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.
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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