Rmcystatin3, a cysteine protease inhibitor from Rhipicephalus microplus hemocytes involved in immune response
Autor(a) principal: | |
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Data de Publicação: | 2014 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | http://repositorio.unifesp.br/handle/11600/38351 http://dx.doi.org/10.1016/j.biochi.2014.07.012 |
Resumo: | The Rhipicephalus microplus tick is responsible for losses in the livestock production estimated in 2 billions USD. Despite its economical importance the knowledge in tick's physiology is sparse. in order to contribute to this scenario we describe the characterization of a cysteine proteinase inhibitor named Rmcystatin-3. Purified recombinant Rmcystatin-3 was able to inhibit cathepsin L (Ki = 2.5 nM), BmCl1 (Ki = 1.8 nM) and cathepsin B (Ki = 136 nM). Western blot and quantitative PCR analysis revealed the presence of Rmcystatin-3 in fat body, salivary gland but mainly in hemocytes. the mRNA levels of Rmcystatin-3 during bacterial challenge are drastically down-regulated. in order to define the Rmcystatin-3 possible role in tick immunity, the cystatin gene was knockdown by RNA interference with and without Escherichia coli infection. Our results showed that the Rmcystatin-3 silenced group was more immune competent to control bacterial infection than the group injected with non-related dsRNA. Taking together, our data strongly suggested an important role of Rmcystatin-3 in tick immunity. (C) 2014 Elsevier B.V. and Societe francaise de biochimie et biologie Moleculaire (SFBBM). All rights reserved. |
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Lu, Stephen [UNIFESP]Soares, Tatiane Sanches [UNIFESP]Vaz Junior, Itabajara S.Lovato, Diogo Ventura [UNIFESP]Tanaka, Aparecida Sadae [UNIFESP]Universidade Federal de São Paulo (UNIFESP)Univ Fed Rio Grande do Sul2016-01-24T14:38:02Z2016-01-24T14:38:02Z2014-11-01Biochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 106C, p. 17-23, 2014.0300-9084http://repositorio.unifesp.br/handle/11600/38351http://dx.doi.org/10.1016/j.biochi.2014.07.012WOS000344434700003.pdf10.1016/j.biochi.2014.07.012WOS:000344434700003The Rhipicephalus microplus tick is responsible for losses in the livestock production estimated in 2 billions USD. Despite its economical importance the knowledge in tick's physiology is sparse. in order to contribute to this scenario we describe the characterization of a cysteine proteinase inhibitor named Rmcystatin-3. Purified recombinant Rmcystatin-3 was able to inhibit cathepsin L (Ki = 2.5 nM), BmCl1 (Ki = 1.8 nM) and cathepsin B (Ki = 136 nM). Western blot and quantitative PCR analysis revealed the presence of Rmcystatin-3 in fat body, salivary gland but mainly in hemocytes. the mRNA levels of Rmcystatin-3 during bacterial challenge are drastically down-regulated. in order to define the Rmcystatin-3 possible role in tick immunity, the cystatin gene was knockdown by RNA interference with and without Escherichia coli infection. Our results showed that the Rmcystatin-3 silenced group was more immune competent to control bacterial infection than the group injected with non-related dsRNA. Taking together, our data strongly suggested an important role of Rmcystatin-3 in tick immunity. (C) 2014 Elsevier B.V. and Societe francaise de biochimie et biologie Moleculaire (SFBBM). All rights reserved.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)INCT-Entomologia Molecular, BrazilUniversidade Federal de São Paulo, Dept Biochem, Escola Paulista Med, BR-04044020 São Paulo, BrazilUniv Fed Rio Grande do Sul, Ctr Biotecnol Estado Rio Grande do Sul, Porto Alegre, RS, BrazilUniversidade Federal de São Paulo, Dept Biochem, Escola Paulista Med, BR-04044020 São Paulo, BrazilFAPESP: 05/03514-9FAPESP: 09/17589-1FAPESP: 12/03657-8Web of Science17-23engElsevier B.V.Biochimiehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policyinfo:eu-repo/semantics/openAccessCystatinRNAiRhipicephalus microplusTicksInnate immunityRmcystatin3, a cysteine protease inhibitor from Rhipicephalus microplus hemocytes involved in immune responseinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlereponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESPORIGINALWOS000344434700003.pdfapplication/pdf1429411${dspace.ui.url}/bitstream/11600/38351/1/WOS000344434700003.pdfc4b6d9ed744ca45a108641c46679d3caMD51open accessTEXTWOS000344434700003.pdf.txtWOS000344434700003.pdf.txtExtracted texttext/plain37552${dspace.ui.url}/bitstream/11600/38351/2/WOS000344434700003.pdf.txt304b37c992a87eaa3b729dd9d558d410MD52open access11600/383512022-06-02 10:24:21.689open accessoai:repositorio.unifesp.br:11600/38351Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652022-06-02T13:24:21Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.fl_str_mv |
