Expression and Characterization of an Iron-Containing Superoxide Dismutase from Burkholderia pseudomallei

Min-Hee Cho; Yong-Woo Shin; Jeong-Hoon Chun; Kee-Jong Hong; Byoung-Kuk Na; Gi-eun Rhie; Baik-Lin Seong; Cheon-Kwon Yoo

doi:10.1007/s12275-012-2267-2

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Expression and Characterization of an Iron-Containing Superoxide Dismutase from Burkholderia pseudomallei: Min-Hee Cho ¹, Yong-Woo Shin ^1,2, Jeong-Hoon Chun ¹, Kee-Jong Hong ¹, Byoung-Kuk Na ³, Gi-eun Rhie ¹, Baik-Lin Seong ², Cheon-Kwon Yoo ¹; Journal of Microbiology 2012;50(6):1029-1033.
DOI: https://doi.org/10.1007/s12275-012-2267-2
Published online: December 30, 2012

¹Division of High-Risk Pathogen Research, Center for Infectious Diseases, National Institute of Health, Chungbuk 363-951, Republic of Korea, ²Department of Biotechnology, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Republic of Korea, ³Department of Parasitology and the Institute of Health Sciences, College of Medicine, Gyeongsang National University, School of Medicine, Jinju 660-751, Republic of Korea¹Division of High-Risk Pathogen Research, Center for Infectious Diseases, National Institute of Health, Chungbuk 363-951, Republic of Korea, ²Department of Biotechnology, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Republic of Korea, ³Department of Parasitology and the Institute of Health Sciences, College of Medicine, Gyeongsang National University, School of Medicine, Jinju 660-751, Republic of Korea

Corresponding author: Cheon-Kwon Yoo , Tel: +82-43-719-8040,

Received: 18 May 2012 • Accepted: 21 August 2012

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Abstract

A superoxide dismutase (SOD) gene from Burkholderia pseudomallei, the causative agent of melioidosis, was cloned and expressed in Escherichia coli, and its product was functionally and physically characterized. The gene has an open-reading frame of 579 bp. The deduced amino acid sequence has 192 residues with a calculated molecular mass of ~22 kDa. Sequence comparison with other bacterial SODs showed that the protein contains typical metal-binding motifs and other Fe-SOD-conserved residues. The sequence has substantial similarity with other bacterial Fe-SOD sequences. The enzymatic activity of the expressed protein was inhibited by hydrogen peroxide but not by sodium azide or potassium cyanide, attributes that indeed are characteristic of typical bacterial Fe-SODs. Western blotting with antiserum against the recombinant Fe-SOD revealed that it is expressed in B. pseudomallei. Transformed E. coli that expressed the Fe-SOD had significantly increased SOD activity and was highly tolerant to paraquat-mediated replication inhibition, compared to transformed cells carrying an empty vector. Our results provide a basis for further biochemical characterization of the enzyme and elucidation of its role in the pathogenesis of B. pseudomallei.

Keywords: Burkholderia pseudomallei;Fe-superoxide dismutase;melioidosis

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Expression and Characterization of an Iron-Containing Superoxide Dismutase from Burkholderia pseudomallei

J. Microbiol. 2012;50(6):1029-1033. Published online December 30, 2012

DOI: https://doi.org/10.1007/s12275-012-2267-2

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