A novel type 1 cystatin involved in the regulation of Rhipicephalus microplus midgut cysteine proteases
- Autores
- Lu, Stephen; Rocha, Leticia A. da; Torquato, Ricardo J.S.; Vaz Junior, Itabajara da Silva; Florin-Christensen, Mónica; Tanaka, Aparecida S.
- Año de publicación
- 2020
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Rhipicephalus microplus is a cattle ectoparasite found in tropical and subtropical regions around the world with great impact on livestock production. R. microplus can also harbor pathogens, such as Babesia sp. and Anaplasma sp. which further compromise cattle production. Blood meal acquisition and digestion are key steps for tick development. In ticks, digestion takes place inside midgut cells and is mediated by aspartic and cysteine peptidases and, therefore, regulated by their inhibitors. Cystatins are a family of cysteine peptidases inhibitors found in several organisms and have been associated in ticks with blood acquisition, blood digestion, modulation of host immune response and tick immunity. In this work, we characterized a novel R. microplus type 1 cystatin, named Rmcystatin-1b. The inhibitor transcripts were found to be highly expressed in the midgut of partially and fully engorged females and they appear to be modulated at different days post-detachment. Purified recombinant Rmcystatin-1b displayed inhibitory activity towards typical cysteine peptidases with high affinity. Moreover, rRmcystatin-1b was able to inhibit native R. microplus cysteine peptidases and RNAi-mediated knockdown of the cystatin transcripts resulted in increased proteolytic activity. Moreover, rRmcystatin-1b was able to interfere with B. bovis growth in vitro. Taken together our data strongly suggest that Rmcystatin-1b is a regulator of blood digestion in R. microplus midgut.
Instituto de Patobiología
Fil: Lu, Stephen. Universidade de Federal de São Paulo. Escola Paulista de Medicina. Department of Biochemistry; Brasil
Fil: Rocha, Leticia A. da. Universidade de Federal de São Paulo. Escola Paulista de Medicina. Department of Biochemistry; Brasil
Fil: Torquato, Ricardo J.S. Universidade de Federal de São Paulo. Escola Paulista de Medicina. Department of Biochemistry; Brasil
Fil: Vaz Junior, Itabajara da Silva. Universidade Federal do Rio Grande do Sul. Centro de Biotecnologia e Faculdade de Veterinária; Brasil. Instituto Nacional de Ciência e Tecnologia em Entomologia Molecular; Brasil
Fil: Florin-Christensen, Monica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Tanaka, Aparecida S. Universidade de Federal de São Paulo. Escola Paulista de Medicina. Department of Biochemistry; Brasil. Instituto Nacional de Ciência e Tecnologia em Entomologia Molecular; Brasil - Fuente
- Ticks and Tick-borne Diseases 11 (3) : 101374 (May 2020)
- Materia
-
Rhipicephalus
Ganado Bovino
Cisteína
Cattle
Cysteine
Garrapatas
Rhipicephalus (Boophilus) microplus
Cystatin - Nivel de accesibilidad
- acceso restringido
- Condiciones de uso
- Repositorio
- Institución
- Instituto Nacional de Tecnología Agropecuaria
- OAI Identificador
- oai:localhost:20.500.12123/7737
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A novel type 1 cystatin involved in the regulation of Rhipicephalus microplus midgut cysteine proteasesLu, StephenRocha, Leticia A. daTorquato, Ricardo J.S.Vaz Junior, Itabajara da SilvaFlorin-Christensen, MónicaTanaka, Aparecida S.RhipicephalusGanado BovinoCisteínaCattleCysteineGarrapatasRhipicephalus (Boophilus) microplusCystatinRhipicephalus microplus is a cattle ectoparasite found in tropical and subtropical regions around the world with great impact on livestock production. R. microplus can also harbor pathogens, such as Babesia sp. and Anaplasma sp. which further compromise cattle production. Blood meal acquisition and digestion are key steps for tick development. In ticks, digestion takes place inside midgut cells and is mediated by aspartic and cysteine peptidases and, therefore, regulated by their inhibitors. Cystatins are a family of cysteine peptidases inhibitors found in several organisms and have been associated in ticks with blood acquisition, blood digestion, modulation of host immune response and tick immunity. In this work, we characterized a novel R. microplus type 1 cystatin, named Rmcystatin-1b. The inhibitor transcripts were found to be highly expressed in the midgut of partially and fully engorged females and they appear to be modulated at different days post-detachment. Purified recombinant Rmcystatin-1b displayed inhibitory activity towards typical cysteine peptidases