Inhibition of Pseudomonas aeruginosa exoenzyme expression by subinhibitory antibiotic concentrations
نویسندگان
چکیده
منابع مشابه
Effect of Subinhibitory concentrations of imipenem and piperacillin on transcriptional expression of algD and lasB genes in Pseudomonas aeruginosa
Sub Minimal Inhibitory concentrations (sub-MIC) of antibiotics, although not able to kill bacteria, can be effect on their physico- chemical characteristics and functions. This study aimed to investigate the effect of sub-MIC of imipenem and piperacillin on the transcriptional expression of virulence related genes algD and lasB in Pseudomonas auroginosa. Five clinical isolates of P. aeruginosa ...
متن کاملPurification of Pseudomonas aeruginosa exoenzyme S.
Pseudomonas aeruginosa produces two distinct ADP-ribosyl transferases, exotoxin A and exoenzyme S, which differ in a number of properties including substrate specificity. Exoenzyme S was purified from culture supernatants of P. aeruginosa DG1. The procedure for purification consists of four major steps: ammonium sulfate precipitation, anion-exchange chromatography on DEAE-Sephacel, acetone prec...
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Exoenzyme S from Pseudomonas aeruginosa has been studied as an adhesion for glycosphingolipids and buccal cells. Binding of exoenzyme S to gangliotriosylceramide (GalNAc beta 1-4Gal beta 1-4Glc beta 1-1Cer), gangliotetraosylceramide (Gal beta 1-3 GalNAcT beta 1-4 Gal beta 1-4Glc beta 1-1Cer), and lactosylceramide (Gal beta 1-4Glc beta 1-1Cer) separated on thin-layer chromatograms was observed. ...
متن کاملInhibition of bacterial adhesion by subinhibitory concentrations of antibiotics.
BACKGROUND Urinary Tract Infections (UTIs) due to Escherichia coli is one of the most common diseases encountered in clinical practice. Most common recognised pathogenic factor in E.coli is adhesion. There is accumulating evidence that through subinhibitory concentrations (sub-MICs) of many antibiotics do not kill bacteria, they are able to interfere with some important aspects of bacterial cel...
متن کاملPurification and characterization of exoenzyme S from Pseudomonas aeruginosa 388.
Exoenzyme S was purified > 1,500-fold from the culture supernatant fluid of Pseudomonas aeruginosa 388 at high yield without utilization of solvents or detergents. Two proteins, with apparent molecular sizes of 53 and 49 kDa, cofractionated with exoenzyme S activity. Rabbit anti-49-kDa-protein immunoglobulin G was prepared by using sodium dodecyl sulfate-polyacrylamide gel electrophoresis-purif...
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ژورنال
عنوان ژورنال: Antimicrobial Agents and Chemotherapy
سال: 1989
ISSN: 0066-4804,1098-6596
DOI: 10.1128/aac.33.1.41