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Molecular cloning, purification and immunogenicity of recombinant Brucella abortus 544 malate dehydrogenase protein
Journal of Veterinary Science ; : 119-122, 2016.
Article in English | WPRIM | ID: wpr-56503
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.
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Full text: Available Index: WPRIM (Western Pacific) Main subject: Recombinant Proteins / Brucella abortus / Brucellosis / Enzyme-Linked Immunosorbent Assay / Cattle Diseases / Cloning, Molecular / Escherichia coli / Malate Dehydrogenase / Antigens, Bacterial Type of study: Screening study Limits: Animals Language: English Journal: Journal of Veterinary Science Year: 2016 Type: Article

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Full text: Available Index: WPRIM (Western Pacific) Main subject: Recombinant Proteins / Brucella abortus / Brucellosis / Enzyme-Linked Immunosorbent Assay / Cattle Diseases / Cloning, Molecular / Escherichia coli / Malate Dehydrogenase / Antigens, Bacterial Type of study: Screening study Limits: Animals Language: English Journal: Journal of Veterinary Science Year: 2016 Type: Article