J Vet Sci.  2016 Mar;17(1):119-122. 10.4142/jvs.2016.17.1.119.

Molecular cloning, purification and immunogenicity of recombinant Brucella abortus 544 malate dehydrogenase protein

Affiliations
  • 1Institute of Animal Medicine, College of Veterinary Medicine, Gyeongsang National University, Jinju 52828, Korea. kimsuk@gnu.ac.kr
  • 2Department of Veterinary Paraclinical Sciences, College of Veterinary Medicine, University of the Philippines Los Baños, College, Laguna 4031, Philippines.
  • 3Institute of Agriculture and Life Science, College of Veterinary Medicine, Gyeongsang National University, Jinju 52828, Korea.

Abstract

The Brucella mdh gene was successfully cloned and expressed in E. coli. The purified recombinant malate dehydrogenase protein (rMDH) was reactive to Brucella-positive bovine serum in the early stage, but not reactive in the middle or late stage, and was reactive to Brucella-positive mouse serum in the late stage, but not in the early or middle stage of infection. In addition, rMDH did not react with Brucella-negative bovine or mouse sera. These results suggest that rMDH has the potential for use as a specific antigen in serological diagnosis for early detection of bovine brucellosis.

Keyword

Brucella; expression; immunogenicity; malate dehydrogenase; recombinant protein
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