Journal of Microbiology

Dae Won Park

2 Articles

Molecular Analysis of a Prolonged Spread of Klebsiella pneumoniae Co-producing DHA-1 and SHV-12 β-Lactamases: Young Kyung Yoon , Hye Won Cheong , Hyunjoo Pai , Kyoung Ho Roh , Jeong Yeon Kim , Dae Won Park , Jang Wook Sohn , Seung Eun Lee , Byung Chul Chun , Hee Sun Sim , Min Ja Kim; J. Microbiol. 2011;49(3):363-368. Published online June 30, 2011; DOI: https://doi.org/10.1007/s12275-011-0491-9

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The study investigated molecular mechanisms for prolonged nosocomial spread of multidrug-resistant Klebsiella pneumoniae co-producing plasmid-mediated AmpC β-lactamase DHA-1 and extended-spectrum β-lactamase SHV-12. Forty-eight clinical isolates of K. pneumonia, resistant to the extended-spectrum cephalosporins, were collected in a 750-bed university hospital over a year. The isolates were characterized for PCR-based β-lactamase genotypes, isoelectric focusing and pulsed-field gel electrophoresis (PFGE) profiles. Resistance transfer was performed by plasmid conjugation and confirmed by a duplex-PCR and Southern hybridization. On β-lactamase typing, the strains producing only the DHA-1 enzyme (n=17) or co-producing DHA-1 and SHV-12 enzymes (n=15) were predominant. Judging from a one year-distribution of PFGE profiles, the co-producer was spread primarily with single clonal expansion of the PFGE-type A with subtypes (n=14), whereas the strains producing only DHA-1 enzyme were spread simultaneously with the PFGE-type A (n=11) and other PFGE types (n=6). Transconjugants of the co-producers were confirmed to harbor either both blaDHA-1 and blaSHV-12 or only the blaDHA-1. In conclusion, this study indicated that the persistent nosocomial spread of multidrug-resistant K. pneumoniae strains was primarily associated with expansion of a clone harboring both the blaDHA-1 and blaSHV-12 or the blaDHA-1 only, and to a lesser extent with the horizontal transfer of the resistant plasmids. Our observations have clinical implication for the control and prevention of nosocomial dissemination of multidrug-resistant K. pneumoniae strains.

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High Prevalence of CTX-M-15-Type Extended-Spectrum β-Lactamase Among AmpC β-Lactamase-Producing Klebsiella pneumoniae Isolates Causing Bacteremia in Korea
Min Kyeong Cha, Cheol-In Kang, So Hyun Kim, Doo Ryeon Chung, Kyong Ran Peck, Nam Yong Lee, Jae-Hoon Song
Microbial Drug Resistance.2018; 24(7): 1002. CrossRef
Role of piperacillin/tazobactam as a carbapenem-sparing antibiotic for treatment of acute pyelonephritis due to extended-spectrum β-lactamase-producing Escherichia coli
Young Kyung Yoon, Jong Hun Kim, Jang Wook Sohn, Kyung Sook Yang, Min Ja Kim
International Journal of Antimicrobial Agents.2017; 49(4): 410. CrossRef
Emergence of serotype K1 Klebsiella pneumoniae ST23 strains co-producing the plasmid-mediated AmpC beta-lactamase DHA-1 and an extended-spectrum beta-lactamase in Korea
Hae Suk Cheong, Doo Ryeon Chung, Chaeyoeng Lee, So Hyun Kim, Cheol-In Kang, Kyong Ran Peck, Jae-Hoon Song
Antimicrobial Resistance & Infection Control.2016;[Epub] CrossRef
Effects of Group 1 versus Group 2 Carbapenems on the Susceptibility of Acinetobacter baumannii to Carbapenems: A Before and After Intervention Study of Carbapenem-Use Stewardship
Young Kyung Yoon, Kyung Sook Yang, Seung Eun Lee, Hyun Jeong Kim, Jang Wook Sohn, Min Ja Kim, Mark Alexander Webber
PLoS ONE.2014; 9(6): e99101. CrossRef

Electrochemical Reduction of Xylose to Xylitol by Whole Cells or Crude Enzyme of Candida peltata: Sun Mi Park , Byung In Sang , Dae Won Park , Doo Hyun Park; J. Microbiol. 2005;43(5):451-455.; DOI: https://doi.org/2276 [pii]

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Abstract PDF: In this study, whole cells and a crude enzyme of Candida peltata were applied to an electrochemical bioreactor, in order to induce an increment of the reduction of xylose to xylitol. Neutral red was utilized as an electron mediator in the whole cell reactor, and a graphite-Mn(IV) electrode was used as a catalyst in the enzyme reactor in order to induce the electrochemical reduction of NAD+ to NADH. The efficiency with which xylose was converted to xylitol in the electrochemical bioreactor was five times higher than that in the conventional bioreactor, when whole cells were employed as a biocatalyst. Meanwhile, the xylose to xylitol reduction efficiency in the enzyme reactor using the graphite-Mn (IV) electrode and NAD+ was twice as high as that observed in the conventional bioreactor which utilized NADH as a reducing power. In order to use the graphite-Mn(IV) electrode as a catalyst for the reduction of NAD+ to NADH, a bioelectrocatalyst was engineered, namely, oxidoreductase (e.g. xylose reductase). NAD+ can function in this biotransformation procedure without any electron mediator or a second oxidoreductase for NAD+/NADH recycling

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