Edodin: A New Type of Toxin from Shiitake Mushroom (Lentinula edodes) That Inactivates Mammalian Ribosomes

Autores
Citores, Lucía; Ragucci, Sara; Gay, Claudia Carolina; Russo, Rosita; Chambery, Angela; Di Maro, Antimo; Iglesias, Rosario; Ferreras, José M.
Año de publicación
2024
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Ribosome-inactivating proteins (RIPs) are a group of proteins with rRNA N-glycosylase activity that irreversibly inhibit protein synthesis and consequently cause cell death. Recently, an RIP called ledodin has been found in shiitake; it is cytotoxic, strongly inhibits protein synthesis, and shows rRNA N-glycosylase activity. In this work, we isolated and characterized a 50 kDa cytotoxic protein from shiitake that we named edodin. Edodin inhibits protein synthesis in a mammalian cell-free system, but not in insect-, yeast-, and bacteria-derived systems. It exhibits rRNA N-glycosylase and DNA-nicking activities, which relate it to plant RIPs. It was also shown to be toxic to HeLa and COLO 320 cells. Its structure is not related to other RIPs found in plants, bacteria, or fungi, but, instead, it presents the characteristic structure of the fold type I of pyridoxal phosphate-dependent enzymes. Homologous sequences have been found in other fungi of the class Agaricomycetes; thus, edodin could be a new type of toxin present in many fungi, some of them edible, which makes them of great interest in health, both for their involvement in food safety and for their potential biomedical and biotechnological applications.
Fil: Citores, Lucía. Universidad de Valladolid. Facultad de Ciencias; España
Fil: Ragucci, Sara. University Of Campania Luigi Vanvitelli; Italia
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: Russo, Rosita. University Of Campania Luigi Vanvitelli; Italia
Fil: Chambery, Angela. University Of Campania Luigi Vanvitelli; Italia
Fil: Di Maro, Antimo. University Of Campania Luigi Vanvitelli; Italia
Fil: Iglesias, Rosario. Universidad de Valladolid. Facultad de Ciencias; España
Fil: Ferreras, José M.. Universidad de Valladolid. Facultad de Ciencias; España
Materia
PROTEIN SYNTHESIS (INHIBITION)
PYRIDOXAL PHOSPHATE (PLP)
RIBOSOME-INACTIVATING PROTEIN (RIP)
RIBOTOXIN
RRNA N-GLYCOSYLASE
SHIITAKE (LENTINULA EDODES)
TOXIN
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/256995

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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Edodin: A New Type of Toxin from Shiitake Mushroom (Lentinula edodes) That Inactivates Mammalian RibosomesCitores, LucíaRagucci, SaraGay, Claudia CarolinaRusso, RositaChambery, AngelaDi Maro, AntimoIglesias, RosarioFerreras, José M.PROTEIN SYNTHESIS (INHIBITION)PYRIDOXAL PHOSPHATE (PLP)RIBOSOME-INACTIVATING PROTEIN (RIP)RIBOTOXINRRNA N-GLYCOSYLASESHIITAKE (LENTINULA EDODES)TOXINhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Ribosome-inactivating proteins (RIPs) are a group of proteins with rRNA N-glycosylase activity that irreversibly inhibit protein synthesis and consequently cause cell death. Recently, an RIP called ledodin has been found in shiitake; it is cytotoxic, strongly inhibits protein synthesis, and shows rRNA N-glycosylase activity. In this work, we isolated and characterized a 50 kDa cytotoxic protein from shiitake that we named edodin. Edodin inhibits protein synthesis in a mammalian cell-free system, but not in insect-, yeast-, and bacteria-derived systems. It exhibits rRNA N-glycosylase and DNA-nicking activities, which relate