Antifungal activity of the ribosome-inactivating protein BE27 from sugar beet (Beta vulgaris L.) against the green mould Penicillium digitatum

Autores
Citores, Lucía; Iglesias, Rosario; Gay, Claudia Carolina; Ferreras, José Miguel
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The ribosome-inactivating protein BE27 from sugar beet (Betavulgaris L.) leaves is an apoplastic protein induced by signallingcompounds, such as hydrogen peroxide and salicylic acid, whichhas been reported to be involved in defence against viruses. Here,we report that, at a concentration much lower than that present inthe apoplast, BE27 displays antifungal activity against the greenmould Penicillium digitatum, a necrotrophic fungus that colonizeswounds and grows in the inter- and intracellular spaces of thetissues of several edible plants. BE27 is able to enter into thecytosol and kill fungal cells, thus arresting the growth of thefungus. The mechanism of action seems to involve ribosomal RNA(rRNA) N-glycosylase activity on the sarcin?ricin loop of the majorrRNA which inactivates irreversibly the fungal ribosomes, thusinhibiting protein synthesis. We compared the C-terminus of theBE27 structure with antifungal plant defensins and hypothesizethat a structural motif composed of an α-helix and a β-hairpin,similar to the γ-core motif of defensins, might contribute to thespecific interaction with the fungal plasma membranes, allowingthe protein to enter into the cell.
Fil: Citores, Lucía. Universidad de Valladolid. Facultad de Ciencias; España
Fil: Iglesias, Rosario. Universidad de Valladolid. Facultad de Ciencias; España
Fil: Gay, Claudia Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; Argentina
Fil: Ferreras, José Miguel. Universidad de Valladolid. Facultad de Ciencias; España
Materia
Apoplast
Defensin
Green Mould
Plant Defence
Pokeweed Antiviral Protein
Polynucleotide:Adenosine Glycosylase
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:11336/41157
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/41157
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Antifungal activity of the ribosome-inactivating protein BE27 from sugar beet (Beta vulgaris L.) against the green mould Penicillium digitatumCitores, LucíaIglesias, RosarioGay, Claudia CarolinaFerreras, José MiguelApoplastDefensinGreen MouldPlant DefencePokeweed Antiviral ProteinPolynucleotide:Adenosine Glycosylasehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The ribosome-inactivating protein BE27 from sugar beet (Betavulgaris L.) leaves is an apoplastic protein induced by signallingcompounds, such as hydrogen peroxide and salicylic acid, whichhas been reported to be involved in defence against viruses. Here,we report that, at a concentration much lower than that present inthe apoplast, BE27 displays antifungal activity against the greenmould Penicillium digitatum, a necrotrophic fungus that colonizeswounds and grows in the inter- and intracellular spaces of thetissues of several edible plants. BE27 is able to enter into thecytosol and kill fungal cells, thus arresting the growth of thefungus. The mechanism of action seems to involve ribosomal RNA(rRNA) N-glycosylase activity on the sarcin?ricin loop of the majorrRNA which inactivates irreversibly the fungal ribosomes, thusinhibiting protein synthesis. We compared the C-terminus of theBE27 structure with antifungal plant defensins and hypothesizethat a structural motif composed of an α-helix and a β-hairpin,similar to the γ-core motif of defensins, might contribute to thespecific interaction with the fungal plasma membranes, allowingthe protein to enter into the cell.Fil: Citores, Lucía. Universidad de Valladolid. Facultad de Ciencias; EspañaFil: Iglesias, Rosario. Universidad de Valladolid. Facultad de Ciencias; EspañaFil: Gay, Claudia Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; ArgentinaFil: Ferreras, José Miguel. Universidad de Valladolid. Facultad de Ciencias; EspañaWiley-Blackwell2016-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/41157Citores, Lucía; Iglesias, Rosario; Gay, Claudia Carolina; Ferreras, José Miguel; Antifungal activity of the ribosome-inactivating protein BE27 from sugar beet (Beta vulgaris L.) against the green mould Penicillium digitatum; Wiley-Blackwell; Molecular Plant Pathology; 17; 2; 2-2016; 261-2711464-67221364-3703CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1111/mpp.12278info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1111/mpp.12278info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:26:54Zoai:ri.conicet.gov.ar:11336/41157instacron: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:34982025-10-15 14:26:54.661CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Antifungal activity of the ribosome-inactivating protein BE27 from sugar beet (Beta vulgaris L.) against the green mould Penicillium digitatum
title Antifungal activity of the ribosome-inactivating protein BE27 from sugar beet (Beta vulgaris L.) against the green mould Penicillium digitatum
spellingShingle Antifungal activity of the ribosome-inactivating protein BE27 from sugar beet (Beta vulgaris L.) against the green mould Penicillium digitatum
Citores, Lucía
Apoplast
Defensin
Green Mould
Plant Defence
Pokeweed Antiviral Protein
Polynucleotide:Adenosine Glycosylase
