Structure-Function insights of Jaburetox and Soyuretox: Novel intrinsically disordered polypeptides derived from plant ureases

Autores
Grahl, Matheus V. Coste; Lopes, Fernanda Cortez; Martinelli, Anne H. Souza; Carlini, Célia Regina R. S.; Fruttero, Leonardo Luis
Año de publicación
2020
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) do not have a stable 3D structure but still have important biological activities. Jaburetox is a recombinant peptide derived from the jack bean (Canavalia ensiformis) urease and presents entomotoxic and antimicrobial actions. The structure of Jaburetox was elucidated using nuclear magnetic resonance which reveals it is an IDP with small amounts of secondary structure. Different approaches have demonstrated that Jaburetox acquires certain folding upon interaction with lipid membranes, a characteristic commonly found in other IDPs and usually important for their biological functions. Soyuretox, a recombinant peptide derived from the soybean (Glycine max) ubiquitous urease and homologous to Jaburetox, was also characterized for its biological activities and structural properties. Soyuretox is also an IDP, presenting more secondary structure in comparison with Jaburetox and similar entomotoxic and fungitoxic effects. Moreover, Soyuretox was found to be nontoxic to zebra fish, while Jaburetox was innocuous to mice and rats. This profile of toxicity affecting detrimental species without damaging mammals or the environment qualified them to be used in biotechnological applications. Both peptides were employed to develop transgenic crops and these plants were active against insects and nematodes, unveiling their immense potentiality for field applications.
Fil: Grahl, Matheus V. Coste. Pontificia Universidade Católica do Rio Grande do Sul; Brasil
Fil: Lopes, Fernanda Cortez. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Martinelli, Anne H. Souza. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Carlini, Célia Regina R. S.. Pontificia Universidade Católica do Rio Grande do Sul; Brasil
Fil: Fruttero, Leonardo Luis. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
Materia
ANTIFUNGAL ACTIVITY
BIOPESTICIDES
INSECTICIDAL ACTIVITY
MECHANISM OF ACTION
TRANSGENIC CROPS
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:11336/130528

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network_name_str CONICET Digital (CONICET)
spelling Structure-Function insights of Jaburetox and Soyuretox: Novel intrinsically disordered polypeptides derived from plant ureasesGrahl, Matheus V. CosteLopes, Fernanda CortezMartinelli, Anne H. SouzaCarlini, Célia Regina R. S.Fruttero, Leonardo LuisANTIFUNGAL ACTIVITYBIOPESTICIDESINSECTICIDAL ACTIVITYMECHANISM OF ACTIONTRANSGENIC CROPShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) do not have a stable 3D structure but still have important biological activities. Jaburetox is a recombinant peptide derived from the jack bean (Canavalia ensiformis) urease and presents entomotoxic and antimicrobial actions. The structure of Jaburetox was elucidated using nuclear magnetic resonance which reveals it is an IDP with small amounts of secondary structure. Different approaches have demonstrated that Jaburetox acquires certain folding upon interaction with lipid membranes, a characteristic commonly found in other IDPs and usually important for their biological functions. Soyuretox, a recombinant peptide derived from the soybean (Glycine max) ubiquitous urease and homologous to Jaburetox, was also characterized for its biological activities and structural properties. Soyuretox is also an IDP, presenting more secondary structure in comparison with Jaburetox and similar entomotoxic and fungitoxic effects. Moreover, Soyuretox was found to be nontoxic to zebra fish, while Jaburetox was innocuous to mice and rats. This profile of toxicity affecting detrimental species without damaging mammals or the environment qualified them to be used in biotechnological applications. Both peptides were employed to develop transgenic crops and these plants were active against insects and nematodes, unveiling their immense potentiality for field applications.Fil: Grahl, Matheus V. Coste. Pontificia Universidade Católica do Rio Grande do Sul; BrasilFil: Lopes, Fernanda Cortez. Universidade Federal do Rio Grande do Sul; BrasilFil: Martinelli, Anne H. Souza. Universidade Federal do Rio Grande do Sul; BrasilFil: Carlini, Célia Regina R. S.. Pontificia Universidade Católica do Rio Grande do Sul; BrasilFil: Fruttero, Leonardo Luis. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; ArgentinaMolecular Diversity Preservation International2020-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/130528Grahl, Matheus V. Coste; Lopes, Fernanda Cortez; Martinelli, Anne H. Souza; Carlini, Célia Regina R. S.; Fruttero, Leonardo Luis; Structure-Function insights of Jaburetox and Soyuretox: Novel intrinsically disordered polypeptides derived from plant ureases; Molecular Diversity Preservation International; Molecules; 25; 22; 11-2020; 1-241420-3049CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/1420-3049/25/22/5338info:eu-repo/semantics/altIdentifier/doi/10.3390/molecules25225338info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:52:09Zoai:ri.conicet.gov.ar:11336/130528instacron: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 09:52:09.707CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Structure-Function insights of Jaburetox and Soyuretox: Novel intrinsically disordered polypeptides derived from plant ureases
title Structure-Function insights of Jaburetox and Soyuretox: Novel intrinsically disordered polypeptides derived from plant ureases
spellingShingle Structure-Function insights of Jaburetox and Soyuretox: Novel intrinsically disordered polypeptides derived from plant ureases
Grahl, Matheus V. Coste
ANTIFUNGAL ACTIVITY
BIOPESTICIDES
INSECTICIDAL ACTIVITY
MECHANISM OF ACTION
TRANSGENIC CROPS
title_short Structure-Function insights of Jaburetox and Soyuretox: Novel intrinsically disordered polypeptides derived from plant ureases
title_full Structure-Function insights of Jaburetox and Soyuretox: Novel intrinsically disordered polypeptides derived from plant ureases
title_fullStr Structure-Function insights of Jaburetox and Soyuretox: Novel intrinsically disordered polypeptides derived from plant ureases
title_full_unstemmed Structure-Function insights of Jaburetox and Soyuretox: Novel intrinsically disordered polypeptides derived from plant ureases
title_sort Structure-Function insights of Jaburetox and Soyuretox: Novel intrinsically disordered polypeptides derived from plant ureases
dc.creator.none.fl_str_mv Grahl, Matheus V. Coste
Lopes, Fernanda Cortez
Martinelli, Anne H. Souza
Carlini, Célia Regina R. S.
