eukaryotic pathogens. A challenge to their future development lies in identifying these compounds' molecular targets and binding modes. In particular, subsequent structure-based chemical optimization and target-based screening require a detailed understanding of the binding event. Here, we use directed evolution and whole-genome sequencing of a drug-sensitive S. cerevisiae strain to identify the yeast ortholog of TcCyp51, lanosterol-14-alpha-demethylase (TcCyp51), as the target of MMV001239, a benzamide compound with activity against Trypanosoma cruzi, the etiological agent of Chagas disease. We show that parasites treated with MMV0001239 phenocopy parasites treated with another TcCyp51 inhibitor, posaconazole, accumulating both lanosterol and eburicol. Direct drug-protein binding of MMV0001239 was confirmed through spectrophotometric binding assays and X-ray crystallography, revealing a binding site shared with other antitrypanosomal compounds that target Cyp51. These studies provide a new probe chemotype for TcCyp51 inhibition.Entities:
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Year: 2016 PMID: 27977118 PMCID: PMC5649375 DOI: 10.1021/acschembio.6b01037
Source DB: PubMed Journal: ACS Chem Biol ISSN: 1554-8929 Impact factor: 5.100