Soybean ubiquitous urease with purification facilitator: An addition to the moonlighting studies toolbox

Autores
Martinelli, Anne H.S.; Lopes, Fernanda C.; Broll, Valquiria; Defferrari, Marina S.; Ligabue-Braun, Rodrigo; Kappaun, Karine; Tichota, Deise M.; Fruttero, Leonardo Luis; Moyetta, Natalia Rita; Demartini, Diogo R.; Postal, Melissa; Medeiros-Silva, Monica; Becker-Ritt, Arlete Beatriz; Pasquali, Giancarlo; Carlini, Célia Regina R S
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Ureases are nickel-dependent enzymes that catalyze the hydrolysis of urea to ammonia and carbon dioxide. In soybean (Glycine max), the embryo-specific urease (eSBU), the ubiquitous urease (uSBU), and a third isoform (SBU-III) are synthesized. Our group has previously demonstrated that eSBU, purified from seeds, has antifungal properties against phytopathogenic fungi, entomotoxicity against Dysdercus peruvianus, the ability to induce blood platelet aggregation, and these properties are independent of its enzymatic activity. Here we describe the biological properties of apo-uSBU fused to glutathione S-transferase (GST) produced in Escherichia coli. Removal of GST affected apo-uSBU stability. We performed a Response Surface Methodology to optimize GST-uSBU production to 5 mg per liter and then bioassays were carried out. The recombinant protein exhibited inhibitory effects on filamentous fungi and affected fungal secondary metabolism. Candida albicans and C. tropicalis were also susceptible to GST-uSBU and formed pseudo-hyphae. The fusion protein was toxic against Rhodnius prolixus, with the toxicity being accompanied by in vivo and in vitro hemocyte aggregation. Rabbit platelet also aggregated in the presence of GST-uSBU. Thus, uSBU displayed similar biological properties as previously described for eSBU even when fused to GST, reinforcing the proposed role of ureases in plant defense.
Fil: Martinelli, Anne H.S.. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Lopes, Fernanda C.. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Broll, Valquiria. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Defferrari, Marina S.. University of Toronto; Canadá
Fil: Ligabue-Braun, Rodrigo. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Kappaun, Karine. Pontificia Universidade Católica do Rio Grande do Sul; Brasil
Fil: Tichota, Deise M.. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Fruttero, Leonardo Luis. Pontificia Universidade Católica do Rio Grande do Sul; Brasil. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
Fil: Moyetta, Natalia Rita. Pontificia Universidade Católica do Rio Grande do Sul; Brasil. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
Fil: Demartini, Diogo R.. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Postal, Melissa. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Medeiros-Silva, Monica. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Becker-Ritt, Arlete Beatriz. Universidade Luterana Do Brasil; Brasil
Fil: Pasquali, Giancarlo. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Carlini, Célia Regina R S. Pontificia Universidade Católica do Rio Grande do Sul; Brasil
Materia
ANTIFUNGAL ACTIVITY
FUNGAL PIGMENTS
INSECTICIDAL ACTIVITY
PRODUCTION OPTIMIZATION
SOYBEAN
UBIQUITOUS UREASE
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/55116
Acceder
id CONICETDig_0a47110196a29617c925f02524473b76
oai_identifier_str oai:ri.conicet.gov.ar:11336/55116
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Soybean ubiquitous urease with purification facilitator: An addition to the moonlighting studies toolboxMartinelli, Anne H.S.Lopes, Fernanda C.Broll, ValquiriaDefferrari, Marina S.Ligabue-Braun, RodrigoKappaun, KarineTichota, Deise M.Fruttero, Leonardo LuisMoyetta, Natalia RitaDemartini, Diogo R.Postal, MelissaMedeiros-Silva, MonicaBecker-Ritt, Arlete BeatrizPasquali, GiancarloCarlini, Célia Regina R SANTIFUNGAL ACTIVITYFUNGAL PIGMENTSINSECTICIDAL ACTIVITYPRODUCTION OPTIMIZATIONSOYBEANUBIQUITOUS UREASEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Ureases are nickel-dependent enzymes that catalyze the hydrolysis of urea to ammonia and carbon dioxide. In soybean (Glycine max), the embryo-specific urease (eSBU), the ubiquitous urease (uSBU), and a third isoform (SBU-III) are synthesized. Our group has previously demonstrated that eSBU, purified from seeds, has antifungal properties against phytopathogenic fungi, entomotoxicity against Dysdercus peruvianus, the ability to induce blood platelet aggregation, and these properties are independent of its enzymatic activity. Here we describe the biological properties of apo-uSBU fused to glutathione S-transferase (GST) produced in Escherichia coli. Removal