Biomaterial Database

Role of AmpD, OprF and penicillin-binding proteins in beta-lactam resistance in clinical isolates of Pseudomonas aeruginosa. 2007

Simona Bratu, and David Landman, and Jyoti Gupta, and John Quale

Division of Infectious Diseases, State University of New York Downstate Medical Center, 450 Clarkson Avenue, Brooklyn, NY 11203, USA.

In this study, the mechanisms leading to increased chromosomal AmpC beta-lactamase expression and the contributory roles of the outer-membrane protein OprF and penicillin-binding proteins were analysed in 33 characterized clinical isolates of Pseudomonas aeruginosa. The genes ampD and ampE were analysed by PCR and DNA sequencing. Expression of the gene oprF was assessed using real-time RT-PCR, and penicillin-binding proteins were analysed using a chemiluminescence assay. Several of the isolates with increased ampC expression had major deletions affecting ampD, although in some isolates the mechanism of increased ampC expression could not be ascertained. Occasional isolates had increased expression of both ampC and oprF but remained susceptible to cephalosporins, suggesting that increased beta-lactamase activity could not offset increased outer-membrane permeability. There were no discernible changes in penicillin-binding proteins. Genomic deletions in ampD were observed in selected clinical isolates of P. aeruginosa with increased expression of the AmpC beta-lactamase. For some isolates, cephalosporin resistance was dependent upon the interplay of ampC and oprF expression.

UI	MeSH Term	Description	Entries
D008163	Luminescent Measurements	Techniques used for determining the values of photometric parameters of light resulting from LUMINESCENCE.	Bioluminescence Measurements,Bioluminescent Assays,Bioluminescent Measurements,Chemiluminescence Measurements,Chemiluminescent Assays,Chemiluminescent Measurements,Chemoluminescence Measurements,Luminescence Measurements,Luminescent Assays,Luminescent Techniques,Phosphorescence Measurements,Phosphorescent Assays,Phosphorescent Measurements,Assay, Bioluminescent,Assay, Chemiluminescent,Assay, Luminescent,Assay, Phosphorescent,Assays, Bioluminescent,Assays, Chemiluminescent,Assays, Luminescent,Assays, Phosphorescent,Bioluminescence Measurement,Bioluminescent Assay,Bioluminescent Measurement,Chemiluminescence Measurement,Chemiluminescent Assay,Chemiluminescent Measurement,Chemoluminescence Measurement,Luminescence Measurement,Luminescent Assay,Luminescent Measurement,Luminescent Technique,Measurement, Bioluminescence,Measurement, Bioluminescent,Measurement, Chemiluminescence,Measurement, Chemiluminescent,Measurement, Chemoluminescence,Measurement, Luminescence,Measurement, Luminescent,Measurement, Phosphorescence,Measurement, Phosphorescent,Measurements, Bioluminescence,Measurements, Bioluminescent,Measurements, Chemiluminescence,Measurements, Chemiluminescent,Measurements, Chemoluminescence,Measurements, Luminescence,Measurements, Luminescent,Measurements, Phosphorescence,Measurements, Phosphorescent,Phosphorescence Measurement,Phosphorescent Assay,Phosphorescent Measurement,Technique, Luminescent,Techniques, Luminescent
D008565	Membrane Proteins	Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.	Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D009238	N-Acetylmuramoyl-L-alanine Amidase	An autolytic enzyme bound to the surface of bacterial cell walls. It catalyzes the hydrolysis of the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell wall glycopeptides, particularly peptidoglycan. EC 3.5.1.28.	Mucopeptide Amidohydrolase,Autolysin,LE-Enzyme,Murein Hydrolase,Peptidoglycan Hydrolase,T7 Endolysin,T7 Lysozyme,Amidase, N-Acetylmuramoyl-L-alanine,Amidohydrolase, Mucopeptide,Endolysin, T7,Hydrolase, Murein,Hydrolase, Peptidoglycan,LE Enzyme,Lysozyme, T7,N Acetylmuramoyl L alanine Amidase
D011550	Pseudomonas aeruginosa	A species of gram-negative, aerobic, rod-shaped bacteria commonly isolated from clinical specimens (wound, burn, and urinary tract infections). It is also found widely distributed in soil and water. P. aeruginosa is a major agent of nosocomial infection.	Bacillus aeruginosus,Bacillus pyocyaneus,Bacterium aeruginosum,Bacterium pyocyaneum,Micrococcus pyocyaneus,Pseudomonas polycolor,Pseudomonas pyocyanea
D011552	Pseudomonas Infections	Infections with bacteria of the genus PSEUDOMONAS.	Infections, Pseudomonas,Pseudomonas aeruginosa Infection,Infection, Pseudomonas,Pseudomonas Infection,Pseudomonas aeruginosa Infections
D004269	DNA, Bacterial	Deoxyribonucleic acid that makes up the genetic material of bacteria.	Bacterial DNA
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D001425	Bacterial Outer Membrane Proteins	Proteins isolated from the outer membrane of Gram-negative bacteria.	OMP Proteins,Outer Membrane Proteins, Bacterial,Outer Membrane Lipoproteins, Bacterial
D001426	Bacterial Proteins	Proteins found in any species of bacterium.	Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial
D001618	beta-Lactamases	Enzymes found in many bacteria which catalyze the hydrolysis of the amide bond in the beta-lactam ring. Well known antibiotics destroyed by these enzymes are penicillins and cephalosporins.	beta-Lactamase,beta Lactamase,beta Lactamases