Evaluation of a Recombinant 27-kDa Outer Membrane Protein of <i>Coxiella burnetii</i> as an Immunodiagnostic Reagent

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  • Zhang Guo Quan
    Department of Veterinary Microbiology, Faculty of Agriculture, Gifu University
  • Hotta Akitoyo
    Department of Veterinary Microbiology, Faculty of Agriculture, Gifu University
  • Ho To
    Department of Veterinary Microbiology, Faculty of Agriculture, Gifu University
  • Yamaguchi Tsuyoshi
    Department of Veterinary Microbiology, Faculty of Agriculture, Gifu University
  • Fukushi Hideto
    Department of Veterinary Microbiology, Faculty of Agriculture, Gifu University
  • Hirai Katsuya
    Department of Veterinary Microbiology, Faculty of Agriculture, Gifu University

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  • Evaluation of a Recombinant 27-kDa Outer Membrane Protein of Coxiella burnetii as an Immunodiagnostic Reagent
  • Evaluation of a Recombinant 27 - kDa Ou
  • Evaluation of a Recombinant 27‐kDa Outer Membrane Protein of <i>Coxiella burnetii</i> as an Immunodiagnostic Reagent

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Abstract

The 27-kDa outer membrane protein from eight strains of Coxiella burnetii was expressed in the pET-21c protein expression system. Two fusion proteins with molecular masses of 30 and 32kDa were evident in all eight of the recombinants by SDS-PAGE and immunoblotting. A protein having an approximate size of 30kDa was purified from the Escherichia coli lysates by one-step affinity purification. The utility of the purified recombinant protein in ELISA was also evaluated by testing its reactivity with human sera and comparing this reactivity with that of Nine Mile phase II antigen. All of the 40 IF-positive serum samples were ELISA-positive for both the Nine Mile phase II and recombinant antigens, and negative serum controls were negative for both antigens. These results suggest that ELISA with the 27-kDa recombinant antigen is a sensitive and specific method for detecting anti-C. burnetii antibodies in human sera.

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