Purification, cloning and characterization of fragaceatoxin C, a novel actinoporin from the sea anemone Actinia fragacea

Autores
Bellomio, Augusto; Morante, Koldo; Barlic, Ariana; Gutiérrez Aguirre, Ion; Viguera, Ana Rosa; Gonzalez Mañas, Juan Manuel
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Actinia fragacea is commonly called the "strawberry" anemone because of the distinctive yellow or green spots displayed on its red column. Its venom contains several haemolytic proteins with a molecular mass of ∼20 kDa that can be separated by ion-exchange column chromatography. One of them was purified to homogeneity and was named fragaceatoxin C (FraC). Its 15 N-terminal residues were identified by Edman degradation and served to obtain its complete DNA coding sequence by RT-PCR. The coding region of FraC was amplified and cloned in the expression vector pBAT-4. Purified recombinant FraC consists of 179 amino acids and multiple sequence alignment with other actinoporins clearly indicates that FraC belongs to this protein family. The secondary structure, thermal stability and lytic activity of native and recombinant FraC were practically identical and exhibit the same basic features already described for equinatoxin-II and sticholysin-II. © 2009 Elsevier Ltd. All rights reserved.
Fil: Bellomio, Augusto. Universidad del País Vasco; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Morante, Koldo. Universidad del País Vasco; España
Fil: Barlic, Ariana. Universidad del País Vasco; España
Fil: Gutiérrez Aguirre, Ion. Universidad del País Vasco; España
Fil: Viguera, Ana Rosa. Universidad del País Vasco; España
Fil: Gonzalez Mañas, Juan Manuel. Universidad del País Vasco; España
Materia
Actinoporins
Fragaceatoxin C
Lipid-Protein Interactions
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:11336/66047
Acceder
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network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling Purification, cloning and characterization of fragaceatoxin C, a novel actinoporin from the sea anemone Actinia fragaceaBellomio, AugustoMorante, KoldoBarlic, ArianaGutiérrez Aguirre, IonViguera, Ana RosaGonzalez Mañas, Juan ManuelActinoporinsFragaceatoxin CLipid-Protein Interactionshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Actinia fragacea is commonly called the "strawberry" anemone because of the distinctive yellow or green spots displayed on its red column. Its venom contains several haemolytic proteins with a molecular mass of ∼20 kDa that can be separated by ion-exchange column chromatography. One of them was purified to homogeneity and was named fragaceatoxin C (FraC). Its 15 N-terminal residues were identified by Edman degradation and served to obtain its complete DNA coding sequence by RT-PCR. The coding region of FraC was amplified and cloned in the expression vector pBAT-4. Purified recombinant FraC consists of 179 amino acids and multiple sequence alignment with other actinoporins clearly indicates that FraC belongs to this protein family. The secondary structure, thermal stability and lytic activity of native and recombinant FraC were practically identical and exhibit the same basic features already described for equinatoxin-II and sticholysin-II. © 2009 Elsevier Ltd. All rights reserved.Fil: Bellomio, Augusto. Universidad del País Vasco; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Morante, Koldo. Universidad del País Vasco; EspañaFil: Barlic, Ariana. Universidad del País Vasco; EspañaFil: Gutiérrez Aguirre, Ion. Universidad del País Vasco; EspañaFil: Viguera, Ana Rosa. Universidad del País Vasco; EspañaFil: Gonzalez Mañas, Juan Manuel. Universidad del País Vasco; EspañaPergamon-Elsevier Science Ltd2009-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/66047Bellomio, Augusto; Morante, Koldo; Barlic, Ariana; Gutiérrez Aguirre, Ion; Viguera, Ana Rosa; et al.; Purification, cloning and characterization of fragaceatoxin C, a novel actinoporin from the sea anemone Actinia fragacea; Pergamon-Elsevier Science Ltd; Toxicon; 54; 6; 11-2009; 869-8800041-0101CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.toxicon.2009.06.022info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0041010109003298info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-12-23T14:03:45Zoai:ri.conicet.gov.ar:11336/66047instacron: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:34982025-12-23 14:03:46.009CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Purification, cloning and characterization of fragaceatoxin C, a novel actinoporin from the sea anemone Actinia fragacea
title Purification, cloning and characterization of fragaceatoxin C, a novel actinoporin from the sea anemone Actinia fragacea
spellingShingle Purification, cloning and characterization of fragaceatoxin C, a novel actinoporin from the sea anemone Actinia fragacea
Bellomio, Augusto
Actinoporins
Fragaceatoxin C
Lipid-Protein Interactions
