Rhipicephalus (Boophilus) microplus: expression and characterization of Bm86-CG in Pichia pastoris
Autor(a) principal: | |
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Data de Publicação: | 2011 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Revista Brasileira de Parasitologia Veterinária (Online) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1984-29612011000200003 |
Resumo: | The cattle tick Rhipicephalus (Boophilus) microplus is responsible for great economic losses. It is mainly controlled chemically, with limitations regarding development of resistance to the chemicals. Vaccines may help control this parasite, thereby reducing tick pesticide use. In this light, we performed subcloning of the gene of the protein Bm86-GC, the homologue protein that currently forms the basis of vaccines (GavacTM and TickGardPLUS) that have been developed against cattle ticks. The subcloning was done in the pPIC9 expression vector, for transformation in the yeast Pichia pastoris. This protein was characterized by expression of the recombinant Mut+ strain, which expressed greater quantities of protein. The expressed protein (rBm86-CG) was recognized in the Western-blot assay using anti-Gavac, anti-TickGard, anti-larval extract and anti-rBm86-CG polyclonal sera. The serum produced in cattle vaccinated with the antigen CG rBm86 presented high antibody titers and recognized the native protein. The rBm86-GC has potential relevance as an immunogen for vaccine formulation against cattle ticks. |
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Rhipicephalus (Boophilus) microplus: expression and characterization of Bm86-CG in Pichia pastorisIxodesticksbovinesrBm86-CGimmunizationThe cattle tick Rhipicephalus (Boophilus) microplus is responsible for great economic losses. It is mainly controlled chemically, with limitations regarding development of resistance to the chemicals. Vaccines may help control this parasite, thereby reducing tick pesticide use. In this light, we performed subcloning of the gene of the protein Bm86-GC, the homologue protein that currently forms the basis of vaccines (GavacTM and TickGardPLUS) that have been developed against cattle ticks. The subcloning was done in the pPIC9 expression vector, for transformation in the yeast Pichia pastoris. This protein was characterized by expression of the recombinant Mut+ strain, which expressed greater quantities of protein. The expressed protein (rBm86-CG) was recognized in the Western-blot assay using anti-Gavac, anti-TickGard, anti-larval extract and anti-rBm86-CG polyclonal sera. The serum produced in cattle vaccinated with the antigen CG rBm86 presented high antibody titers and recognized the native protein. The rBm86-GC has potential relevance as an immunogen for vaccine formulation against cattle ticks.Colégio Brasileiro de Parasitologia Veterinária2011-06-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1984-29612011000200003Revista Brasileira de Parasitologia Veterinária v.20 n.2 2011reponame:Revista Brasileira de Parasitologia Veterinária (Online)instname:Colégio Brasileiro de Parasitologia Veterinária (CBPV)instacron:CBPV10.1590/S1984-29612011000200003info:eu-repo/semantics/openAccessCunha,Rodrigo CasqueroAndreotti,RenatoLeite,Fábio Pereira Leivaseng2011-07-07T00:00:00Zoai:scielo:S1984-29612011000200003Revistahttp://www.scielo.br/scielo.php?script=sci_serial&lng=pt&pid=1984-2961https://old.scielo.br/oai/scielo-oai.php||zacariascbpv@fcav.unesp.br1984-29610103-846Xopendoar:2011-07-07T00:00Revista Brasileira de Parasitologia Veterinária (Online) - Colégio Brasileiro de Parasitologia Veterinária (CBPV)false |
dc.title.none.fl_str_mv |
Rhipicephalus (Boophilus) microplus: expression and characterization of Bm86-CG in Pichia pastoris |
title |
Rhipicephalus (Boophilus) microplus: expression and characterization of Bm86-CG in Pichia pastoris |
spellingShingle |
Rhipicephalus (Boophilus) microplus: expression and characterization of Bm86-CG in Pichia pastoris Cunha,Rodrigo Casquero Ixodes ticks bovines rBm86-CG immunization |
title_short |
Rhipicephalus (Boophilus) microplus: expression and characterization of Bm86-CG in Pichia pastoris |
title_full |
Rhipicephalus (Boophilus) microplus: expression and characterization of Bm86-CG in Pichia pastoris |
title_fullStr |
Rhipicephalus (Boophilus) microplus: expression and characterization of Bm86-CG in Pichia pastoris |
title_full_unstemmed |
Rhipicephalus (Boophilus) microplus: expression and characterization of Bm86-CG in Pichia pastoris |
title_sort |
Rhipicephalus (Boophilus) microplus: expression and characterization of Bm86-CG in Pichia pastoris |
author |
Cunha,Rodrigo Casquero |
author_facet |
Cunha,Rodrigo Casquero Andreotti,Renato Leite,Fábio Pereira Leivas |
author_role |
author |
author2 |
Andreotti,Renato Leite,Fábio Pereira Leivas |
author2_role |
author author |
dc.contributor.author.fl_str_mv |
Cunha,Rodrigo Casquero Andreotti,Renato Leite,Fábio Pereira Leivas |
dc.subject.por.fl_str_mv |
Ixodes ticks bovines rBm86-CG immunization |
topic |
Ixodes ticks bovines rBm86-CG immunization |
description |
The cattle tick Rhipicephalus (Boophilus) microplus is responsible for great economic losses. It is mainly controlled chemically, with limitations regarding development of resistance to the chemicals. Vaccines may help control this parasite, thereby reducing tick pesticide use. In this light, we performed subcloning of the gene of the protein Bm86-GC, the homologue protein that currently forms the basis of vaccines (GavacTM and TickGardPLUS) that have been developed against cattle ticks. The subcloning was done in the pPIC9 expression vector, for transformation in the yeast Pichia pastoris. This protein was characterized by expression of the recombinant Mut+ strain, which expressed greater quantities of protein. The expressed protein (rBm86-CG) was recognized in the Western-blot assay using anti-Gavac, anti-TickGard, anti-larval extract and anti-rBm86-CG polyclonal sera. The serum produced in cattle vaccinated with the antigen CG rBm86 presented high antibody titers and recognized the native protein. The rBm86-GC has potential relevance as an immunogen for vaccine formulation against cattle ticks. |
publishDate |
2011 |
dc.date.none.fl_str_mv |
2011-06-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1984-29612011000200003 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1984-29612011000200003 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S1984-29612011000200003 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Colégio Brasileiro de Parasitologia Veterinária |
publisher.none.fl_str_mv |
Colégio Brasileiro de Parasitologia Veterinária |
dc.source.none.fl_str_mv |
Revista Brasileira de Parasitologia Veterinária v.20 n.2 2011 reponame:Revista Brasileira de Parasitologia Veterinária (Online) instname:Colégio Brasileiro de Parasitologia Veterinária (CBPV) instacron:CBPV |
instname_str |
Colégio Brasileiro de Parasitologia Veterinária (CBPV) |
instacron_str |
CBPV |
institution |
CBPV |
reponame_str |
Revista Brasileira de Parasitologia Veterinária (Online) |
collection |
Revista Brasileira de Parasitologia Veterinária (Online) |
repository.name.fl_str_mv |
Revista Brasileira de Parasitologia Veterinária (Online) - Colégio Brasileiro de Parasitologia Veterinária (CBPV) |
repository.mail.fl_str_mv |
||zacariascbpv@fcav.unesp.br |
_version_ |
1754208913984585728 |