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

10 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

  • General Veterinary

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