Rmcystatin3, a cysteine protease inhibitor from Rhipicephalus microplus hemocytes involved in immune response |
title |
Rmcystatin3, a cysteine protease inhibitor from Rhipicephalus microplus hemocytes involved in immune response |
spellingShingle |
Rmcystatin3, a cysteine protease inhibitor from Rhipicephalus microplus hemocytes involved in immune response Lu, Stephen [UNIFESP] Cystatin RNAi Rhipicephalus microplus Ticks Innate immunity |
title_short |
Rmcystatin3, a cysteine protease inhibitor from Rhipicephalus microplus hemocytes involved in immune response |
title_full |
Rmcystatin3, a cysteine protease inhibitor from Rhipicephalus microplus hemocytes involved in immune response |
title_fullStr |
Rmcystatin3, a cysteine protease inhibitor from Rhipicephalus microplus hemocytes involved in immune response |
title_full_unstemmed |
Rmcystatin3, a cysteine protease inhibitor from Rhipicephalus microplus hemocytes involved in immune response |
title_sort |
Rmcystatin3, a cysteine protease inhibitor from Rhipicephalus microplus hemocytes involved in immune response |
author |
Lu, Stephen [UNIFESP] |
author_facet |
Lu, Stephen [UNIFESP] Soares, Tatiane Sanches [UNIFESP] Vaz Junior, Itabajara S. Lovato, Diogo Ventura [UNIFESP] Tanaka, Aparecida Sadae [UNIFESP] |
author_role |
author |
author2 |
Soares, Tatiane Sanches [UNIFESP] Vaz Junior, Itabajara S. Lovato, Diogo Ventura [UNIFESP] Tanaka, Aparecida Sadae [UNIFESP] |
author2_role |
author author author author |
dc.contributor.institution.none.fl_str_mv |
Universidade Federal de São Paulo (UNIFESP) Univ Fed Rio Grande do Sul |
dc.contributor.author.fl_str_mv |
Lu, Stephen [UNIFESP] Soares, Tatiane Sanches [UNIFESP] Vaz Junior, Itabajara S. Lovato, Diogo Ventura [UNIFESP] Tanaka, Aparecida Sadae [UNIFESP] |
dc.subject.eng.fl_str_mv |
Cystatin RNAi Rhipicephalus microplus Ticks Innate immunity |
topic |
Cystatin RNAi Rhipicephalus microplus Ticks Innate immunity |
description |
The Rhipicephalus microplus tick is responsible for losses in the livestock production estimated in 2 billions USD. Despite its economical importance the knowledge in tick's physiology is sparse. in order to contribute to this scenario we describe the characterization of a cysteine proteinase inhibitor named Rmcystatin-3. Purified recombinant Rmcystatin-3 was able to inhibit cathepsin L (Ki = 2.5 nM), BmCl1 (Ki = 1.8 nM) and cathepsin B (Ki = 136 nM). Western blot and quantitative PCR analysis revealed the presence of Rmcystatin-3 in fat body, salivary gland but mainly in hemocytes. the mRNA levels of Rmcystatin-3 during bacterial challenge are drastically down-regulated. in order to define the Rmcystatin-3 possible role in tick immunity, the cystatin gene was knockdown by RNA interference with and without Escherichia coli infection. Our results showed that the Rmcystatin-3 silenced group was more immune competent to control bacterial infection than the group injected with non-related dsRNA. Taking together, our data strongly suggested an important role of Rmcystatin-3 in tick immunity. (C) 2014 Elsevier B.V. and Societe francaise de biochimie et biologie Moleculaire (SFBBM). All rights reserved. |
publishDate |
2014 |
dc.date.issued.fl_str_mv |
2014-11-01 |
dc.date.accessioned.fl_str_mv |
2016-01-24T14:38:02Z |
dc.date.available.fl_str_mv |
2016-01-24T14:38:02Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
Biochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 106C, p. 17-23, 2014. |
dc.identifier.uri.fl_str_mv |
http://repositorio.unifesp.br/handle/11600/38351 http://dx.doi.org/10.1016/j.biochi.2014.07.012 |
dc.identifier.issn.none.fl_str_mv |
0300-9084 |
dc.identifier.file.none.fl_str_mv |
WOS000344434700003.pdf |
dc.identifier.doi.none.fl_str_mv |
10.1016/j.biochi.2014.07.012 |
dc.identifier.wos.none.fl_str_mv |
WOS:000344434700003 |
identifier_str_mv |
Biochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 106C, p. 17-23, 2014. 0300-9084 WOS000344434700003.pdf 10.1016/j.biochi.2014.07.012 WOS:000344434700003 |
url |
http://repositorio.unifesp.br/handle/11600/38351 http://dx.doi.org/10.1016/j.biochi.2014.07.012 |
dc.language.iso.fl_str_mv |
eng |
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eng |
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Biochimie |
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http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy |
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openAccess |
dc.format.none.fl_str_mv |
17-23 |
dc.publisher.none.fl_str_mv |
Elsevier B.V. |
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Elsevier B.V. |
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