Molecular cloning, purification and immunogenicity of recombinant Brucella abortus 544 malate dehydrogenase protein.
| Autor: | Reyes AW; Institute of Animal Medicine, College of Veterinary Medicine, Gyeongsang National University, Jinju 52828, Korea.; Department of Veterinary Paraclinical Sciences, College of Veterinary Medicine, University of the Philippines Los Baños, College, Laguna 4031, Philippines., Simborio HL; Institute of Animal Medicine, College of Veterinary Medicine, Gyeongsang National University, Jinju 52828, Korea., Hop HT; Institute of Animal Medicine, College of Veterinary Medicine, Gyeongsang National University, Jinju 52828, Korea., Arayan LT; Institute of Animal Medicine, College of Veterinary Medicine, Gyeongsang National University, Jinju 52828, Korea., Kim S; Institute of Animal Medicine, College of Veterinary Medicine, Gyeongsang National University, Jinju 52828, Korea.; Institute of Agriculture and Life Science, College of Veterinary Medicine, Gyeongsang National University, Jinju 52828, Korea. |
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| Jazyk: | angličtina |
| Zdroj: | Journal of veterinary science [J Vet Sci] 2016 Mar; Vol. 17 (1), pp. 119-22. Date of Electronic Publication: 2016 Mar 22. |
| DOI: | 10.4142/jvs.2016.17.1.119 |
| Abstrakt: | 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. |
| Databáze: | MEDLINE |
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