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    Cloning and purification of recombinant proteins of Mycoplasma hyopneumoniae expressed in Escherichia coli

    Access Status
    Fulltext not available
    Authors
    Simionatto, S.
    Marchioro, S.
    Galli, V.
    Hartwig, D.
    Carlessi, Rodrigo
    Munari, F.
    Laurino, J.
    Conceição, F.
    Dellagostin, O.
    Date
    2010
    Type
    Journal Article
    
    Metadata
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    Citation
    Simionatto, S. and Marchioro, S. and Galli, V. and Hartwig, D. and Carlessi, R. and Munari, F. and Laurino, J. et al. 2010. Cloning and purification of recombinant proteins of Mycoplasma hyopneumoniae expressed in Escherichia coli. Protein Expression and Purification. 69 (2): pp. 132-136.
    Source Title
    Protein Expression and Purification
    DOI
    10.1016/j.pep.2009.09.001
    ISSN
    1046-5928
    School
    School of Biomedical Sciences
    URI
    http://hdl.handle.net/20.500.11937/42269
    Collection
    • Curtin Research Publications
    Abstract

    Mycoplasma hyopneumoniae, the etiological agent of swine enzootic pneumonia, is an important pathogen in the swine industry worldwide. Vaccination is the most cost-effective strategy for controlling and prevention of this disease. However, investigations on pathogenicity mechanisms as well as current serological detection methods and the development of new recombinant subunit vaccines are hampered by the lack of known and well characterized species-specific M. hyopneumoniae antigens. In this work, 54 predicted genes encoding proteins with potential to be used as subunit vaccine or antigens in diagnostic tests were selected, amplified by PCR and cloned into Escherichia coli expression vectors. Recombinant protein expression, solubility and yields were analyzed. The majority of the recombinant proteins were expressed in inclusion bodies. After solubilization with urea or N-lauroyl sarcosine, recombinant proteins were purified by Ni2+ affinity chromatography. This approach allowed purification of thirty recombinant M. hyopneumoniae proteins which will be evaluated as vaccine candidates and/or as antigens to be used in diagnostic tests. © 2009 Elsevier Inc. All rights reserved.

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