cDNA cloning, expression and characterization of a Boophilus microplus paramyosin.

Detalhes bibliográficos
Autor(a) principal: Ferreira, Carlos Alexandre Sanchez
Data de Publicação: 2002
Outros Autores: Barbosa, M. C., Silveira, Thiago Cesar Lima, Valenzuela, J.G., Vaz Junior, Itabajara da Silva, Masuda, Aoi
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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spelling 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
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dc.relation.ispartof.pt_BR.fl_str_mv Parasitology. Inglaterra. Vol. 125, no. 3 (2002), p. 265-274
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