Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formation

Autores
Valle, Aisel; Pérez Socas, Luis Benito; Canet, Liem; Hervis, Yadira De La Patria; De Armas Guitart, German; Martins De Sa, Diogo; Lima, Jônatas Cunha Barbosa; Souza, Adolfo Carlos Barros; Barbosa, João Alexandre Ribeiro Gonçalves; De Freitas, Sonia Maria; Pazos, Isabel Fabiola
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The Trp111 to Cys mutant of sticholysin I, an actinoporin from Stichodactyla helianthus sea anemone, forms a homodimer via a disulfide bridge. The purified dimer is 193 times less hemolytic than the monomer. Ultracentrifugation, dynamic light scattering and size-exclusion chromatography demonstrate that monomers and dimers are the only independent oligomeric states encountered. Indeed, circular dichroism and fluorescence spectroscopies showed that Trp/Tyr residues participate in homodimerization and that the dimer is less thermostable than the monomer. A homodimer three-dimensional model was constructed and indicates that Trp147/Tyr137 are at the homodimer interface. Spectroscopy results validated the 3D-model and assigned 85° to the disulfide bridge dihedral angle responsible for dimerization. The homodimer model suggests that alterations in the membrane/carbohydrate-binding sites in one of the monomers, as result of dimerization, could explain the decrease in the homodimer ability to form pores.
Fil: Valle, Aisel. Universidad de La Habana; Cuba
Fil: Pérez Socas, Luis Benito. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Física de Buenos Aires. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Física de Buenos Aires; Argentina. Universidad de La Habana; Cuba
Fil: Canet, Liem. Universidad de La Habana; Cuba
Fil: Hervis, Yadira De La Patria. Universidad de La Habana; Cuba
Fil: De Armas Guitart, German. Universidad de La Habana; Cuba
Fil: Martins De Sa, Diogo. Universidade do Brasília; Brasil
Fil: Lima, Jônatas Cunha Barbosa. Universidade do Brasília; Brasil
Fil: Souza, Adolfo Carlos Barros. Universidade do Brasília; Brasil
Fil: Barbosa, João Alexandre Ribeiro Gonçalves. Universidade do Brasília; Brasil
Fil: De Freitas, Sonia Maria. Universidade do Brasília; Brasil
Fil: Pazos, Isabel Fabiola. Universidad de La Habana; Cuba
Materia
Pore-formin toxin
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:11336/97226
Acceder
id CONICETDig_db381a6265d5327e987982f9b3b20450
oai_identifier_str oai:ri.conicet.gov.ar:11336/97226
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formationValle, AiselPérez Socas, Luis BenitoCanet, LiemHervis, Yadira De La PatriaDe Armas Guitart, GermanMartins De Sa, DiogoLima, Jônatas Cunha BarbosaSouza, Adolfo Carlos BarrosBarbosa, João Alexandre Ribeiro GonçalvesDe Freitas, Sonia MariaPazos, Isabel FabiolaPore-formin toxinhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The Trp111 to Cys mutant of sticholysin I, an actinoporin from Stichodactyla helianthus sea anemone, forms a homodimer via a disulfide bridge. The purified dimer is 193 times less hemolytic than the monomer. Ultracentrifugation, dynamic light scattering and size-exclusion chromatography demonstrate that monomers and dimers are the only independent oligomeric states encountered. Indeed, circular dichroism and fluorescence spectroscopies showed that Trp/Tyr residues participate in homodimerization and that the dimer is less thermostable than the monomer. A homodimer three-dimensional model was constructed and indicates that Trp147/Tyr137 are at the homodimer interface. Spectroscopy results validated the 3D-model and assigned 85° to the disulfide bridge dihedral angle responsible for dimerization. The homodimer model suggests that alterations in the membrane/carbohydrate-binding sites in one of the monomers, as result of dimerization, could explain the decrease in the homodimer ability to form pores.Fil: Valle, Aisel. Universidad de La Habana; CubaFil: Pérez Socas, Luis Benito. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Física de Buenos Aires. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Física de Buenos Aires; Argentina. Universidad de La Habana; CubaFil: Canet, Liem. Universidad de La Habana; CubaFil: Hervis, Yadira De La Patria. Universidad de La Habana; CubaFil: De Armas Guitart, German. Universidad de La Habana; CubaFil: Martins De Sa, Diogo. Universidade do Brasília; BrasilFil: Lima, Jônatas Cunha Barbosa. Universidade do Brasília; BrasilFil: Souza, Adolfo Carlos Barros. Universidade do Brasília; BrasilFil: Barbosa, João Alexandre Ribeiro Gonçalves. Universidade do Brasília; BrasilFil: De Freitas, Sonia Maria. Universidade do Brasília; BrasilFil: Pazos, Isabel Fabiola. Universidad de La Habana; CubaNature Publishing Group2018-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/97226Valle, Aisel; Pérez Socas, Luis Benito; Canet, Liem; Hervis, Yadira De La Patria; De Armas Guitart, German; et al.; Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formation; Nature Publishing Group; Scientific Reports; 8; 1; 12-20182045-2322CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.nature.com/articles/s41598-018-24688-2info:eu-repo/semantics/altIdentifier/doi/10.1038/s41598-018-24688-2info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:27:15Zoai:ri.conicet.gov.ar:11336/97226instacron: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:34982025-09-29 10:27:15.316CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formation
title Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formation