title_short Purification, cloning and characterization of fragaceatoxin C, a novel actinoporin from the sea anemone Actinia fragacea
title_full Purification, cloning and characterization of fragaceatoxin C, a novel actinoporin from the sea anemone Actinia fragacea
title_fullStr Purification, cloning and characterization of fragaceatoxin C, a novel actinoporin from the sea anemone Actinia fragacea
title_full_unstemmed Purification, cloning and characterization of fragaceatoxin C, a novel actinoporin from the sea anemone Actinia fragacea
title_sort Purification, cloning and characterization of fragaceatoxin C, a novel actinoporin from the sea anemone Actinia fragacea
dc.creator.none.fl_str_mv Bellomio, Augusto
Morante, Koldo
Barlic, Ariana
Gutiérrez Aguirre, Ion
Viguera, Ana Rosa
Gonzalez Mañas, Juan Manuel
author Bellomio, Augusto
author_facet Bellomio, Augusto
Morante, Koldo
Barlic, Ariana
Gutiérrez Aguirre, Ion
Viguera, Ana Rosa
Gonzalez Mañas, Juan Manuel
author_role author
author2 Morante, Koldo
Barlic, Ariana
Gutiérrez Aguirre, Ion
Viguera, Ana Rosa
Gonzalez Mañas, Juan Manuel
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Actinoporins
Fragaceatoxin C
Lipid-Protein Interactions
topic Actinoporins
Fragaceatoxin C
Lipid-Protein Interactions
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Actinia fragacea is commonly called the "strawberry" anemone because of the distinctive yellow or green spots displayed on its red column. Its venom contains several haemolytic proteins with a molecular mass of ∼20 kDa that can be separated by ion-exchange column chromatography. One of them was purified to homogeneity and was named fragaceatoxin C (FraC). Its 15 N-terminal residues were identified by Edman degradation and served to obtain its complete DNA coding sequence by RT-PCR. The coding region of FraC was amplified and cloned in the expression vector pBAT-4. Purified recombinant FraC consists of 179 amino acids and multiple sequence alignment with other actinoporins clearly indicates that FraC belongs to this protein family. The secondary structure, thermal stability and lytic activity of native and recombinant FraC were practically identical and exhibit the same basic features already described for equinatoxin-II and sticholysin-II. © 2009 Elsevier Ltd. All rights reserved.
Fil: Bellomio, Augusto. Universidad del País Vasco; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Morante, Koldo. Universidad del País Vasco; España
Fil: Barlic, Ariana. Universidad del País Vasco; España
Fil: Gutiérrez Aguirre, Ion. Universidad del País Vasco; España
Fil: Viguera, Ana Rosa. Universidad del País Vasco; España
Fil: Gonzalez Mañas, Juan Manuel. Universidad del País Vasco; España
description Actinia fragacea is commonly called the "strawberry" anemone because of the distinctive yellow or green spots displayed on its red column. Its venom contains several haemolytic proteins with a molecular mass of ∼20 kDa that can be separated by ion-exchange column chromatography. One of them was purified to homogeneity and was named fragaceatoxin C (FraC). Its 15 N-terminal residues were identified by Edman degradation and served to obtain its complete DNA coding sequence by RT-PCR. The coding region of FraC was amplified and cloned in the expression vector pBAT-4. Purified recombinant FraC consists of 179 amino acids and multiple sequence alignment with other actinoporins clearly indicates that FraC belongs to this protein family. The secondary structure, thermal stability and lytic activity of native and recombinant FraC were practically identical and exhibit the same basic features already described for equinatoxin-II and sticholysin-II. © 2009 Elsevier Ltd. All rights reserved.
publishDate 2009
dc.date.none.fl_str_mv 2009-11
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/11336/66047
Bellomio, Augusto; Morante, Koldo; Barlic, Ariana; Gutiérrez Aguirre, Ion; Viguera, Ana Rosa; et al.; Purification, cloning and characterization of fragaceatoxin C, a novel actinoporin from the sea anemone Actinia fragacea; Pergamon-Elsevier Science Ltd; Toxicon; 54; 6; 11-2009; 869-880
0041-0101
CONICET Digital
CONICET
url http://hdl.handle.net/11336/66047
identifier_str_mv Bellomio, Augusto; Morante, Koldo; Barlic, Ariana; Gutiérrez Aguirre, Ion; Viguera, Ana Rosa; et al.; Purification, cloning and characterization of fragaceatoxin C, a novel actinoporin from the sea anemone Actinia fragacea; Pergamon-Elsevier Science Ltd; Toxicon; 54; 6; 11-2009; 869-880
0041-0101
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.toxicon.2009.06.022
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0041010109003298
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 Pergamon-Elsevier Science Ltd
publisher.none.fl_str_mv Pergamon-Elsevier Science Ltd
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 12.952241

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