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Journal of Bacteriology, February 2003, p. 1010-1017, Vol. 185, No. 3
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.3.1010-1017.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

The Iron-Binding Protein Dps Confers Hydrogen Peroxide Stress Resistance to Campylobacter jejuni

Takahiko Ishikawa,1,2 Yoshimitsu Mizunoe,1* Shun-ichiro Kawabata,3 Akemi Takade,1 Mine Harada,2 Sun Nyunt Wai,1,4 and Shin-ichi Yoshida1

Department of Bacteriology,1 Department of Medicine and Biosystemic Science, Internal Medicine,2 Faculty of Medical Sciences, and Department of Biology, Faculty of Sciences, Kyushu University, Fukuoka 812-8582, Japan,3 Department of Molecular Biology, Umeå University, S901 87 Umeå, Sweden4

Received 26 September 2002/ Accepted 15 November 2002

We identified and characterized the iron-binding protein Dps from Campylobacter jejuni. Electron microscopic analysis of this protein revealed a spherical structure of 8.5 nm in diameter, with an electron-dense core similar to those of other proteins of the Dps (DNA-binding protein from starved cells) family. Cloning and sequencing of the Dps-encoding gene (dps) revealed that a 450-bp open reading frame (ORF) encoded a protein of 150 amino acids with a calculated molecular mass of 17,332 Da. Amino acid sequence comparison indicated a high similarity between C. jejuni Dps and other Dps family proteins. In C. jejuni Dps, there are iron-binding motifs, as reported in other Dps family proteins. C. jejuni Dps bound up to 40 atoms of iron per monomer, whereas it did not appear to bind DNA. An isogenic dps-deficient mutant was more vulnerable to hydrogen peroxide than its parental strain, as judged by growth inhibition tests. The iron chelator Desferal restored the resistance of the Dps-deficient mutant to hydrogen peroxide, suggesting that this iron-binding protein prevented generation of hydroxyl radicals via the Fenton reaction. Dps was constitutively expressed during both exponential and stationary phase, and no induction was observed when the cells were exposed to H2O2 or grown under iron-supplemented or iron-restricted conditions. On the basis of these data, we propose that this iron-binding protein in C. jejuni plays an important role in protection against hydrogen peroxide stress by sequestering intracellular free iron and is expressed constitutively to cope with the harmful effect of hydrogen peroxide stress on this microaerophilic organism without delay.

* Corresponding author. Mailing address: Department of Bacteriology, Faculty of Medical Sciences, Kyushu University, Fukuoka 812-8582, Japan. Phone: 81-92-642-6128. Fax: 81-92-642-6133. E-mail: ymizunoe{at}bact.med.kyushu-u.ac.jp.

Journal of Bacteriology, February 2003, p. 1010-1017, Vol. 185, No. 3
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.3.1010-1017.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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