RT info:eu-repo/semantics/article
T1 Characterization of a recombinant transferrin-binding proteinA (TbpA) fragment fromHaemophilus parasuis serovar 5
A1 Martínez, Sonia
A1 Frandoloso, Rafael
A1 Rodríguez Ferri, Elías Fernando
A1 González Zorn, Bruno
A1 Gutiérrez Martín, César Bernardo
A2 Sanidad Animal
K1 Sanidad animal
K1 Veterinaria
K1 Glässer’s disease
K1 Haemophilus parasuis
AB Haemophilus parasuis, the etiological agent of Gl¨asser’s disease in pigs, possessesiron acquisition pathways mediated by a surface receptor that specifically bindporcine 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. Inthis study, a 600-bp tbpA fragment of the gene encoding TbpA from H. parasuisserovar 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 transformedwith this construction, followed by the induction of protein expression witharabinose. A band (38.5 kDa) corresponding to a 200-amino acid recombinantTbpA (rTbpA) fragment was seen on the sodium dodecyl sulfate polyacrylamidegel electrophoresis and confirmed by immunoblotting. Polyclonal antibodiesraised against this fragment were specific for H. parasuis and Actinobacilluspleuropneumoniae, reacted at the cell surface with H. parasuis, and a significantbactericidal activity was also detected. Therefore, this rTbpA fragment induces animmunological response and might be useful as an antigen for vaccination againstGl¨asser’s disease
PB Oxford Academic
YR 2017
FD 2017-08-01
LK http://hdl.handle.net/10612/6463
UL http://hdl.handle.net/10612/6463
NO FEMS Microbiology Letters, 2010
NO 9 p.
DS BULERIA. Repositorio Institucional de la Universidad de León
RD 27-jun-2024