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Title: Proteomic Analysis of DNA Starvation/Stationary Phase Protection Proteins from Extended Spectrum β – Lactamase Producing Escherichia coli
Authors: Siriwoot Sookkhee
Banyong Khantawa
Wachiraphorn Srihinkong
Authors: Siriwoot Sookkhee
Banyong Khantawa
Wachiraphorn Srihinkong
Keywords: ESBL;Escherichia coli;Ciprofloxacin;DNA starvation;stationary phase protection proteins;Proteomic analysis
Issue Date: 2017
Publisher: Chiang Mai University
Citation: Chiang Mai University (CMU) Journal of Natural Sciences 16, 3 (Jul-Sep 2017), 215-230
Abstract: Escherichia coli, especially the extended-spectrum β-lactamase producing E. coli (ESBL-EC), is the most frequent cause of urinary tract infections. They are not only resistant to β - lactams, but also may be resistant to other drugs, such as ciprofloxacin (CIP). This study aims to identify the proteins related to its CIP resistance using proteomic analysis by isolating ESBL-EC from urine specimens, and comparing the significantly different intracellular proteins extracted from these high-resistant isolates, with or without ciprofloxacin. Among 2,072 uropathogenic E. coli that were screened, 1,644 (79.34%) were confirmed as ESBL-EC isolates. Based on the minimal inhibitory concentrations (MIC) of ceftazidime (CAZ) and ciprofloxacin, 193 isolates (12.12%) exhibited high-level resistance (CAZHRCIPHR). Fourteen isolates of (CAZHRCIPHR) and a representative isolate each of intermediate resistance (CAZI CIPI) and resistance (CAZR CIPR) were selected to detect the different protein bands. They were cultured in Mueller Hinton broth (MHB) with various concentrations of CIP or without CIP. Intracellular protein of each selected isolate was separately extracted, detected, and compared by SDS – PAGE. Interestingly, we found a distinct intracellular protein band at approximately 19 kDa in the presence of ciprofloxacin after extracting from the MHB culture. Comparative analysis by 2-D gel revealed 10 protein spots at an interesting range of molecular weight; these were selected and further analyzed with LC-MS/MS. Proteomic identification showed that two of these protein spots matched a DNA starvation/stationary phase protection protein. This protein is responsible for protecting DNA from damage by ciprofloxacin. This protein may play a role in maintaining ciprofloxacin tolerance in ESBL-EC when MIC of ciprofloxacin is increased.
Description: Chiang Mai University (CMU) Journal of Natural Sciences is dedicated to the publication of original research in Sciences &Technology and the Health Sciences. Submissions are welcomed from CMU, as well as other Thai and foreign institutions. All submissions must be original research not previously published or simultaneously submitted for publication. Manuscripts are peer reviewed using the double -blinded review system by at least 2 reviewers before acceptance. The CMU Journal of Natural Sciences is published four times a year, in January, April, July and October.
ISSN: 2465-4337
Appears in Collections:CMUL: Journal Articles

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