Bacterial quantification in tissue homogenates from in vivo pharmacodynamic studies using growth curves.

Bacterial quantification in tissue homogenates from in vivo pharmacodynamic studies using growth curves. J Med Microbiol. 2020 Mar 31;: Authors: Georgiou PC, Mouton JW, Pournaras S, Meletiadis J Abstract Introduction. Quantification of bacterial load in tissue homogenates in in vivo pharmacodynamic studies is cumbersome and time-consuming.Aim. We therefore developed a new method for quantifying bacterial load in tissue homogenates of animals treated with a β-lactam and β-lactamase inhibitor using growth curves.Methods. The log10 colony-forming units (c.f.u.) ml-1 of 184 thigh and lung homogenates from female CD-1 mice infected intranasally and intramuscularly with 4 Pseudomonas aeruginosa, 4 Klebsiella pneumoniae, 3 Enterobacter cloacae and 2 Escherichia coli strains treated with a β-lactam drug and tazobactam were calculated using the standard approach of serial quantitative cultures and analysis of growth curves. Growth curves were obtained with continuous (every 10 min) monitoring of optical density at 630 nm (OD630) after 20 µl tissue homogenates were inoculated in total volume of 200 µl Mueller-Hinton broth in 96-well microtitration plates and incubated at 37 °C for 18 h.Results. The best correlation between log10 c.f.u. ml-1 determined with the serial quantitative cultures and growth curves was found at the time point corresponding to an OD630 of 0.25 increase above the baseline OD (...
Source: Journal of Medical Microbiology - Category: Microbiology Authors: Tags: J Med Microbiol Source Type: research

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Source: Allergy, Asthma and Immunology Research - Category: Allergy & Immunology Tags: Allergy Asthma Immunol Res Source Type: research
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In a wide range of organisms, from bacteria to humans, numerous proteins have to be posttranslationally acylated to become biologically active. Bacterial repeats in toxin (RTX) cytolysins form a prominent group of proteins that are synthesized as inactive protoxins and undergo posttranslational acylation on ε-amino groups of two internal conserved lysine residues by co-expressed toxin-activating acyltransferases. Here, we investigated how the chemical nature, position, and number of bound acyl chains govern the activities of Bordetella pertussis adenylate cyclase toxin (CyaA), Escherichia coli α-hemolysin (Hl...
Source: Journal of Biological Chemistry - Category: Chemistry Authors: Tags: Editors ' Picks Source Type: research
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