Int J Environ Res Public Health
April 2021
Botulinum neurotoxins are considered as one of the most potent toxins and are produced by . It is crucial to have a rapid and sensitive method to detect the bacterium in food. In this study, a rapid detection assay of in food using loop-mediated isothermal amplification (LAMP) technology was developed.
View Article and Find Full Text PDFDegradation efficiency of Atrazine by Klebsiella variicola FH-1 is improved by the addition of Zn. Both the chromosome and plasmid genomes of strain FH-1 were sequenced and annotated to identify genes involved in the degradation of Atrazine. Four open reading frames (ORFs) 1040, 2582, 3597, and 4043 encoding Zn-dependent hydrolases were knocked out to verify their predicted functions in the degradation of Atrazine.
View Article and Find Full Text PDFMicrobiology (Reading)
October 2011
The integrase IntI1 catalyses recombination of antibiotic-resistance gene cassettes in the integron, a widely found bacterial mobile element active in spreading antibiotic multi-resistance. We have previously shown that resistance cassette recombination rate and specificity depend on the amount of intracellular integrase. Here, we used in vivo and in vitro methods to examine convergent expression of the integrase promoter (P(int)) and of the cassette promoters (P(c) and P(2)) in the prototypical plasmid-borne class 1 integron, In2.
View Article and Find Full Text PDFUSA300 methicillin-resistant Staphylococcus aureus (MRSA) isolates are usually resistant only to oxacillin, erythromycin, and, increasingly, levofloxacin. Of these, oxacillin and levofloxacin resistances are chromosomally encoded. Plasmid-mediated clindamycin, mupirocin, and/or tetracycline resistance has been observed among USA300 isolates, but these descriptions were limited to specific patient populations or isolated occurrences.
View Article and Find Full Text PDFIntI1 mediates the recombination of antibiotic-resistant gene cassettes between different integrons in the same cell, facilitating the persistence and dissemination of these genes. Historically, integrase activity has been measured by conjugating recombinant products from donor cells overexpressing integrase and quantifying them in recipient cells. Here we report the first measurements of the steady-state intracellular abundance of integrase-mediated recombination products in strains expressing natural or high IntI1 levels.
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