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

Issue Date

3-2016

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.

Source or Periodical Title

Journal of Veterinary Science

ISSN

1229-845X

Volume

17

Issue

1

Page

119-122

Document Type

Article

Physical Description

illustrations

Language

English

Subject

Brucella, Expression, Immunogenicity, Malate dehydrogenase, Recombinant protein

Identifier

doi:10.4142/jvs.2016.17.1.119.

Digital Copy

yes

Link to Full Text

Share

COinS