Fruttero, Leonardo Luis
author Grahl, Matheus V. Coste
author_facet Grahl, Matheus V. Coste
Lopes, Fernanda Cortez
Martinelli, Anne H. Souza
Carlini, Célia Regina R. S.
Fruttero, Leonardo Luis
author_role author
author2 Lopes, Fernanda Cortez
Martinelli, Anne H. Souza
Carlini, Célia Regina R. S.
Fruttero, Leonardo Luis
author2_role author
author
author
author
dc.subject.none.fl_str_mv ANTIFUNGAL ACTIVITY
BIOPESTICIDES
INSECTICIDAL ACTIVITY
MECHANISM OF ACTION
TRANSGENIC CROPS
topic ANTIFUNGAL ACTIVITY
BIOPESTICIDES
INSECTICIDAL ACTIVITY
MECHANISM OF ACTION
TRANSGENIC CROPS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) do not have a stable 3D structure but still have important biological activities. Jaburetox is a recombinant peptide derived from the jack bean (Canavalia ensiformis) urease and presents entomotoxic and antimicrobial actions. The structure of Jaburetox was elucidated using nuclear magnetic resonance which reveals it is an IDP with small amounts of secondary structure. Different approaches have demonstrated that Jaburetox acquires certain folding upon interaction with lipid membranes, a characteristic commonly found in other IDPs and usually important for their biological functions. Soyuretox, a recombinant peptide derived from the soybean (Glycine max) ubiquitous urease and homologous to Jaburetox, was also characterized for its biological activities and structural properties. Soyuretox is also an IDP, presenting more secondary structure in comparison with Jaburetox and similar entomotoxic and fungitoxic effects. Moreover, Soyuretox was found to be nontoxic to zebra fish, while Jaburetox was innocuous to mice and rats. This profile of toxicity affecting detrimental species without damaging mammals or the environment qualified them to be used in biotechnological applications. Both peptides were employed to develop transgenic crops and these plants were active against insects and nematodes, unveiling their immense potentiality for field applications.
Fil: Grahl, Matheus V. Coste. Pontificia Universidade Católica do Rio Grande do Sul; Brasil
Fil: Lopes, Fernanda Cortez. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Martinelli, Anne H. Souza. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Carlini, Célia Regina R. S.. Pontificia Universidade Católica do Rio Grande do Sul; Brasil
Fil: Fruttero, Leonardo Luis. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
description Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) do not have a stable 3D structure but still have important biological activities. Jaburetox is a recombinant peptide derived from the jack bean (Canavalia ensiformis) urease and presents entomotoxic and antimicrobial actions. The structure of Jaburetox was elucidated using nuclear magnetic resonance which reveals it is an IDP with small amounts of secondary structure. Different approaches have demonstrated that Jaburetox acquires certain folding upon interaction with lipid membranes, a characteristic commonly found in other IDPs and usually important for their biological functions. Soyuretox, a recombinant peptide derived from the soybean (Glycine max) ubiquitous urease and homologous to Jaburetox, was also characterized for its biological activities and structural properties. Soyuretox is also an IDP, presenting more secondary structure in comparison with Jaburetox and similar entomotoxic and fungitoxic effects. Moreover, Soyuretox was found to be nontoxic to zebra fish, while Jaburetox was innocuous to mice and rats. This profile of toxicity affecting detrimental species without damaging mammals or the environment qualified them to be used in biotechnological applications. Both peptides were employed to develop transgenic crops and these plants were active against insects and nematodes, unveiling their immense potentiality for field applications.
publishDate 2020
dc.date.none.fl_str_mv 2020-11
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/11336/130528
Grahl, Matheus V. Coste; Lopes, Fernanda Cortez; Martinelli, Anne H. Souza; Carlini, Célia Regina R. S.; Fruttero, Leonardo Luis; Structure-Function insights of Jaburetox and Soyuretox: Novel intrinsically disordered polypeptides derived from plant ureases; Molecular Diversity Preservation International; Molecules; 25; 22; 11-2020; 1-24
1420-3049
CONICET Digital
CONICET
url http://hdl.handle.net/11336/130528
identifier_str_mv Grahl, Matheus V. Coste; Lopes, Fernanda Cortez; Martinelli, Anne H. Souza; Carlini, Célia Regina R. S.; Fruttero, Leonardo Luis; Structure-Function insights of Jaburetox and Soyuretox: Novel intrinsically disordered polypeptides derived from plant ureases; Molecular Diversity Preservation International; Molecules; 25; 22; 11-2020; 1-24
1420-3049
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/1420-3049/25/22/5338
info:eu-repo/semantics/altIdentifier/doi/10.3390/molecules25225338
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
dc.publisher.none.fl_str_mv Molecular Diversity Preservation International
publisher.none.fl_str_mv Molecular Diversity Preservation International
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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