Identification and structural -functional analysis of cyclin-dependent kinases of the cattle tick Rhipicephalus (Boophilus) microplus

Detalhes bibliográficos
Autor(a) principal: Gomes, Helga
Data de Publicação: 2013
Outros Autores: 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
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.
id UFRGS-2_7af5b0e94a45b61a4b994d527b76f83b
oai_identifier_str oai:www.lume.ufrgs.br:10183/225246
network_acronym_str UFRGS-2
network_name_str Repositório Institucional da UFRGS
repository_id_str
spelling 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
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10183/225246
dc.identifier.issn.pt_BR.fl_str_mv 1932-6203
dc.identifier.nrb.pt_BR.fl_str_mv 000903250
identifier_str_mv 1932-6203
000903250
url http://hdl.handle.net/10183/225246
dc.language.iso.fl_str_mv eng
language eng
dc.relation.ispartof.pt_BR.fl_str_mv PLOS ONE. San Francisco,. Vol. 8, n. 10 (Aug. 2013), e76128, 12 p.
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Repositório Institucional da UFRGS
instname:Universidade Federal do Rio Grande do Sul (UFRGS)
instacron:UFRGS
instname_str Universidade Federal do Rio Grande do Sul (UFRGS)
instacron_str UFRGS
institution UFRGS
reponame_str Repositório Institucional da UFRGS
collection Repositório Institucional da UFRGS
bitstream.url.fl_str_mv http://www.lume.ufrgs.br/bitstream/10183/225246/2/000903250.pdf.txt
http://www.lume.ufrgs.br/bitstream/10183/225246/1/000903250.pdf
bitstream.checksum.fl_str_mv 188a906accd9029774f99b73cb95c06c
0a02eef2c9e1e5a7d3643d8e815d3b3b
bitstream.checksumAlgorithm.fl_str_mv MD5
MD5
repository.name.fl_str_mv Repositório Institucional da UFRGS - Universidade Federal do Rio Grande do Sul (UFRGS)
repository.mail.fl_str_mv
_version_ 1801225030996066304