it to plant RIPs. It was also shown to be toxic to HeLa and COLO 320 cells. Its structure is not related to other RIPs found in plants, bacteria, or fungi, but, instead, it presents the characteristic structure of the fold type I of pyridoxal phosphate-dependent enzymes. Homologous sequences have been found in other fungi of the class Agaricomycetes; thus, edodin could be a new type of toxin present in many fungi, some of them edible, which makes them of great interest in health, both for their involvement in food safety and for their potential biomedical and biotechnological applications.Fil: Citores, Lucía. Universidad de Valladolid. Facultad de Ciencias; EspañaFil: Ragucci, Sara. University Of Campania Luigi Vanvitelli; ItaliaFil: 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: Russo, Rosita. University Of Campania Luigi Vanvitelli; ItaliaFil: Chambery, Angela. University Of Campania Luigi Vanvitelli; ItaliaFil: Di Maro, Antimo. University Of Campania Luigi Vanvitelli; ItaliaFil: Iglesias, Rosario. Universidad de Valladolid. Facultad de Ciencias; EspañaFil: Ferreras, José M.. Universidad de Valladolid. Facultad de Ciencias; EspañaMultidisciplinary Digital Publishing Institute2024-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/256995Citores, Lucía; Ragucci, Sara; Gay, Claudia Carolina; Russo, Rosita; Chambery, Angela; et al.; Edodin: A New Type of Toxin from Shiitake Mushroom (Lentinula edodes) That Inactivates Mammalian Ribosomes; Multidisciplinary Digital Publishing Institute; Toxins; 16; 4; 4-2024; 1-172072-6651CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2072-6651/16/4/185info:eu-repo/semantics/altIdentifier/doi/10.3390/toxins16040185info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:03:00Zoai:ri.conicet.gov.ar:11336/256995instacron: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:34982025-09-03 10:03:00.941CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Edodin: A New Type of Toxin from Shiitake Mushroom (Lentinula edodes) That Inactivates Mammalian Ribosomes
title Edodin: A New Type of Toxin from Shiitake Mushroom (Lentinula edodes) That Inactivates Mammalian Ribosomes
spellingShingle Edodin: A New Type of Toxin from Shiitake Mushroom (Lentinula edodes) That Inactivates Mammalian Ribosomes
Citores, Lucía
PROTEIN SYNTHESIS (INHIBITION)
PYRIDOXAL PHOSPHATE (PLP)
RIBOSOME-INACTIVATING PROTEIN (RIP)
RIBOTOXIN
RRNA N-GLYCOSYLASE
SHIITAKE (LENTINULA EDODES)
TOXIN
title_short Edodin: A New Type of Toxin from Shiitake Mushroom (Lentinula edodes) That Inactivates Mammalian Ribosomes
title_full Edodin: A New Type of Toxin from Shiitake Mushroom (Lentinula edodes) That Inactivates Mammalian Ribosomes
title_fullStr Edodin: A New Type of Toxin from Shiitake Mushroom (Lentinula edodes) That Inactivates Mammalian Ribosomes
title_full_unstemmed Edodin: A New Type of Toxin from Shiitake Mushroom (Lentinula edodes) That Inactivates Mammalian Ribosomes
title_sort Edodin: A New Type of Toxin from Shiitake Mushroom (Lentinula edodes) That Inactivates Mammalian Ribosomes
dc.creator.none.fl_str_mv Citores, Lucía
Ragucci, Sara
Gay, Claudia Carolina
Russo, Rosita
Chambery, Angela
Di Maro, Antimo
Iglesias, Rosario
Ferreras, José M.
author Citores, Lucía
author_facet Citores, Lucía
Ragucci, Sara
Gay, Claudia Carolina
Russo, Rosita
Chambery, Angela
Di Maro, Antimo
Iglesias, Rosario
Ferreras, José M.
author_role author
author2 Ragucci, Sara
Gay, Claudia Carolina
Russo, Rosita
Chambery, Angela
Di Maro, Antimo
Iglesias, Rosario
Ferreras, José M.
