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Escherichia coli ampicillin resistance

Complicated exacerbation FEV, less than 50% predicted Comorbid cardiac disease Greater than or equal to 3 exacerbations per year Antibiotic therapy in the previous 3 months Above organisms plus drug-resistant pneumococci, P-lactamase-producing H. influenzae and M. catarrhalis, Escherichia coli, Proteus spp., Enterobacter spp., Klebsiella pneumoniae Oral P-Lactam/P-Iactamase inhibitor (amoxicil 1 i n-clavulanate) Fluoroquinolone with enhanced pneumococcal activity (levofloxacin, gemifloxacin, moxifloxacin) Intravenous P-Iactam/P-Iactamase inhibitor (ampicillin-sulbactam) Second- or third-generation cephalosporin (cefuroxime, ceftriaxone) Fluoroquinolone with enhanced pneumococcal activity (levofloxacin, moxifloxacin)... [Pg.241]

Ampicillin is the standard penicillin that has broad-spectrum activity. Increasing Escherichia coli resistance has limited amoxicillin use in acute cystitis. Drug of choice for enterococci sensitive to penicillin. Amoxidllin-davulanate is preferred for resistance problems. [Pg.560]

Amoxicillin, ampicillin and sulfonamides are no longer reliable agents as 25-35% of Escherichia coli are now resistant. When bacteruria occurs under therapy, resistance must be suspected. [Pg.528]

Hoyle, D.V., Shaw, D.J., Knight, H.I., Davison, H.C., Pearce, M.C., Fow, J.C., Gunn, G.J. and Woolhouse, M.E.J. 2004. Age-related decline in carriage of ampicillin-resistant Escherichia coli in young calves. Applied and Environmental Microbiology 70 6927-6930. [Pg.325]

The result suggested that thioridazine was able to eliminate different antibiotic resistances singly or jointly in Escherichia coli strains and Shigella flexneri 6 BDC1 quite efficiently, but had a much weaker effect on Vibrio cholerae (Table 42). The pattern of elimination further indicated that penicillin, ampicillin, and amoxicillin were determined by a single plasmid in these bacteria. It seems that effective elimination depended on the curing concentrations, which were close to the MIC value of thioridazine for any... [Pg.125]

Fig. 16. Map of the plasmid used for expression of flavocytochrome 62 in Escherichia coli. The flavocytochrome 62 coding region (CYB2) is located between a strong E. coli promoter (p) and terminator (t). Selection is based on ampicillin resistance conferred by the /3-lactamase gene (bla). coRI, BglU, and HindW. cleavage sites are indicated ori, origin of replication cat, chloramphenicol acetyltransferase coding sequence rbs, ribosome-binding site. Fig. 16. Map of the plasmid used for expression of flavocytochrome 62 in Escherichia coli. The flavocytochrome 62 coding region (CYB2) is located between a strong E. coli promoter (p) and terminator (t). Selection is based on ampicillin resistance conferred by the /3-lactamase gene (bla). coRI, BglU, and HindW. cleavage sites are indicated ori, origin of replication cat, chloramphenicol acetyltransferase coding sequence rbs, ribosome-binding site.
Fig. 24.1 Simplified diagram of the plasmid pUCl 8. lacZ represents the insertional inactivation marker coding for fl-galactosidase activity. A multiple cloning site (MCS) is present within the LacZ gene to enable the cloning of DNA fragments. Ori represents the origin of replication which, in this case, works in Escherichia coli. Finally, Ampr represents an ampicillin resistance marker. Fig. 24.1 Simplified diagram of the plasmid pUCl 8. lacZ represents the insertional inactivation marker coding for fl-galactosidase activity. A multiple cloning site (MCS) is present within the LacZ gene to enable the cloning of DNA fragments. Ori represents the origin of replication which, in this case, works in Escherichia coli. Finally, Ampr represents an ampicillin resistance marker.
ScFv into the culture media. Escherichia coli strain XLl/Blue was transformed with pEScFv 2G42D7 plasmid, and plasmid DNA was obtained by alkaline lysis (57) from the ampicillin-resistant line. [Pg.176]

Enterohemorrhagic Escherichia coli (EHEC) 0157 H7 causes serious hemorrhagic colitis, thrombotic thrombocytopenic purpura, and hemolytic uremic syndrome in humans. Verotoxins produced by EHEC are the pathogens of these diseases. Two different verotoxins have been reported, VTl and VT2, that destroy mucosa and renal epithelium. The effect of macrolides at sub-MIC concentration was reported on the production of verotoxin (VT) by E. coli 0157. Nakata et al observed that the production of VTl was suppressed up to 10 hr when bacteria were incubated with 1/100 of MIC of CAM [83]. The production of VTl reached the control level after 22 hr even with 1/10 of MIC of CAM. On the other hand, production of VT2 was completely suppressed by 22 hr with 1/10 of MIC. This effect was observed when E. coli 0157 was incubated with EM. In contrast to the macrolides, ampicillin at sub-MIC levels did not inhibit the production of both VTl and VT2. To clarify the mechanism of suppression of VT production by macrolides, a macrolide-resistant gene of a S. pneumonia strain, the ermAM gene, encoding an enzyme of methylation of 23S RNA was transformed into an... [Pg.556]

Antibacterial activities of novel active pharmaceutical ingredient ionic liquids based on ampicillin 31 have been evaluated (14MI4301). Structural and mechanistic insights into New Delhi metallo-P-lactamase catalyzed hydrolysis of cephalosporins have been reported (14JA14694). The hydrolysis of the antibiotic meropenem 32 by Escherichia coli cells carrying the gene for New Delhi metallo-P-lactamase, which confers antibiotic resistance, has been monitored by NMR spectroscopy in real time (14AGE2130). An... [Pg.96]

Camara JE, Hays FA. Discrimination between wild-type and ampicillin-resistant Escherichia coli by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Anal Bioanal Chem. 2007 389 1633-8. [Pg.44]

Xu C, Lin X, Ren H, Zhang Y, Wang S, Peng X. Analysis of outer membrane proteome of Escherichia coli related to resistance to ampicillin and tetracycline. Proteomics. 2006 6 462-73. [Pg.304]


See other pages where Escherichia coli ampicillin resistance is mentioned: [Pg.106]    [Pg.434]    [Pg.166]    [Pg.476]    [Pg.1]    [Pg.311]    [Pg.434]    [Pg.225]    [Pg.36]    [Pg.263]    [Pg.14]    [Pg.62]    [Pg.76]    [Pg.59]    [Pg.16]    [Pg.14]    [Pg.95]    [Pg.258]   
See also in sourсe #XX -- [ Pg.181 ]




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