Molecular cloning, purification and immunogenicity of recombinant Brucella abortus 544 malate dehydrogenase protein

Alisha Wehdnesday Bernardo Reyes, Hannah Leah Tadeja Simborio, Huynh Tan Hop, Lauren Togonon Arayan, Suk Kim

Research output: Contribution to journalShort surveypeer-review

8 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)119-122
Number of pages4
JournalJournal of Veterinary Science
Volume17
Issue number1
DOIs
Publication statusPublished - 2016

All Science Journal Classification (ASJC) codes

  • veterinary(all)

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