of GST affected apo-uSBU stability. We performed a Response Surface Methodology to optimize GST-uSBU production to 5 mg per liter and then bioassays were carried out. The recombinant protein exhibited inhibitory effects on filamentous fungi and affected fungal secondary metabolism. Candida albicans and C. tropicalis were also susceptible to GST-uSBU and formed pseudo-hyphae. The fusion protein was toxic against Rhodnius prolixus, with the toxicity being accompanied by in vivo and in vitro hemocyte aggregation. Rabbit platelet also aggregated in the presence of GST-uSBU. Thus, uSBU displayed similar biological properties as previously described for eSBU even when fused to GST, reinforcing the proposed role of ureases in plant defense.Fil: Martinelli, Anne H.S.. Universidade Federal do Rio Grande do Sul; BrasilFil: Lopes, Fernanda C.. Universidade Federal do Rio Grande do Sul; BrasilFil: Broll, Valquiria. Universidade Federal do Rio Grande do Sul; BrasilFil: Defferrari, Marina S.. University of Toronto; CanadáFil: Ligabue-Braun, Rodrigo. Universidade Federal do Rio Grande do Sul; BrasilFil: Kappaun, Karine. Pontificia Universidade Católica do Rio Grande do Sul; BrasilFil: Tichota, Deise M.. Universidade Federal do Rio Grande do Sul; BrasilFil: Fruttero, Leonardo Luis. Pontificia Universidade Católica do Rio Grande do Sul; Brasil. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; ArgentinaFil: Moyetta, Natalia Rita. Pontificia Universidade Católica do Rio Grande do Sul; Brasil. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; ArgentinaFil: Demartini, Diogo R.. Universidade Federal do Rio Grande do Sul; BrasilFil: Postal, Melissa. Universidade Federal do Rio Grande do Sul; BrasilFil: Medeiros-Silva, Monica. Universidade Federal do Rio Grande do Sul; BrasilFil: Becker-Ritt, Arlete Beatriz. Universidade Luterana Do Brasil; BrasilFil: Pasquali, Giancarlo. Universidade Federal do Rio Grande do Sul; BrasilFil: Carlini, Célia Regina R S. Pontificia Universidade Católica do Rio Grande do Sul; BrasilElsevier2017-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/55116Martinelli, Anne H.S.; Lopes, Fernanda C.; Broll, Valquiria; Defferrari, Marina S.; Ligabue-Braun, Rodrigo; et al.; Soybean ubiquitous urease with purification facilitator: An addition to the moonlighting studies toolbox; Elsevier; Process Biochemistry; 53; 2-2017; 245-2581359-5113CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1359511316310352info:eu-repo/semantics/altIdentifier/doi/10.1016/j.procbio.2016.12.003info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:14:49Zoai:ri.conicet.gov.ar:11336/55116instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:14:49.734CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Soybean ubiquitous urease with purification facilitator: An addition to the moonlighting studies toolbox
title Soybean ubiquitous urease with purification facilitator: An addition to the moonlighting studies toolbox
spellingShingle Soybean ubiquitous urease with purification facilitator: An addition to the moonlighting studies toolbox
Martinelli, Anne H.S.
ANTIFUNGAL ACTIVITY
FUNGAL PIGMENTS
INSECTICIDAL ACTIVITY
PRODUCTION OPTIMIZATION
SOYBEAN
UBIQUITOUS UREASE
title_short Soybean ubiquitous urease with purification facilitator: An addition to the moonlighting studies toolbox
title_full Soybean ubiquitous urease with purification facilitator: An addition to the moonlighting studies toolbox
title_fullStr Soybean ubiquitous urease with purification facilitator: An addition to the moonlighting studies toolbox
title_full_unstemmed Soybean ubiquitous urease with purification facilitator: An addition to the moonlighting studies toolbox
title_sort Soybean ubiquitous urease with purification facilitator: An addition to the moonlighting studies toolbox
dc.creator.none.fl_str_mv Martinelli, Anne H.S.
Lopes, Fernanda C.
Broll, Valquiria
Defferrari, Marina S.
Ligabue-Braun, Rodrigo
Kappaun, Karine
Tichota, Deise M.
Fruttero, Leonardo Luis
Moyetta, Natalia Rita
Demartini, Diogo R.
Postal, Melissa
Medeiros-Silva, Monica
Becker-Ritt, Arlete Beatriz
Pasquali, Giancarlo
Carlini, Célia Regina R S
author Martinelli, Anne H.S.
author_facet Martinelli, Anne H.S.
Lopes, Fernanda C.
Broll, Valquiria
Defferrari, Marina S.
Ligabue-Braun, Rodrigo
Kappaun, Karine
Tichota, Deise M.
Fruttero, Leonardo Luis
Moyetta, Natalia Rita
Demartini, Diogo R.
Postal, Melissa
Medeiros-Silva, Monica
Becker-Ritt, Arlete Beatriz
Pasquali, Giancarlo
Carlini, Célia Regina R S
author_role author
author2 Lopes, Fernanda C.
Broll, Valquiria
Defferrari, Marina S.
Ligabue-Braun, Rodrigo
Kappaun, Karine
Tichota, Deise M.
Fruttero, Leonardo Luis
Moyetta, Natalia Rita
Demartini, Diogo R.
