Identification and structural -functional analysis of cyclin-dependent kinases of the cattle tick Rhipicephalus (Boophilus) microplus
Autor(a) principal: | |
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Data de Publicação: | 2013 |
Outros Autores: | , , , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UFRGS |
Texto Completo: | http://hdl.handle.net/10183/225246 |
Resumo: | Cyclin-dependent kinases (CDKs) are a family of serine/threonine kinases essential for cell cycle progression. Herein, we describe the participation of CDKs in the physiology of Rhipicephalus microplus, the southern cattle tick and an important disease vector. Firstly, amino acid sequences homologous with CDKs of other organisms were identified from a R. microplus transcriptome database in silico. The analysis of the deduced amino acid sequences of CDK1 and CDK10 from R. microplus showed that both have caspase-3/7 cleavage motifs despite their differences in motif position and length of encoded proteins. CDK1 has two motifs (DKRGD and SAKDA) located opposite to the ATP binding site while CDK10 has only one motif (SLLDN) for caspase 3–7 near the ATP binding site. Roscovitine (Rosco), a purine derivative that inhibits CDK/cyclin complexes by binding to the catalytic domain of the CDK molecule at the ATP binding site, which prevents the transfer of ATP’s cphosphoryl group to the substrate. To determine the effect of Rosco on tick CDKs, BME26 cells derived from R. microplus embryo cells were utilized in vitro inhibition assays. Cell viability decreased in the Rosco-treated groups after 24 hours of incubation in a concentration-dependent manner and this was observed up to 48 hours following incubation. To our knowledge, this is the first report on characterization of a cell cycle protein in arachnids, and the sensitivity of BME26 tick cell line to Rosco treatment suggests that CDKs are potential targets for novel drug design to control tick infestation. |
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Gomes, HelgaRomeiro, Nelilma C.Braz, Greicy Rose de CarvalhoOliveira, Eduardo Alves GamosaRodrigues, CamilaFonseca, Rodrigo N. daGithaka, NaftalyIsezaki, MasayoshiKonnai, SatoruOhashi, KazuhikoVaz Junior, Itabajara da SilvaLogullo, CarlosMoraes, Jorge2021-08-06T04:40:57Z20131932-6203http://hdl.handle.net/10183/225246000903250Cyclin-dependent kinases (CDKs) are a family of serine/threonine kinases essential for cell cycle progression. Herein, we describe the participation of CDKs in the physiology of Rhipicephalus microplus, the southern cattle tick and an important disease vector. Firstly, amino acid sequences homologous with CDKs of other organisms were identified from a R. microplus transcriptome database in silico. The analysis of the deduced amino acid sequences of CDK1 and CDK10 from R. microplus showed that both have caspase-3/7 cleavage motifs despite their differences in motif position and length of encoded proteins. CDK1 has two motifs (DKRGD and SAKDA) located opposite to the ATP binding site while CDK10 has only one motif (SLLDN) for caspase 3–7 near the ATP binding site. Roscovitine (Rosco), a purine derivative that inhibits CDK/cyclin complexes by binding to the catalytic domain of the CDK molecule at the ATP binding site, which prevents the transfer of ATP’s cphosphoryl group to the substrate. To determine the effect of Rosco on tick CDKs, BME26 cells derived from R. microplus embryo cells were utilized in vitro inhibition assays. Cell viability decreased in the Rosco-treated groups after 24 hours of incubation in a concentration-dependent manner and this was observed up to 48 hours following incubation. To our knowledge, this is the first report on characterization of a cell cycle protein in arachnids, and the sensitivity of BME26 tick cell line to Rosco treatment suggests that CDKs are potential targets for novel drug design to control tick infestation.application/pdfengPLOS ONE. San Francisco,. Vol. 8, n. 10 (Aug. 2013), e76128, 12 p.Rhipicephalus microplusIdentification and structural -functional analysis of cyclin-dependent kinases of the cattle tick Rhipicephalus (Boophilus) microplusEstrangeiroinfo: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:UFRGSTEXT000903250.pdf.txt000903250.pdf.txtExtracted Texttext/plain51989http://www.lume.ufrgs.br/bitstream/10183/225246/2/000903250.pdf.txt188a906accd9029774f99b73cb95c06cMD52ORIGINAL000903250.pdfTexto completo (inglês)application/pdf4448559http://www.lume.ufrgs.br/bitstream/10183/225246/1/000903250.pdf0a02eef2c9e1e5a7d3643d8e815d3b3bMD5110183/2252462023-09-23 03:34:04.734192oai:www.lume.ufrgs.br:10183/225246Repositório de PublicaçõesPUBhttps://lume.ufrgs.br/oai/requestopendoar:2023-09-23T06:34:04Repositório Institucional da UFRGS - Universidade Federal do Rio Grande do Sul (UFRGS)false |