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv PROTEIN SYNTHESIS (INHIBITION)
PYRIDOXAL PHOSPHATE (PLP)
RIBOSOME-INACTIVATING PROTEIN (RIP)
RIBOTOXIN
RRNA N-GLYCOSYLASE
SHIITAKE (LENTINULA EDODES)
TOXIN
topic PROTEIN SYNTHESIS (INHIBITION)
PYRIDOXAL PHOSPHATE (PLP)
RIBOSOME-INACTIVATING PROTEIN (RIP)
RIBOTOXIN
RRNA N-GLYCOSYLASE
SHIITAKE (LENTINULA EDODES)
TOXIN
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Ribosome-inactivating proteins (RIPs) are a group of proteins with rRNA N-glycosylase activity that irreversibly inhibit protein synthesis and consequently cause cell death. Recently, an RIP called ledodin has been found in shiitake; it is cytotoxic, strongly inhibits protein synthesis, and shows rRNA N-glycosylase activity. In this work, we isolated and characterized a 50 kDa cytotoxic protein from shiitake that we named edodin. Edodin inhibits protein synthesis in a mammalian cell-free system, but not in insect-, yeast-, and bacteria-derived systems. It exhibits rRNA N-glycosylase and DNA-nicking activities, which relate it to plant RIPs. It was also shown to be toxic to HeLa and COLO 320 cells. Its structure is not related to other RIPs found in plants, bacteria, or fungi, but, instead, it presents the characteristic structure of the fold type I of pyridoxal phosphate-dependent enzymes. Homologous sequences have been found in other fungi of the class Agaricomycetes; thus, edodin could be a new type of toxin present in many fungi, some of them edible, which makes them of great interest in health, both for their involvement in food safety and for their potential biomedical and biotechnological applications.
Fil: Citores, Lucía. Universidad de Valladolid. Facultad de Ciencias; España
Fil: Ragucci, Sara. University Of Campania Luigi Vanvitelli; Italia
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: Russo, Rosita. University Of Campania Luigi Vanvitelli; Italia
Fil: Chambery, Angela. University Of Campania Luigi Vanvitelli; Italia
Fil: Di Maro, Antimo. University Of Campania Luigi Vanvitelli; Italia
Fil: Iglesias, Rosario. Universidad de Valladolid. Facultad de Ciencias; España
Fil: Ferreras, José M.. Universidad de Valladolid. Facultad de Ciencias; España
description Ribosome-inactivating proteins (RIPs) are a group of proteins with rRNA N-glycosylase activity that irreversibly inhibit protein synthesis and consequently cause cell death. Recently, an RIP called ledodin has been found in shiitake; it is cytotoxic, strongly inhibits protein synthesis, and shows rRNA N-glycosylase activity. In this work, we isolated and characterized a 50 kDa cytotoxic protein from shiitake that we named edodin. Edodin inhibits protein synthesis in a mammalian cell-free system, but not in insect-, yeast-, and bacteria-derived systems. It exhibits rRNA N-glycosylase and DNA-nicking activities, which relate it to plant RIPs. It was also shown to be toxic to HeLa and COLO 320 cells. Its structure is not related to other RIPs found in plants, bacteria, or fungi, but, instead, it presents the characteristic structure of the fold type I of pyridoxal phosphate-dependent enzymes. Homologous sequences have been found in other fungi of the class Agaricomycetes; thus, edodin could be a new type of toxin present in many fungi, some of them edible, which makes them of great interest in health, both for their involvement in food safety and for their potential biomedical and biotechnological applications.
publishDate 2024
dc.date.none.fl_str_mv 2024-04
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/11336/256995
Citores, Lucía; Ragucci, Sara; Gay, Claudia Carolina; Russo, Rosita; Chambery, Angela; et al.; Edodin: A New Type of Toxin from Shiitake Mushroom (Lentinula edodes) That Inactivates Mammalian Ribosomes; Multidisciplinary Digital Publishing Institute; Toxins; 16; 4; 4-2024; 1-17
2072-6651
CONICET Digital
CONICET
url http://hdl.handle.net/11336/256995
identifier_str_mv Citores, Lucía; Ragucci, Sara; Gay, Claudia Carolina; Russo, Rosita; Chambery, Angela; et al.; Edodin: A New Type of Toxin from Shiitake Mushroom (Lentinula edodes) That Inactivates Mammalian Ribosomes; Multidisciplinary Digital Publishing Institute; Toxins; 16; 4; 4-2024; 1-17
2072-6651
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/2072-6651/16/4/185
info:eu-repo/semantics/altIdentifier/doi/10.3390/toxins16040185
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
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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