The Isolation of new pore-forming toxins from the sea anemone actinia fragacea provides insights into the mechanisms of actinoporin evolution

Autores
Morante, Koldo; Bellomio, Augusto; Vergara, Ana Rosa; González Mañas, Juan Manuel; Tsumoto, Kouhei; Caaveiro, José M. M.
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Random mutations and selective pressure drive protein adaptation to the changing demands of the environment. As a consequence, nature favors the evolution of protein diversity. A group of proteins subject to exceptional environmental stress and known for their widespread diversity are the pore-forming hemolytic proteins from sea anemones, known as actinoporins. In this study, we identified and isolated new isoforms of actinoporins from the sea anemone Actinia fragacea (fragaceatoxins). We characterized their hemolytic activity, examined their stability and structure, and performed a comparative analysis of their primary sequence. Sequence alignment reveals that most of the variability among actinoporins is associated with non-functional residues. The differences in the thermal behavior among fragaceatoxins suggest that these variability sites contribute to changes in protein stability. In addition, the protein-protein interaction region showed a very high degree of identity (92%) within fragaceatoxins, but only 25% among all actinoporins examined, suggesting some degree of specificity at the species level. Our findings support the mechanism of evolutionary adaptation in actinoporins and reflect common pathways conducive toprotein variability.
Fil: Morante, Koldo. University of Tokyo; Japón. Universidad Politécnica de Valencia; España. Universidad del País Vasco; España
Fil: Bellomio, Augusto. 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. Universidad Politécnica de Valencia; España. Universidad del País Vasco; España
Fil: Vergara, Ana Rosa. Universidad Politécnica de Valencia; España
Fil: González Mañas, Juan Manuel. Universidad del País Vasco; España
Fil: Tsumoto, Kouhei. University of Tokyo; Japón
Fil: Caaveiro, José M. M.. University of Tokyo; Japón. Kyushu University; Japón
Materia
ACTINOPORINS
PROTEIN VARIABILITY
PROTEIN STABILITY
PROTEIN STRUCTURE
PROTEIN EVOLUTION
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:11336/121611
Acceder
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network_name_str CONICET Digital (CONICET)
spelling The Isolation of new pore-forming toxins from the sea anemone actinia fragacea provides insights into the mechanisms of actinoporin evolutionMorante, KoldoBellomio, AugustoVergara, Ana RosaGonzález Mañas, Juan ManuelTsumoto, KouheiCaaveiro, José M. M.ACTINOPORINSPROTEIN VARIABILITYPROTEIN STABILITYPROTEIN STRUCTUREPROTEIN EVOLUTIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Random mutations and selective pressure drive protein adaptation to the changing demands of the environment. As a consequence, nature favors the evolution of protein diversity. A group of proteins subject to exceptional environmental stress and known for their widespread diversity are the pore-forming hemolytic proteins from sea anemones, known as actinoporins. In this study, we identified and isolated new isoforms of actinoporins from the sea anemone Actinia fragacea (fragaceatoxins). We characterized their hemolytic activity, examined their stability and structure, and performed a comparative analysis of their primary sequence. Sequence alignment reveals that most of the variability among actinoporins is associated with non-functional residues. The differences in the thermal behavior among fragaceatoxins suggest that these variability sites contribute to changes in protein stability. In addition, the protein-protein interaction region showed a very high degree of identity (92%) within fragaceatoxins, but only 25% among all actinoporins examined, suggesting some degree of specificity at the species level. Our findings support the mechanism of evolutionary adaptation in actinoporins and reflect common pathways conducive toprotein variability.Fil: Morante, Koldo. University of Tokyo; Japón. Universidad Politécnica de Valencia; España. Universidad del País Vasco; EspañaFil: Bellomio, Augusto. 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. Universidad Politécnica de Valencia; España. Universidad del País Vasco; EspañaFil: Vergara, Ana Rosa. Universidad Politécnica de Valencia; EspañaFil: González Mañas, Juan Manuel. Universidad del País Vasco; EspañaFil: Tsumoto, Kouhei. University of Tokyo; JapónFil: Caaveiro, José M. M.. University of Tokyo; Japón. Kyushu University; JapónMultidisciplinary Digital Publishing Institute2019-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/121611Morante, Koldo; Bellomio, Augusto; Vergara, Ana Rosa; González Mañas, Juan Manuel; Tsumoto, Kouhei; et al.; The Isolation of new pore-forming toxins from the sea anemone actinia fragacea provides insights into the mechanisms of actinoporin evolution; Multidisciplinary Digital Publishing Institute; Toxins; 11; 7; 7-2019; 1-18;401-4012072-66512072-6651CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.3390/toxins11070401info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2072-6651/11/7/401info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-12-23T14:04:36Zoai:ri.conicet.gov.ar:11336/121611instacron: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 14:04:36.456CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The Isolation of new pore-forming toxins from the sea anemone actinia fragacea provides insights into the mechanisms of actinoporin evolution
title The Isolation of new pore-forming toxins from the sea anemone actinia fragacea provides insights into the mechanisms of actinoporin evolution
spellingShingle The Isolation of new pore-forming toxins from the sea anemone actinia fragacea provides insights into the mechanisms of actinoporin evolution
Morante, Koldo
ACTINOPORINS
PROTEIN VARIABILITY
PROTEIN STABILITY
PROTEIN STRUCTURE
PROTEIN EVOLUTION
title_short The Isolation of new pore-forming toxins from the sea anemone actinia fragacea provides insights into the mechanisms of actinoporin evolution
title_full The Isolation of new pore-forming toxins from the sea anemone actinia fragacea provides insights into the mechanisms of actinoporin evolution
title_fullStr The Isolation of new pore-forming toxins from the sea anemone actinia fragacea provides insights into the mechanisms of actinoporin evolution
title_full_unstemmed The Isolation of new pore-forming toxins from the sea anemone actinia fragacea provides insights into the mechanisms of actinoporin evolution
title_sort The Isolation of new pore-forming toxins from the sea anemone actinia fragacea provides insights into the mechanisms of actinoporin evolution
dc.creator.none.fl_str_mv Morante, Koldo
Bellomio, Augusto
Vergara, Ana Rosa
González Mañas, Juan Manuel
Tsumoto, Kouhei
Caaveiro, José M. M.
