Aurora kinase as a putative target to tick control
Aurora kinases (AURK) play a central role in controlling cell cycle in a wide range of organisms. They belong to the family of serine-threonine kinase proteins. Their role in the cell cycle includes, among others, the entry into mitosis, maturation of the centrosome and formation of the mitotic spin...
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Cambridge University Press
2024-08-01
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| Series: | Parasitology |
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| Online Access: | https://www.cambridge.org/core/product/identifier/S003118202400101X/type/journal_article |
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| author | Bruno Moraes Helga Gomes Luiz Saramago Valdir Braz Luís Fernando Parizi Gloria Braz Itabajara da Silva Vaz Carlos Logullo Jorge Moraes Ala Tabor |
| author_facet | Bruno Moraes Helga Gomes Luiz Saramago Valdir Braz Luís Fernando Parizi Gloria Braz Itabajara da Silva Vaz Carlos Logullo Jorge Moraes Ala Tabor |
| author_sort | Bruno Moraes |
| collection | DOAJ |
| description | Aurora kinases (AURK) play a central role in controlling cell cycle in a wide range of organisms. They belong to the family of serine-threonine kinase proteins. Their role in the cell cycle includes, among others, the entry into mitosis, maturation of the centrosome and formation of the mitotic spindle. In mammals, 3 isoforms have been described: A, B and C, which are distinguished mainly by their function throughout the cell cycle. Two aurora kinase coding sequences have been identified in the transcriptome of the cattle tick Rhipicephalus microplus (Rm-AURKA and Rm-AURKB) containing the aurora kinase-specific domain. For both isoforms, the highest number of AURK coding transcripts is found in ovaries. Based on deduced amino acid sequences, it was possible to identify non-conserved threonine residues which are essential to AURK functions in vertebrates and which are not present in R. microplus sequences. A pan AURK inhibitor (CCT137690) caused cell viability decline in the BME26 tick embryonic cell line. In silico docking assay showed an interaction between Aurora kinase and CCT137690 with exclusive interaction sites in Rm-AURKA. The characterization of exclusive regions of the enzyme will enable new studies aimed at promoting species-specific enzymatic inhibition in ectoparasites. |
| format | Article |
| id | doaj-art-513a57eeda404305823493a568f5c85e |
| institution | Kabale University |
| issn | 0031-1820 1469-8161 |
| language | English |
| publishDate | 2024-08-01 |
| publisher | Cambridge University Press |
| record_format | Article |
| series | Parasitology |
| spelling | doaj-art-513a57eeda404305823493a568f5c85e2025-01-23T07:11:40ZengCambridge University PressParasitology0031-18201469-81612024-08-0115198399110.1017/S003118202400101XAurora kinase as a putative target to tick controlBruno Moraes0Helga Gomes1Luiz Saramago2Valdir Braz3Luís Fernando Parizi4Gloria Braz5Itabajara da Silva Vaz6https://orcid.org/0000-0003-0309-9328Carlos Logullo7https://orcid.org/0000-0003-2798-5439Jorge Moraes8Ala TaborLaboratório de Bioquímica de Artrópodes Hematófagos, Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, RJ, Brazil Laboratório Integrado de Bioquímica Hatisaburo Masuda, NUPEM-Universidade Federal do Rio de Janeiro campus Macaé, BrazilLaboratório de Tecido Conjuntivo, Hospital Universitário Clementino Fraga Filho and Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, RJ, BrazilLaboratório Integrado de Bioquímica Hatisaburo Masuda, NUPEM-Universidade Federal do Rio de Janeiro campus Macaé, BrazilLaboratório Integrado de Bioquímica Hatisaburo Masuda, NUPEM-Universidade Federal do Rio de Janeiro campus Macaé, BrazilCentro de Biotecnologia and Faculdade de Veterinária, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS, BrazilInstituto de Química, Universidade Federal do Rio de Janeiro, RJ, BrazilCentro de Biotecnologia and Faculdade de Veterinária, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS, Brazil Instituto Nacional de Ciência e Tecnologia em Entomologia Molecular, Rio de Janeiro, RJ, BrazilLaboratório de Bioquímica de Artrópodes Hematófagos, Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, RJ, Brazil Instituto Nacional de Ciência e Tecnologia em Entomologia Molecular, Rio de Janeiro, RJ, BrazilLaboratório Integrado de Bioquímica Hatisaburo Masuda, NUPEM-Universidade Federal do Rio de Janeiro campus Macaé, Brazil Instituto Nacional de Ciência e Tecnologia em Entomologia Molecular, Rio de Janeiro, RJ, BrazilAurora kinases (AURK) play a central role in controlling cell cycle in a wide range of organisms. They belong to the family of serine-threonine kinase proteins. Their role in the cell cycle includes, among others, the entry into mitosis, maturation of the centrosome and formation of the mitotic spindle. In mammals, 3 isoforms have been described: A, B and C, which are distinguished mainly by their function throughout the cell cycle. Two aurora kinase coding sequences have been identified in the transcriptome of the cattle tick Rhipicephalus microplus (Rm-AURKA and Rm-AURKB) containing the aurora kinase-specific domain. For both isoforms, the highest number of AURK coding transcripts is found in ovaries. Based on deduced amino acid sequences, it was possible to identify non-conserved threonine residues which are essential to AURK functions in vertebrates and which are not present in R. microplus sequences. A pan AURK inhibitor (CCT137690) caused cell viability decline in the BME26 tick embryonic cell line. In silico docking assay showed an interaction between Aurora kinase and CCT137690 with exclusive interaction sites in Rm-AURKA. The characterization of exclusive regions of the enzyme will enable new studies aimed at promoting species-specific enzymatic inhibition in ectoparasites.https://www.cambridge.org/core/product/identifier/S003118202400101X/type/journal_articleAurora-kinaseBME26CCT137690embryonic cellRhipicephalus microplustick |
| spellingShingle | Bruno Moraes Helga Gomes Luiz Saramago Valdir Braz Luís Fernando Parizi Gloria Braz Itabajara da Silva Vaz Carlos Logullo Jorge Moraes Ala Tabor Aurora kinase as a putative target to tick control Parasitology Aurora-kinase BME26 CCT137690 embryonic cell Rhipicephalus microplus tick |
| title | Aurora kinase as a putative target to tick control |
| title_full | Aurora kinase as a putative target to tick control |
| title_fullStr | Aurora kinase as a putative target to tick control |
| title_full_unstemmed | Aurora kinase as a putative target to tick control |
| title_short | Aurora kinase as a putative target to tick control |
| title_sort | aurora kinase as a putative target to tick control |
| topic | Aurora-kinase BME26 CCT137690 embryonic cell Rhipicephalus microplus tick |
| url | https://www.cambridge.org/core/product/identifier/S003118202400101X/type/journal_article |
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