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
INTA Digital (INTA)
Institución
Instituto Nacional de Tecnología Agropecuaria
OAI Identificador
oai:localhost:20.500.12123/7737

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oai_identifier_str oai:localhost:20.500.12123/7737
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network_name_str INTA Digital (INTA)
spelling 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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