Postal, Melissa
Medeiros-Silva, Monica
Becker-Ritt, Arlete Beatriz
Pasquali, Giancarlo
Carlini, Célia Regina R S
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv ANTIFUNGAL ACTIVITY
FUNGAL PIGMENTS
INSECTICIDAL ACTIVITY
PRODUCTION OPTIMIZATION
SOYBEAN
UBIQUITOUS UREASE
topic ANTIFUNGAL ACTIVITY
FUNGAL PIGMENTS
INSECTICIDAL ACTIVITY
PRODUCTION OPTIMIZATION
SOYBEAN
UBIQUITOUS UREASE
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Ureases are nickel-dependent enzymes that catalyze the hydrolysis of urea to ammonia and carbon dioxide. In soybean (Glycine max), the embryo-specific urease (eSBU), the ubiquitous urease (uSBU), and a third isoform (SBU-III) are synthesized. Our group has previously demonstrated that eSBU, purified from seeds, has antifungal properties against phytopathogenic fungi, entomotoxicity against Dysdercus peruvianus, the ability to induce blood platelet aggregation, and these properties are independent of its enzymatic activity. Here we describe the biological properties of apo-uSBU fused to glutathione S-transferase (GST) produced in Escherichia coli. Removal of GST affected apo-uSBU stability. We performed a Response Surface Methodology to optimize GST-uSBU production to 5 mg per liter and then bioassays were carried out. The recombinant protein exhibited inhibitory effects on filamentous fungi and affected fungal secondary metabolism. Candida albicans and C. tropicalis were also susceptible to GST-uSBU and formed pseudo-hyphae. The fusion protein was toxic against Rhodnius prolixus, with the toxicity being accompanied by in vivo and in vitro hemocyte aggregation. Rabbit platelet also aggregated in the presence of GST-uSBU. Thus, uSBU displayed similar biological properties as previously described for eSBU even when fused to GST, reinforcing the proposed role of ureases in plant defense.
Fil: Martinelli, Anne H.S.. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Lopes, Fernanda C.. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Broll, Valquiria. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Defferrari, Marina S.. University of Toronto; Canadá
Fil: Ligabue-Braun, Rodrigo. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Kappaun, Karine. Pontificia Universidade Católica do Rio Grande do Sul; Brasil
Fil: Tichota, Deise M.. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Fruttero, Leonardo Luis. Pontificia Universidade Católica do Rio Grande do Sul; Brasil. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
Fil: Moyetta, Natalia Rita. Pontificia Universidade Católica do Rio Grande do Sul; Brasil. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
Fil: Demartini, Diogo R.. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Postal, Melissa. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Medeiros-Silva, Monica. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Becker-Ritt, Arlete Beatriz. Universidade Luterana Do Brasil; Brasil
Fil: Pasquali, Giancarlo. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Carlini, Célia Regina R S. Pontificia Universidade Católica do Rio Grande do Sul; Brasil
description Ureases are nickel-dependent enzymes that catalyze the hydrolysis of urea to ammonia and carbon dioxide. In soybean (Glycine max), the embryo-specific urease (eSBU), the ubiquitous urease (uSBU), and a third isoform (SBU-III) are synthesized. Our group has previously demonstrated that eSBU, purified from seeds, has antifungal properties against phytopathogenic fungi, entomotoxicity against Dysdercus peruvianus, the ability to induce blood platelet aggregation, and these properties are independent of its enzymatic activity. Here we describe the biological properties of apo-uSBU fused to glutathione S-transferase (GST) produced in Escherichia coli. Removal of GST affected apo-uSBU stability. We performed a Response Surface Methodology to optimize GST-uSBU production to 5 mg per liter and then bioassays were carried out. The recombinant protein exhibited inhibitory effects on filamentous fungi and affected fungal secondary metabolism. Candida albicans and C. tropicalis were also susceptible to GST-uSBU and formed pseudo-hyphae. The fusion protein was toxic against Rhodnius prolixus, with the toxicity being accompanied by in vivo and in vitro hemocyte aggregation. Rabbit platelet also aggregated in the presence of GST-uSBU. Thus, uSBU displayed similar biological properties as previously described for eSBU even when fused to GST, reinforcing the proposed role of ureases in plant defense.
publishDate 2017
dc.date.none.fl_str_mv 2017-02
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/11336/55116
Martinelli, Anne H.S.; Lopes, Fernanda C.; Broll, Valquiria; Defferrari, Marina S.; Ligabue-Braun, Rodrigo; et al.; Soybean ubiquitous urease with purification facilitator: An addition to the moonlighting studies toolbox; Elsevier; Process Biochemistry; 53; 2-2017; 245-258
1359-5113
CONICET Digital
CONICET
url http://hdl.handle.net/11336/55116
identifier_str_mv Martinelli, Anne H.S.; Lopes, Fernanda C.; Broll, Valquiria; Defferrari, Marina S.; Ligabue-Braun, Rodrigo; et al.; Soybean ubiquitous urease with purification facilitator: An addition to the moonlighting studies toolbox; Elsevier; Process Biochemistry; 53; 2-2017; 245-258
1359-5113
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1359511316310352
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.procbio.2016.12.003
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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