title_short Antifungal activity of the ribosome-inactivating protein BE27 from sugar beet (Beta vulgaris L.) against the green mould Penicillium digitatum
title_full Antifungal activity of the ribosome-inactivating protein BE27 from sugar beet (Beta vulgaris L.) against the green mould Penicillium digitatum
title_fullStr Antifungal activity of the ribosome-inactivating protein BE27 from sugar beet (Beta vulgaris L.) against the green mould Penicillium digitatum
title_full_unstemmed Antifungal activity of the ribosome-inactivating protein BE27 from sugar beet (Beta vulgaris L.) against the green mould Penicillium digitatum
title_sort Antifungal activity of the ribosome-inactivating protein BE27 from sugar beet (Beta vulgaris L.) against the green mould Penicillium digitatum
dc.creator.none.fl_str_mv Citores, Lucía
Iglesias, Rosario
Gay, Claudia Carolina
Ferreras, José Miguel
author Citores, Lucía
author_facet Citores, Lucía
Iglesias, Rosario
Gay, Claudia Carolina
Ferreras, José Miguel
author_role author
author2 Iglesias, Rosario
Gay, Claudia Carolina
Ferreras, José Miguel
author2_role author
author
author
dc.subject.none.fl_str_mv Apoplast
Defensin
Green Mould
Plant Defence
Pokeweed Antiviral Protein
Polynucleotide:Adenosine Glycosylase
topic Apoplast
Defensin
Green Mould
Plant Defence
Pokeweed Antiviral Protein
Polynucleotide:Adenosine Glycosylase
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The ribosome-inactivating protein BE27 from sugar beet (Betavulgaris L.) leaves is an apoplastic protein induced by signallingcompounds, such as hydrogen peroxide and salicylic acid, whichhas been reported to be involved in defence against viruses. Here,we report that, at a concentration much lower than that present inthe apoplast, BE27 displays antifungal activity against the greenmould Penicillium digitatum, a necrotrophic fungus that colonizeswounds and grows in the inter- and intracellular spaces of thetissues of several edible plants. BE27 is able to enter into thecytosol and kill fungal cells, thus arresting the growth of thefungus. The mechanism of action seems to involve ribosomal RNA(rRNA) N-glycosylase activity on the sarcin?ricin loop of the majorrRNA which inactivates irreversibly the fungal ribosomes, thusinhibiting protein synthesis. We compared the C-terminus of theBE27 structure with antifungal plant defensins and hypothesizethat a structural motif composed of an α-helix and a β-hairpin,similar to the γ-core motif of defensins, might contribute to thespecific interaction with the fungal plasma membranes, allowingthe protein to enter into the cell.
Fil: Citores, Lucía. Universidad de Valladolid. Facultad de Ciencias; España
Fil: Iglesias, Rosario. Universidad de Valladolid. Facultad de Ciencias; España
Fil: Gay, Claudia Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; Argentina
Fil: Ferreras, José Miguel. Universidad de Valladolid. Facultad de Ciencias; España
description The ribosome-inactivating protein BE27 from sugar beet (Betavulgaris L.) leaves is an apoplastic protein induced by signallingcompounds, such as hydrogen peroxide and salicylic acid, whichhas been reported to be involved in defence against viruses. Here,we report that, at a concentration much lower than that present inthe apoplast, BE27 displays antifungal activity against the greenmould Penicillium digitatum, a necrotrophic fungus that colonizeswounds and grows in the inter- and intracellular spaces of thetissues of several edible plants. BE27 is able to enter into thecytosol and kill fungal cells, thus arresting the growth of thefungus. The mechanism of action seems to involve ribosomal RNA(rRNA) N-glycosylase activity on the sarcin?ricin loop of the majorrRNA which inactivates irreversibly the fungal ribosomes, thusinhibiting protein synthesis. We compared the C-terminus of theBE27 structure with antifungal plant defensins and hypothesizethat a structural motif composed of an α-helix and a β-hairpin,similar to the γ-core motif of defensins, might contribute to thespecific interaction with the fungal plasma membranes, allowingthe protein to enter into the cell.
publishDate 2016
dc.date.none.fl_str_mv 2016-02
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/11336/41157
Citores, Lucía; Iglesias, Rosario; Gay, Claudia Carolina; Ferreras, José Miguel; Antifungal activity of the ribosome-inactivating protein BE27 from sugar beet (Beta vulgaris L.) against the green mould Penicillium digitatum; Wiley-Blackwell; Molecular Plant Pathology; 17; 2; 2-2016; 261-271
1464-6722
1364-3703
CONICET Digital
CONICET
url http://hdl.handle.net/11336/41157
identifier_str_mv Citores, Lucía; Iglesias, Rosario; Gay, Claudia Carolina; Ferreras, José Miguel; Antifungal activity of the ribosome-inactivating protein BE27 from sugar beet (Beta vulgaris L.) against the green mould Penicillium digitatum; Wiley-Blackwell; Molecular Plant Pathology; 17; 2; 2-2016; 261-271
1464-6722
1364-3703
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1111/mpp.12278
info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1111/mpp.12278
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 Wiley-Blackwell
publisher.none.fl_str_mv Wiley-Blackwell
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
_version_ 1846082719691309056
score 13.22299

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