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KMID : 0893420160170010119
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Journal of Veterinary Science
2016 Volume.17 No. 1 p.119 ~ p.122
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Molecular cloning, purification and immunogenicity of recombinant Brucella abortus 544 malate dehydrogenase protein
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Reyes Alisha Wehdnesday Bernardo
Simborio Hannah Leah Tadeja
Hop Huynh Tan
Arayan Lauren Togonon
Kim Suk
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Abstract
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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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KEYWORD
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Brucella, expression, immunogenicity, malate dehydrogenase, recombinant protein
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