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Non-typhoid Salmonella spp. resistant to cefotaxime
The Journal of Antimicrobial Chemotherapy
|October 1, 1995
Summary
Beta-lactamase enzymes, including TEM-1 and an extended-spectrum variant, were found in cefotaxime-resistant Salmonella serovars in Argentina. These enzymes contribute to antibiotic resistance in the bacterial strains.
Area of Science:
- Microbiology
- Molecular Biology
- Antimicrobial Resistance
Background:
- Salmonella spp. are significant foodborne pathogens.
- Antimicrobial resistance in Salmonella poses a global health threat.
- Beta-lactamase enzymes are a primary mechanism of resistance to beta-lactam antibiotics.
Purpose of the Study:
- To investigate the presence and types of beta-lactamases in cefotaxime-resistant Salmonella serovars from Argentina.
- To identify specific beta-lactamase enzymes conferring resistance.
Main Methods:
- Detection of beta-lactamases by analyzing enzyme hydrolysis of ampicillin and ceftriaxone.
- Isoelectric focusing (pI) to characterize the detected beta-lactamases.
Main Results:
- Two distinct beta-lactamases with isoelectric points (pIs) of 5.4 and 8.1 were identified.
- The beta-lactamase with pI 5.4 was identified as TEM-1.
- An unidentified extended-spectrum beta-lactamase was detected in the resistant Salmonella strains.
Conclusions:
- The spread of TEM-1 and an extended-spectrum beta-lactamase is evident in Salmonella serovars in Argentina.
- These findings highlight the growing challenge of antimicrobial resistance in Salmonella.
- Further characterization of the unidentified extended-spectrum beta-lactamase is warranted.