with high affinity. Moreover, rRmcystatin-1b was able to inhibit native R. microplus cysteine peptidases and RNAi-mediated knockdown of the cystatin transcripts resulted in increased proteolytic activity. Moreover, rRmcystatin-1b was able to interfere with B. bovis growth in vitro. Taken together our data strongly suggest that Rmcystatin-1b is a regulator of blood digestion in R. microplus midgut.Instituto de PatobiologíaFil: Lu, Stephen. Universidade de Federal de São Paulo. Escola Paulista de Medicina. Department of Biochemistry; BrasilFil: Rocha, Leticia A. da. Universidade de Federal de São Paulo. Escola Paulista de Medicina. Department of Biochemistry; BrasilFil: Torquato, Ricardo J.S. Universidade de Federal de São Paulo. Escola Paulista de Medicina. Department of Biochemistry; BrasilFil: Vaz Junior, Itabajara da Silva. Universidade Federal do Rio Grande do Sul. Centro de Biotecnologia e Faculdade de Veterinária; Brasil. Instituto Nacional de Ciência e Tecnologia em Entomologia Molecular; BrasilFil: Florin-Christensen, Monica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Tanaka, Aparecida S. Universidade de Federal de São Paulo. Escola Paulista de Medicina. Department of Biochemistry; Brasil. Instituto Nacional de Ciência e Tecnologia em Entomologia Molecular; BrasilElsevier2020-08-19T13:27:22Z2020-08-19T13:27:22Z2020-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12123/7737https://www.sciencedirect.com/science/article/abs/pii/S1877959X193040421877-959Xhttps://doi.org/10.1016/j.ttbdis.2020.101374Ticks and Tick-borne Diseases 11 (3) : 101374 (May 2020)reponame:INTA Digital (INTA)instname:Instituto Nacional de Tecnología Agropecuariaenginfo:eu-repo/semantics/restrictedAccess2025-09-11T10:23:29Zoai:localhost:20.500.12123/7737instacron:INTAInstitucionalhttp://repositorio.inta.gob.ar/Organismo científico-tecnológicoNo correspondehttp://repositorio.inta.gob.ar/oai/requesttripaldi.nicolas@inta.gob.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:l2025-09-11 10:23:29.961INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuariafalse |
dc.title.none.fl_str_mv |
A novel type 1 cystatin involved in the regulation of Rhipicephalus microplus midgut cysteine proteases |
title |
A novel type 1 cystatin involved in the regulation of Rhipicephalus microplus midgut cysteine proteases |
spellingShingle |
A novel type 1 cystatin involved in the regulation of Rhipicephalus microplus midgut cysteine proteases Lu, Stephen Rhipicephalus Ganado Bovino Cisteína Cattle Cysteine Garrapatas Rhipicephalus (Boophilus) microplus Cystatin |
title_short |
A novel type 1 cystatin involved in the regulation of Rhipicephalus microplus midgut cysteine proteases |
title_full |
A novel type 1 cystatin involved in the regulation of Rhipicephalus microplus midgut cysteine proteases |
title_fullStr |
A novel type 1 cystatin involved in the regulation of Rhipicephalus microplus midgut cysteine proteases |
title_full_unstemmed |
A novel type 1 cystatin involved in the regulation of Rhipicephalus microplus midgut cysteine proteases |
title_sort |
A novel type 1 cystatin involved in the regulation of Rhipicephalus microplus midgut cysteine proteases |
dc.creator.none.fl_str_mv |
Lu, Stephen Rocha, Leticia A. da Torquato, Ricardo J.S. Vaz Junior, Itabajara da Silva Florin-Christensen, Mónica Tanaka, Aparecida S. |
author |
Lu, Stephen |
author_facet |
Lu, Stephen Rocha, Leticia A. da Torquato, Ricardo J.S. Vaz Junior, Itabajara da Silva Florin-Christensen, Mónica Tanaka, Aparecida S. |
author_role |
author |
author2 |
Rocha, Leticia A. da Torquato, Ricardo J.S. Vaz Junior, Itabajara da Silva Florin-Christensen, Mónica Tanaka, Aparecida S. |
author2_role |
author author author author author |
dc.subject.none.fl_str_mv |
Rhipicephalus Ganado Bovino Cisteína Cattle Cysteine Garrapatas Rhipicephalus (Boophilus) microplus Cystatin |
topic |
Rhipicephalus Ganado Bovino Cisteína Cattle Cysteine Garrapatas Rhipicephalus (Boophilus) microplus Cystatin |
dc.description.none.fl_txt_mv |