author Morante, Koldo
author_facet Morante, Koldo
Bellomio, Augusto
Vergara, Ana Rosa
González Mañas, Juan Manuel
Tsumoto, Kouhei
Caaveiro, José M. M.
author_role author
author2 Bellomio, Augusto
Vergara, Ana Rosa
González Mañas, Juan Manuel
Tsumoto, Kouhei
Caaveiro, José M. M.
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv ACTINOPORINS
PROTEIN VARIABILITY
PROTEIN STABILITY
PROTEIN STRUCTURE
PROTEIN EVOLUTION
topic ACTINOPORINS
PROTEIN VARIABILITY
PROTEIN STABILITY
PROTEIN STRUCTURE
PROTEIN EVOLUTION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Random mutations and selective pressure drive protein adaptation to the changing demands of the environment. As a consequence, nature favors the evolution of protein diversity. A group of proteins subject to exceptional environmental stress and known for their widespread diversity are the pore-forming hemolytic proteins from sea anemones, known as actinoporins. In this study, we identified and isolated new isoforms of actinoporins from the sea anemone Actinia fragacea (fragaceatoxins). We characterized their hemolytic activity, examined their stability and structure, and performed a comparative analysis of their primary sequence. Sequence alignment reveals that most of the variability among actinoporins is associated with non-functional residues. The differences in the thermal behavior among fragaceatoxins suggest that these variability sites contribute to changes in protein stability. In addition, the protein-protein interaction region showed a very high degree of identity (92%) within fragaceatoxins, but only 25% among all actinoporins examined, suggesting some degree of specificity at the species level. Our findings support the mechanism of evolutionary adaptation in actinoporins and reflect common pathways conducive toprotein variability.
Fil: Morante, Koldo. University of Tokyo; Japón. Universidad Politécnica de Valencia; España. Universidad del País Vasco; España
Fil: Bellomio, Augusto. 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. Universidad Politécnica de Valencia; España. Universidad del País Vasco; España
Fil: Vergara, Ana Rosa. Universidad Politécnica de Valencia; España
Fil: González Mañas, Juan Manuel. Universidad del País Vasco; España
Fil: Tsumoto, Kouhei. University of Tokyo; Japón
Fil: Caaveiro, José M. M.. University of Tokyo; Japón. Kyushu University; Japón
description Random mutations and selective pressure drive protein adaptation to the changing demands of the environment. As a consequence, nature favors the evolution of protein diversity. A group of proteins subject to exceptional environmental stress and known for their widespread diversity are the pore-forming hemolytic proteins from sea anemones, known as actinoporins. In this study, we identified and isolated new isoforms of actinoporins from the sea anemone Actinia fragacea (fragaceatoxins). We characterized their hemolytic activity, examined their stability and structure, and performed a comparative analysis of their primary sequence. Sequence alignment reveals that most of the variability among actinoporins is associated with non-functional residues. The differences in the thermal behavior among fragaceatoxins suggest that these variability sites contribute to changes in protein stability. In addition, the protein-protein interaction region showed a very high degree of identity (92%) within fragaceatoxins, but only 25% among all actinoporins examined, suggesting some degree of specificity at the species level. Our findings support the mechanism of evolutionary adaptation in actinoporins and reflect common pathways conducive toprotein variability.
publishDate 2019
dc.date.none.fl_str_mv 2019-07
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/11336/121611
Morante, Koldo; Bellomio, Augusto; Vergara, Ana Rosa; González Mañas, Juan Manuel; Tsumoto, Kouhei; et al.; The Isolation of new pore-forming toxins from the sea anemone actinia fragacea provides insights into the mechanisms of actinoporin evolution; Multidisciplinary Digital Publishing Institute; Toxins; 11; 7; 7-2019; 1-18;401-401
2072-6651
2072-6651
CONICET Digital
CONICET
url http://hdl.handle.net/11336/121611
identifier_str_mv Morante, Koldo; Bellomio, Augusto; Vergara, Ana Rosa; González Mañas, Juan Manuel; Tsumoto, Kouhei; et al.; The Isolation of new pore-forming toxins from the sea anemone actinia fragacea provides insights into the mechanisms of actinoporin evolution; Multidisciplinary Digital Publishing Institute; Toxins; 11; 7; 7-2019; 1-18;401-401
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/doi/10.3390/toxins11070401
info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2072-6651/11/7/401
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
_version_ 1852335515901100032
score 12.952241

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