cDNA cloning, expression and characterization of a Boophilus microplus paramyosin.
Autor(a) principal: | |
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Data de Publicação: | 2002 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UFRGS |
Texto Completo: | http://hdl.handle.net/10183/27454 |
Resumo: | The tick Boophilus microplus is a 1-host tick that causes important losses to bovine herds, and protective antigens are being investigated in order to develop vaccines that avoid the use of acaricides. Paramyosins are multi-functional invertebrate muscle proteins, whose roles may include host immunomodulation, and seem to be a prominent candidate in a schistosomiasis vaccine. We report here the cloning, expression and characterization of a B. microplus paramyosin (BmPRM). Sequence analysis of the full length coding sequence cDNA shows high identity to other arthropod paramyosin sequences, and the predicted molecular weight, pI and secondary structure are consistent with a typical paramyosin. Western-blot expression analysis indicates the presence of BmPRM in all tissues and developmental stages tested, but not in saliva. The recombinant protein (rBmPRM) was shown to bind both IgG and collagen. Possible implications of these activities with host evasion mechanisms are discussed. |
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Ferreira, Carlos Alexandre SanchezBarbosa, M. C.Silveira, Thiago Cesar LimaValenzuela, J.G.Vaz Junior, Itabajara da SilvaMasuda, Aoi2011-01-21T05:59:00Z20020031-1820http://hdl.handle.net/10183/27454000337062The tick Boophilus microplus is a 1-host tick that causes important losses to bovine herds, and protective antigens are being investigated in order to develop vaccines that avoid the use of acaricides. Paramyosins are multi-functional invertebrate muscle proteins, whose roles may include host immunomodulation, and seem to be a prominent candidate in a schistosomiasis vaccine. We report here the cloning, expression and characterization of a B. microplus paramyosin (BmPRM). Sequence analysis of the full length coding sequence cDNA shows high identity to other arthropod paramyosin sequences, and the predicted molecular weight, pI and secondary structure are consistent with a typical paramyosin. Western-blot expression analysis indicates the presence of BmPRM in all tissues and developmental stages tested, but not in saliva. The recombinant protein (rBmPRM) was shown to bind both IgG and collagen. Possible implications of these activities with host evasion mechanisms are discussed.application/pdfengParasitology. Inglaterra. Vol. 125, no. 3 (2002), p. 265-274Parasitologia veterináriaParamyosinBoophilus microplusIgG binding proteinCollagen binding proteinTickcDNA cloning, expression and characterization of a Boophilus microplus paramyosin.Estrangeiroinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UFRGSinstname:Universidade Federal do Rio Grande do Sul (UFRGS)instacron:UFRGSORIGINAL000337062.pdf000337062.pdfTexto completo (inglês)application/pdf825785http://www.lume.ufrgs.br/bitstream/10183/27454/1/000337062.pdf0b6611deb83d6f3d6d5cb649fa0a0be1MD51TEXT000337062.pdf.txt000337062.pdf.txtExtracted Texttext/plain41934http://www.lume.ufrgs.br/bitstream/10183/27454/2/000337062.pdf.txtdb1ffaa68aaa10c9bedb919bce0b2858MD52THUMBNAIL000337062.pdf.jpg000337062.pdf.jpgGenerated Thumbnailimage/jpeg1710http://www.lume.ufrgs.br/bitstream/10183/27454/3/000337062.pdf.jpg137690a9f223ffc8d4d2beab12eff11bMD5310183/274542021-06-26 04:46:21.380567oai:www.lume.ufrgs.br:10183/27454Repositório de PublicaçõesPUBhttps://lume.ufrgs.br/oai/requestopendoar:2021-06-26T07:46:21Repositório Institucional da UFRGS - Universidade Federal do Rio Grande do Sul (UFRGS)false |
dc.title.pt_BR.fl_str_mv |
cDNA cloning, expression and characterization of a Boophilus microplus paramyosin. |
title |
cDNA cloning, expression and characterization of a Boophilus microplus paramyosin. |
spellingShingle |
cDNA cloning, expression and characterization of a Boophilus microplus paramyosin. Ferreira, Carlos Alexandre Sanchez Parasitologia veterinária Paramyosin Boophilus microplus IgG binding protein Collagen binding protein Tick |
title_short |
cDNA cloning, expression and characterization of a Boophilus microplus paramyosin. |
title_full |
cDNA cloning, expression and characterization of a Boophilus microplus paramyosin. |
title_fullStr |
cDNA cloning, expression and characterization of a Boophilus microplus paramyosin. |
title_full_unstemmed |
cDNA cloning, expression and characterization of a Boophilus microplus paramyosin. |
title_sort |
cDNA cloning, expression and characterization of a Boophilus microplus paramyosin. |
author |
Ferreira, Carlos Alexandre Sanchez |
author_facet |
Ferreira, Carlos Alexandre Sanchez Barbosa, M. C. Silveira, Thiago Cesar Lima Valenzuela, J.G. Vaz Junior, Itabajara da Silva Masuda, Aoi |
author_role |
author |
author2 |
Barbosa, M. C. Silveira, Thiago Cesar Lima Valenzuela, J.G. Vaz Junior, Itabajara da Silva Masuda, Aoi |
author2_role |
author author author author author |
dc.contributor.author.fl_str_mv |
Ferreira, Carlos Alexandre Sanchez Barbosa, M. C. Silveira, Thiago Cesar Lima Valenzuela, J.G. Vaz Junior, Itabajara da Silva Masuda, Aoi |
dc.subject.por.fl_str_mv |
Parasitologia veterinária |
topic |
Parasitologia veterinária Paramyosin Boophilus microplus IgG binding protein Collagen binding protein Tick |
dc.subject.eng.fl_str_mv |
Paramyosin Boophilus microplus IgG binding protein Collagen binding protein Tick |
description |
The tick Boophilus microplus is a 1-host tick that causes important losses to bovine herds, and protective antigens are being investigated in order to develop vaccines that avoid the use of acaricides. Paramyosins are multi-functional invertebrate muscle proteins, whose roles may include host immunomodulation, and seem to be a prominent candidate in a schistosomiasis vaccine. We report here the cloning, expression and characterization of a B. microplus paramyosin (BmPRM). Sequence analysis of the full length coding sequence cDNA shows high identity to other arthropod paramyosin sequences, and the predicted molecular weight, pI and secondary structure are consistent with a typical paramyosin. Western-blot expression analysis indicates the presence of BmPRM in all tissues and developmental stages tested, but not in saliva. The recombinant protein (rBmPRM) was shown to bind both IgG and collagen. Possible implications of these activities with host evasion mechanisms are discussed. |
publishDate |
2002 |
dc.date.issued.fl_str_mv |
2002 |
dc.date.accessioned.fl_str_mv |
2011-01-21T05:59:00Z |
dc.type.driver.fl_str_mv |
Estrangeiro info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
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publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10183/27454 |
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0031-1820 |
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000337062 |
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0031-1820 000337062 |
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http://hdl.handle.net/10183/27454 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartof.pt_BR.fl_str_mv |
Parasitology. Inglaterra. Vol. 125, no. 3 (2002), p. 265-274 |
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info:eu-repo/semantics/openAccess |
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openAccess |
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application/pdf |
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