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

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 t...

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Autores principales: Reyes, Alisha Wehdnesday Bernardo, Simborio, Hannah Leah Tadeja, Hop, Huynh Tan, Arayan, Lauren Togonon, Kim, Suk
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Korean Society of Veterinary Science 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4808637/
https://www.ncbi.nlm.nih.gov/pubmed/27051349
http://dx.doi.org/10.4142/jvs.2016.17.1.119
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author Reyes, Alisha Wehdnesday Bernardo
Simborio, Hannah Leah Tadeja
Hop, Huynh Tan
Arayan, Lauren Togonon
Kim, Suk
author_facet Reyes, Alisha Wehdnesday Bernardo
Simborio, Hannah Leah Tadeja
Hop, Huynh Tan
Arayan, Lauren Togonon
Kim, Suk
author_sort Reyes, Alisha Wehdnesday Bernardo
collection PubMed
description 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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spelling pubmed-48086372016-04-05 Molecular cloning, purification and immunogenicity of recombinant Brucella abortus 544 malate dehydrogenase protein Reyes, Alisha Wehdnesday Bernardo Simborio, Hannah Leah Tadeja Hop, Huynh Tan Arayan, Lauren Togonon Kim, Suk J Vet Sci Short Communication 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. The Korean Society of Veterinary Science 2016-03 2016-03-22 /pmc/articles/PMC4808637/ /pubmed/27051349 http://dx.doi.org/10.4142/jvs.2016.17.1.119 Text en © 2016 The Korean Society of Veterinary Science. http://creativecommons.org/licenses/by-nc/4.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Short Communication
Reyes, Alisha Wehdnesday Bernardo
Simborio, Hannah Leah Tadeja
Hop, Huynh Tan
Arayan, Lauren Togonon
Kim, Suk
Molecular cloning, purification and immunogenicity of recombinant Brucella abortus 544 malate dehydrogenase protein
title Molecular cloning, purification and immunogenicity of recombinant Brucella abortus 544 malate dehydrogenase protein
title_full Molecular cloning, purification and immunogenicity of recombinant Brucella abortus 544 malate dehydrogenase protein
title_fullStr Molecular cloning, purification and immunogenicity of recombinant Brucella abortus 544 malate dehydrogenase protein
title_full_unstemmed Molecular cloning, purification and immunogenicity of recombinant Brucella abortus 544 malate dehydrogenase protein
title_short Molecular cloning, purification and immunogenicity of recombinant Brucella abortus 544 malate dehydrogenase protein
title_sort molecular cloning, purification and immunogenicity of recombinant brucella abortus 544 malate dehydrogenase protein
topic Short Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4808637/
https://www.ncbi.nlm.nih.gov/pubmed/27051349
http://dx.doi.org/10.4142/jvs.2016.17.1.119
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