Rhipicephalus microplus is a cattle ectoparasite found in tropical and subtropical regions around the world with great impact on livestock production. R. microplus can also harbor pathogens, such as Babesia sp. and Anaplasma sp. which further compromise cattle production. Blood meal acquisition and digestion are key steps for tick development. In ticks, digestion takes place inside midgut cells and is mediated by aspartic and cysteine peptidases and, therefore, regulated by their inhibitors. Cystatins are a family of cysteine peptidases inhibitors found in several organisms and have been associated in ticks with blood acquisition, blood digestion, modulation of host immune response and tick immunity. In this work, we characterized a novel R. microplus type 1 cystatin, named Rmcystatin-1b. The inhibitor transcripts were found to be highly expressed in the midgut of partially and fully engorged females and they appear to be modulated at different days post-detachment. Purified recombinant Rmcystatin-1b displayed inhibitory activity towards typical cysteine peptidases with high affinity. Moreover, rRmcystatin-1b was able to inhibit native R. microplus cysteine peptidases and RNAi-mediated knockdown of the cystatin transcripts resulted in increased proteolytic activity. Moreover, rRmcystatin-1b was able to interfere with B. bovis growth in vitro. Taken together our data strongly suggest that Rmcystatin-1b is a regulator of blood digestion in R. microplus midgut. Instituto de Patobiología Fil: Lu, Stephen. Universidade de Federal de São Paulo. Escola Paulista de Medicina. Department of Biochemistry; Brasil Fil: Rocha, Leticia A. da. Universidade de Federal de São Paulo. Escola Paulista de Medicina. Department of Biochemistry; Brasil Fil: Torquato, Ricardo J.S. Universidade de Federal de São Paulo. Escola Paulista de Medicina. Department of Biochemistry; Brasil Fil: Vaz Junior, Itabajara da Silva. Universidade Federal do Rio Grande do Sul. Centro de Biotecnologia e Faculdade de Veterinária; Brasil. Instituto Nacional de Ciência e Tecnologia em Entomologia Molecular; Brasil Fil: Florin-Christensen, Monica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Tanaka, Aparecida S. Universidade de Federal de São Paulo. Escola Paulista de Medicina. Department of Biochemistry; Brasil. Instituto Nacional de Ciência e Tecnologia em Entomologia Molecular; Brasil |
description |
Rhipicephalus microplus is a cattle ectoparasite found in tropical and subtropical regions around the world with great impact on livestock production. R. microplus can also harbor pathogens, such as Babesia sp. and Anaplasma sp. which further compromise cattle production. Blood meal acquisition and digestion are key steps for tick development. In ticks, digestion takes place inside midgut cells and is mediated by aspartic and cysteine peptidases and, therefore, regulated by their inhibitors. Cystatins are a family of cysteine peptidases inhibitors found in several organisms and have been associated in ticks with blood acquisition, blood digestion, modulation of host immune response and tick immunity. In this work, we characterized a novel R. microplus type 1 cystatin, named Rmcystatin-1b. The inhibitor transcripts were found to be highly expressed in the midgut of partially and fully engorged females and they appear to be modulated at different days post-detachment. Purified recombinant Rmcystatin-1b displayed inhibitory activity towards typical cysteine peptidases with high affinity. Moreover, rRmcystatin-1b was able to inhibit native R. microplus cysteine peptidases and RNAi-mediated knockdown of the cystatin transcripts resulted in increased proteolytic activity. Moreover, rRmcystatin-1b was able to interfere with B. bovis growth in vitro. Taken together our data strongly suggest that Rmcystatin-1b is a regulator of blood digestion in R. microplus midgut. |
publishDate |
2020 |
dc.date.none.fl_str_mv |
2020-08-19T13:27:22Z 2020-08-19T13:27:22Z 2020-05 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/20.500.12123/7737 https://www.sciencedirect.com/science/article/abs/pii/S1877959X19304042 1877-959X https://doi.org/10.1016/j.ttbdis.2020.101374 |
url |
http://hdl.handle.net/20.500.12123/7737 https://www.sciencedirect.com/science/article/abs/pii/S1877959X19304042 https://doi.org/10.1016/j.ttbdis.2020.101374 |
identifier_str_mv |
1877-959X |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/restrictedAccess |
eu_rights_str_mv |
restrictedAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier |
publisher.none.fl_str_mv |
Elsevier |
dc.source.none.fl_str_mv |
Ticks and Tick-borne Diseases 11 (3) : 101374 (May 2020) reponame:INTA Digital (INTA) instname:Instituto Nacional de Tecnología Agropecuaria |
reponame_str |
INTA Digital (INTA) |
collection |
INTA Digital (INTA) |
instname_str |
Instituto Nacional de Tecnología Agropecuaria |
repository.name.fl_str_mv |
INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuaria |
repository.mail.fl_str_mv |
tripaldi.nicolas@inta.gob.ar |
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1842975491471966208 |
score |
12.993085 |