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HideToolbar: false HideMenubar: false HideWindowUI: false FitWindow: false CenterWindow: false DisplayDocTitle: false NonFullScreenPageMode: UseNone Direction: L2R ViewArea: CropBox ViewClip: CropBox PrintArea: CropBox PageClip: CropBox PageLayout: SinglePage PageMode: UseOutlines Language: en-US Outlines: Item: Title: An acyl-homoserine lactone acylase found in Stenotrophomonas maltophilia exhibits both quorum quenching activity and the ability to degrade penicillin antibiotics Children: Item: Title: Results Children: Item: Title: Smlt1522 belongs to the bacterial N-acyl-L-homoserine lactones acylase group B Item: Title: S. maltophilia K279a can degrade AHLs through Smlt1522 Item: Title: Purified recombinant Smlt1522 heterologously expressed in E. coli shows penicillin-degrading activity Item: Title: Smlt1522 has dual activity capable of degrading diverse AHLs and penicillin antibiotics Item: Title: Potential physiological role of Smlt1522 in S. maltophilia Item: Title: Sequence variability and selective pressure detected on gene smlt1522 among S. maltophilia strains Item: Title: Discussion Item: Title: Methods Children: Item: Title: Bacterial strains and general growth conditions Item: Title: Chemical reagents Item: Title: Smlt1522 protein production in Escherichia coli and purification Item: Title: Construction of K279a smlt1522 markerless deletion mutant and complementation Item: Title: Extraction of AHLs Item: Title: Bioassay for AHL activity detection Item: Title: In vivo AHL-degrading activity Item: Title: Analyses of AHLs and beta-lactam antibiotics degradation in vitro Item: Title: Metabolite analyses of C10-HSL and Piperacillin degradation Item: Title: Antimicrobial susceptibility testing Item: Title: Bacterial phenotypic assays Item: Title: Protein sequence and structural analysis Item: Title: Sequence diversity and phylogenetic analysis Item: Title: Statistical analysis Item: Title: References Info: Creator: Adobe InDesign 18.3 (Windows) Producer: 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