spellingShingle Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formation
Valle, Aisel
Pore-formin toxin
title_short Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formation
title_full Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formation
title_fullStr Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formation
title_full_unstemmed Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formation
title_sort Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formation
dc.creator.none.fl_str_mv Valle, Aisel
Pérez Socas, Luis Benito
Canet, Liem
Hervis, Yadira De La Patria
De Armas Guitart, German
Martins De Sa, Diogo
Lima, Jônatas Cunha Barbosa
Souza, Adolfo Carlos Barros
Barbosa, João Alexandre Ribeiro Gonçalves
De Freitas, Sonia Maria
Pazos, Isabel Fabiola
author Valle, Aisel
author_facet Valle, Aisel
Pérez Socas, Luis Benito
Canet, Liem
Hervis, Yadira De La Patria
De Armas Guitart, German
Martins De Sa, Diogo
Lima, Jônatas Cunha Barbosa
Souza, Adolfo Carlos Barros
Barbosa, João Alexandre Ribeiro Gonçalves
De Freitas, Sonia Maria
Pazos, Isabel Fabiola
author_role author
author2 Pérez Socas, Luis Benito
Canet, Liem
Hervis, Yadira De La Patria
De Armas Guitart, German
Martins De Sa, Diogo
Lima, Jônatas Cunha Barbosa
Souza, Adolfo Carlos Barros
Barbosa, João Alexandre Ribeiro Gonçalves
De Freitas, Sonia Maria
Pazos, Isabel Fabiola
author2_role author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Pore-formin toxin
topic Pore-formin 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 The Trp111 to Cys mutant of sticholysin I, an actinoporin from Stichodactyla helianthus sea anemone, forms a homodimer via a disulfide bridge. The purified dimer is 193 times less hemolytic than the monomer. Ultracentrifugation, dynamic light scattering and size-exclusion chromatography demonstrate that monomers and dimers are the only independent oligomeric states encountered. Indeed, circular dichroism and fluorescence spectroscopies showed that Trp/Tyr residues participate in homodimerization and that the dimer is less thermostable than the monomer. A homodimer three-dimensional model was constructed and indicates that Trp147/Tyr137 are at the homodimer interface. Spectroscopy results validated the 3D-model and assigned 85° to the disulfide bridge dihedral angle responsible for dimerization. The homodimer model suggests that alterations in the membrane/carbohydrate-binding sites in one of the monomers, as result of dimerization, could explain the decrease in the homodimer ability to form pores.
Fil: Valle, Aisel. Universidad de La Habana; Cuba
Fil: Pérez Socas, Luis Benito. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Física de Buenos Aires. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Física de Buenos Aires; Argentina. Universidad de La Habana; Cuba
Fil: Canet, Liem. Universidad de La Habana; Cuba
Fil: Hervis, Yadira De La Patria. Universidad de La Habana; Cuba
Fil: De Armas Guitart, German. Universidad de La Habana; Cuba
Fil: Martins De Sa, Diogo. Universidade do Brasília; Brasil
Fil: Lima, Jônatas Cunha Barbosa. Universidade do Brasília; Brasil
Fil: Souza, Adolfo Carlos Barros. Universidade do Brasília; Brasil
Fil: Barbosa, João Alexandre Ribeiro Gonçalves. Universidade do Brasília; Brasil
Fil: De Freitas, Sonia Maria. Universidade do Brasília; Brasil
Fil: Pazos, Isabel Fabiola. Universidad de La Habana; Cuba
description The Trp111 to Cys mutant of sticholysin I, an actinoporin from Stichodactyla helianthus sea anemone, forms a homodimer via a disulfide bridge. The purified dimer is 193 times less hemolytic than the monomer. Ultracentrifugation, dynamic light scattering and size-exclusion chromatography demonstrate that monomers and dimers are the only independent oligomeric states encountered. Indeed, circular dichroism and fluorescence spectroscopies showed that Trp/Tyr residues participate in homodimerization and that the dimer is less thermostable than the monomer. A homodimer three-dimensional model was constructed and indicates that Trp147/Tyr137 are at the homodimer interface. Spectroscopy results validated the 3D-model and assigned 85° to the disulfide bridge dihedral angle responsible for dimerization. The homodimer model suggests that alterations in the membrane/carbohydrate-binding sites in one of the monomers, as result of dimerization, could explain the decrease in the homodimer ability to form pores.
publishDate 2018
dc.date.none.fl_str_mv 2018-12
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/11336/97226
Valle, Aisel; Pérez Socas, Luis Benito; Canet, Liem; Hervis, Yadira De La Patria; De Armas Guitart, German; et al.; Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formation; Nature Publishing Group; Scientific Reports; 8; 1; 12-2018
2045-2322
CONICET Digital
CONICET
url http://hdl.handle.net/11336/97226
identifier_str_mv Valle, Aisel; Pérez Socas, Luis Benito; Canet, Liem; Hervis, Yadira De La Patria; De Armas Guitart, German; et al.; Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formation; Nature Publishing Group; Scientific Reports; 8; 1; 12-2018
2045-2322
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.nature.com/articles/s41598-018-24688-2
info:eu-repo/semantics/altIdentifier/doi/10.1038/s41598-018-24688-2
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 Nature Publishing Group
publisher.none.fl_str_mv Nature Publishing Group
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 13.070432

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