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    Título
    Characterization of a recombinant transferrin-binding proteinA (TbpA) fragment fromHaemophilus parasuis serovar 5
    Autor
    Martínez, Sonia
    Frandoloso, Rafael
    Rodríguez Ferri, Elías FernandoAutoridad Buleria ORCID
    González Zorn, Bruno
    Gutiérrez Martín, César BernardoAutoridad Buleria ORCID
    Facultad/Centro
    Facultad de Veterinaria
    Área de conocimiento
    Sanidad Animal
    Datos de la obra
    FEMS Microbiology Letters, 2010
    Editor
    Oxford Academic
    Fecha
    2010
    Descripción física
    9 p.
    Abstract
    Haemophilus parasuis, the etiological agent of Gl¨asser’s disease in pigs, possesses iron acquisition pathways mediated by a surface receptor that specifically bind porcine transferrin. This receptor is composed of transferrin-binding protein A (TbpA) and TbpB. As it has been reported for other gram-negative organisms, H. parasuis TbpA could be useful as a candidate target for H. parasuis vaccination. In this study, a 600-bp tbpA fragment of the gene encoding TbpA from H. parasuis serovar 5, the Nagasaki strain, was amplified by PCR and cloned into a pBAD/ Thio-TOPO expression vector, generating the pBAD-Thio-TbpA-V5-His (TbpAHis) construction. Escherichia coli LMG194-competent cells were transformed with this construction, followed by the induction of protein expression with arabinose. A band (38.5 kDa) corresponding to a 200-amino acid recombinant TbpA (rTbpA) fragment was seen on the sodium dodecyl sulfate polyacrylamide gel electrophoresis and confirmed by immunoblotting. Polyclonal antibodies raised against this fragment were specific for H. parasuis and Actinobacillus pleuropneumoniae, reacted at the cell surface with H. parasuis, and a significant bactericidal activity was also detected. Therefore, this rTbpA fragment induces an immunological response and might be useful as an antigen for vaccination against Gl¨asser’s disease
    Materia
    Sanidad animal
    Veterinaria
    Palabras clave
    Glässer’s disease
    Haemophilus parasuis
    Idioma
    eng
    Tipo documental
    info:eu-repo/semantics/article
    Peer review
    SI
    URI
    http://hdl.handle.net/10612/6463
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    • Artículos de revista (post-print) [2050]
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