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Comparative study of the beta-lactamase activity found in Achromobacter
Canadian Journal of Microbiology
|July 1, 1983
Summary
Achromobacter species exhibit high beta-lactamase activity, with three distinct cephalosporinases identified. These enzymes are of clinical interest due to their prevalence and unique characteristics in Gram-negative bacteria.
Area of Science:
- Microbiology
- Enzymology
- Genetics
Background:
- Achromobacter species are Gram-negative bacteria.
- Beta-lactamase activity is a significant factor in antibiotic resistance.
- Understanding beta-lactamases in Achromobacter is crucial for clinical microbiology.
Purpose of the Study:
- To characterize beta-lactamase activity in clinical isolates of Achromobacter species.
- To identify and differentiate the types of beta-lactamases present.
- To assess the clinical relevance of these enzymes.
Main Methods:
- Survey of 21 clinical Achromobacter isolates.
- Isoelectric focusing for enzyme characterization.
- Affinity chromatography, molecular weight determination, immunological identity, and genetic analysis.
- Microacidimetric method for kinetic analysis (Km, Vmax).
Main Results:
- All tested strains showed high beta-lactamase activity.
- Three distinct beta-lactamase patterns were identified in 19 strains.
- Two cephalosporinases (MULB 901, pI 7.4; MULB 905, pI 9.3) are of chromosomal origin.
- One cephalosporinase (MULB 906, pI 8.1) is plasmid-mediated (8.2 MDal) and hydrolyzes cefoxitin, cefotaxime, and moxalactam.
- Enzymes primarily function as cephalosporinases, not hydrolyzing oxacillin, cloxacillin, or methicillin.
- Beta-lactamase synthesis was constitutive in all cases.
Conclusions:
- Beta-lactamase activity is common in Achromobacter clinical isolates.
- The identified cephalosporinases are distinct from those in other Gram-negative bacteria.
- These enzymes possess significant clinical interest due to their prevalence and unique properties.