Prevalence of Extended-Spectrum β-Lactamase-Producing Multidrug-Resistant Escherichia coli Among Isolates from Community-Acquired Infections and In Silico Structural Modeling of an ESBL Protein

Escherichia coli is a common major cause of bacterial infections in tea tribe patients of the northeast region of Assam, India. In this study, we documented multidrug resistance (MDR) and the prevalence of extended-spectrum β-lactamases (ESBLs) among 148 E. coli strains that were isolated from bacte...

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Veröffentlicht in:Microbial drug resistance (Larchmont, N.Y.) N.Y.), 2014-04, Vol.20 (2), p.17-176
Hauptverfasser: Rajapandiyan, Krishnamoorthy, Shanthi, Subbarayan, Vijayalakshmi, Periyasamy, Daisy, Pitchai, Murugan, Munusamy, Ranjitsingh, Amirtham Jacob Appadurai
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Sprache:eng
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Zusammenfassung:Escherichia coli is a common major cause of bacterial infections in tea tribe patients of the northeast region of Assam, India. In this study, we documented multidrug resistance (MDR) and the prevalence of extended-spectrum β-lactamases (ESBLs) among 148 E. coli strains that were isolated from bacterial infections in tea tribe patients who had a history of self-medication. High prevalence of resistance to ampicillin (82%), amoxicillin (68%), cefixime (60%), norfloxacin (60%), nalidixic acid (60%), and co-trimoxazole (53%) was observed. Of 148 E. coli isolates, 38 (26%) were confirmed as ESBL producers. The ESBL genes were sequenced from highly resistant ESBL producing E. coli isolates. Molecular modeling was performed using MODELLER 9v10 software to determine the three-dimensional structure of a protein. This result indicates that the prevailing reason for the high prevalence of antibiotic resistance in this community is prior exposure to low-quality antibiotics, hence MDR in E. coli is increasing. ESBLs are enzymes that are produced by resistant bacteria that hydrolyze advanced generations of cephalosporin antibiotics and cause resistance, even in patients with community-acquired infections. So our results provide a framework for understanding the structure and possible binding sites of ESBL proteins for drug targeting, and the results were found to be reliable.
ISSN:1076-6294
1931-8448
DOI:10.1089/mdr.2013.0088