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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/256995
Ver los metadatos del registro completo
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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 |
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CONICET Digital (CONICET) |
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CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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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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1842269778749685760 |
score |
13.13397 |