dc.title.pt_BR.fl_str_mv |
Identification and structural -functional analysis of cyclin-dependent kinases of the cattle tick Rhipicephalus (Boophilus) microplus |
title |
Identification and structural -functional analysis of cyclin-dependent kinases of the cattle tick Rhipicephalus (Boophilus) microplus |
spellingShingle |
Identification and structural -functional analysis of cyclin-dependent kinases of the cattle tick Rhipicephalus (Boophilus) microplus Gomes, Helga Rhipicephalus microplus |
title_short |
Identification and structural -functional analysis of cyclin-dependent kinases of the cattle tick Rhipicephalus (Boophilus) microplus |
title_full |
Identification and structural -functional analysis of cyclin-dependent kinases of the cattle tick Rhipicephalus (Boophilus) microplus |
title_fullStr |
Identification and structural -functional analysis of cyclin-dependent kinases of the cattle tick Rhipicephalus (Boophilus) microplus |
title_full_unstemmed |
Identification and structural -functional analysis of cyclin-dependent kinases of the cattle tick Rhipicephalus (Boophilus) microplus |
title_sort |
Identification and structural -functional analysis of cyclin-dependent kinases of the cattle tick Rhipicephalus (Boophilus) microplus |
author |
Gomes, Helga |
author_facet |
Gomes, Helga Romeiro, Nelilma C. Braz, Greicy Rose de Carvalho Oliveira, Eduardo Alves Gamosa Rodrigues, Camila Fonseca, Rodrigo N. da Githaka, Naftaly Isezaki, Masayoshi Konnai, Satoru Ohashi, Kazuhiko Vaz Junior, Itabajara da Silva Logullo, Carlos Moraes, Jorge |
author_role |
author |
author2 |
Romeiro, Nelilma C. Braz, Greicy Rose de Carvalho Oliveira, Eduardo Alves Gamosa Rodrigues, Camila Fonseca, Rodrigo N. da Githaka, Naftaly Isezaki, Masayoshi Konnai, Satoru Ohashi, Kazuhiko Vaz Junior, Itabajara da Silva Logullo, Carlos Moraes, Jorge |
author2_role |
author author author author author author author author author author author author |
dc.contributor.author.fl_str_mv |
Gomes, Helga Romeiro, Nelilma C. Braz, Greicy Rose de Carvalho Oliveira, Eduardo Alves Gamosa Rodrigues, Camila Fonseca, Rodrigo N. da Githaka, Naftaly Isezaki, Masayoshi Konnai, Satoru Ohashi, Kazuhiko Vaz Junior, Itabajara da Silva Logullo, Carlos Moraes, Jorge |
dc.subject.por.fl_str_mv |
Rhipicephalus microplus |
topic |
Rhipicephalus microplus |
description |
Cyclin-dependent kinases (CDKs) are a family of serine/threonine kinases essential for cell cycle progression. Herein, we describe the participation of CDKs in the physiology of Rhipicephalus microplus, the southern cattle tick and an important disease vector. Firstly, amino acid sequences homologous with CDKs of other organisms were identified from a R. microplus transcriptome database in silico. The analysis of the deduced amino acid sequences of CDK1 and CDK10 from R. microplus showed that both have caspase-3/7 cleavage motifs despite their differences in motif position and length of encoded proteins. CDK1 has two motifs (DKRGD and SAKDA) located opposite to the ATP binding site while CDK10 has only one motif (SLLDN) for caspase 3–7 near the ATP binding site. Roscovitine (Rosco), a purine derivative that inhibits CDK/cyclin complexes by binding to the catalytic domain of the CDK molecule at the ATP binding site, which prevents the transfer of ATP’s cphosphoryl group to the substrate. To determine the effect of Rosco on tick CDKs, BME26 cells derived from R. microplus embryo cells were utilized in vitro inhibition assays. Cell viability decreased in the Rosco-treated groups after 24 hours of incubation in a concentration-dependent manner and this was observed up to 48 hours following incubation. To our knowledge, this is the first report on characterization of a cell cycle protein in arachnids, and the sensitivity of BME26 tick cell line to Rosco treatment suggests that CDKs are potential targets for novel drug design to control tick infestation. |
publishDate |
2013 |
dc.date.issued.fl_str_mv |
2013 |
dc.date.accessioned.fl_str_mv |
2021-08-06T04:40:57Z |
dc.type.driver.fl_str_mv |
Estrangeiro info:eu-repo/semantics/article |
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format |
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publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10183/225246 |
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1932-6203 |
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000903250 |
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http://hdl.handle.net/10183/225246 |
dc.language.iso.fl_str_mv |
eng |
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dc.relation.ispartof.pt_BR.fl_str_mv |
PLOS ONE. San Francisco,. Vol. 8, n. 10 (Aug. 2013), e76128, 12 p. |
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info:eu-repo/semantics/openAccess |
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