Molecular cloning, purification and immunogenicity of recombinant Brucella abortus 544 malate dehydrogenase protein.
10.4142/jvs.2016.17.1.119
- Author:
Alisha Wehdnesday Bernardo REYES
1
;
Hannah Leah Tadeja SIMBORIO
;
Huynh Tan HOP
;
Lauren Togonon ARAYAN
;
Suk KIM
Author Information
1. Institute of Animal Medicine, College of Veterinary Medicine, Gyeongsang National University, Jinju 52828, Korea. kimsuk@gnu.ac.kr
- Publication Type:Brief Communication ; Research Support, Non-U.S. Gov't
- Keywords:
Brucella;
expression;
immunogenicity;
malate dehydrogenase;
recombinant protein
- MeSH:
Animals;
Antigens, Bacterial/*immunology;
Brucella abortus/*enzymology/immunology;
Brucellosis/diagnosis/*veterinary;
Cattle;
Cattle Diseases/*diagnosis;
Cloning, Molecular;
Enzyme-Linked Immunosorbent Assay;
Escherichia coli/genetics;
Malate Dehydrogenase/*genetics/*immunology/isolation & purification;
Mice;
Recombinant Proteins/genetics/*immunology
- From:Journal of Veterinary Science
2016;17(1):119-122
- CountryRepublic of Korea
- Language:English
-
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.
