The Vip3Ag4 insecticidal protoxin from Bacillus thuringiensis adopts a tetrameric configuration that is maintained on proteolysis

The Vip3 proteins produced during vegetative growth by strains of the bacterium Bacillus thuringiensis show insecticidal activity against lepidopteran insects with a mechanism of action that may involve pore formation and apoptosis. These proteins are promising supplements to our arsenal of insectic...

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Autores: Palma, Leopoldo, Scott, David J., Harris, Gemma, Din, Salah-Ud, Williams, Thomas L., Roberts, Oliver J., Young, Mark T., Caballero, Primitivo, Berry, Colin
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2017
País:Argentina
Institución:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositorio:CONICET Digital (CONICET)
Idioma:inglés
OAI Identifier:oai:ri.conicet.gov.ar:11336/76942
Acceso en línea:http://hdl.handle.net/11336/76942
Access Level:acceso abierto
Palabra clave:BACILLUS THURINGIENSIS
VEGETATIVE INSECTICIDAL PROTEIN
TOXINS STRUCTURE
MODE OF ACTION
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
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spelling The Vip3Ag4 insecticidal protoxin from Bacillus thuringiensis adopts a tetrameric configuration that is maintained on proteolysisPalma, LeopoldoScott, David J.Harris, GemmaDin, Salah-UdWilliams, Thomas L.Roberts, Oliver J.Young, Mark T.Caballero, PrimitivoBerry, ColinBACILLUS THURINGIENSISVEGETATIVE INSECTICIDAL PROTEINTOXINS STRUCTUREMODE OF ACTIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The Vip3 proteins produced during vegetative growth by strains of the bacterium Bacillus thuringiensis show insecticidal activity against lepidopteran insects with a mechanism of action that may involve pore formation and apoptosis. These proteins are promising supplements to our arsenal of insecticidal proteins, but the molecular details of their activity are not understood. As a first step in the structural characterisation of these proteins, we have analysed their secondary structure and resolved the surface topology of a tetrameric complex of the Vip3Ag4 protein by transmission electron microscopy. Sites sensitive to proteolysis by trypsin are identified and the trypsin-cleaved protein appears to retain a similar structure as an octomeric complex comprising four copies each of the ~65 kDa and ~21 kDa products of proteolysis. This processed form of the toxin may represent the active toxin. The quality and monodispersity of the protein produced in this study make Vip3Ag4 a candidate for more detailed structural analysis using cryo-electron microscopy.Fil: Palma, Leopoldo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones y Transferencia de Villa María. Universidad Nacional de Villa María. Centro de Investigaciones y Transferencia de Villa María; ArgentinaFil: Scott, David J.. Science and Technology Facilities Council of Nottingham. Rutherford Appleton Laboratory; Reino Unido. University of Nottingham; Estados UnidosFil: Harris, Gemma. University of Nottingham; Estados UnidosFil: Din, Salah-Ud. Cardiff University; Reino UnidoFil: Williams, Thomas L.. Cardiff University; Reino UnidoFil: Roberts, Oliver J.. Cardiff University; Reino UnidoFil: Young, Mark T.. Cardiff University; Reino UnidoFil: Caballero, Primitivo. Universidad de Navarra; EspañaFil: Berry, Colin. Cardiff University; Reino UnidoMDPI AG2017-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/76942Palma, Leopoldo; Scott, David J.; Harris, Gemma; Din, Salah-Ud; Williams, Thomas L.; et al.; The Vip3Ag4 insecticidal protoxin from Bacillus thuringiensis adopts a tetrameric configuration that is maintained on proteolysis; MDPI AG; Toxins; 9; 5; 5-20172072-66512072-6651CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2072-6651/9/5/165info:eu-repo/semantics/altIdentifier/doi/10.3390/toxins9050165info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2024-05-08T13:42:15Zoai:ri.conicet.gov.ar:11336/76942instacron: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:34982024-05-08 13:42:15.71CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The Vip3Ag4 insecticidal protoxin from Bacillus thuringiensis adopts a tetrameric configuration that is maintained on proteolysis
title The Vip3Ag4 insecticidal protoxin from Bacillus thuringiensis adopts a tetrameric configuration that is maintained on proteolysis
spellingShingle The Vip3Ag4 insecticidal protoxin from Bacillus thuringiensis adopts a tetrameric configuration that is maintained on proteolysis
Palma, Leopoldo
BACILLUS THURINGIENSIS
VEGETATIVE INSECTICIDAL PROTEIN
TOXINS STRUCTURE
MODE OF ACTION
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
title_short The Vip3Ag4 insecticidal protoxin from Bacillus thuringiensis adopts a tetrameric configuration that is maintained on proteolysis
title_full The Vip3Ag4 insecticidal protoxin from Bacillus thuringiensis adopts a tetrameric configuration that is maintained on proteolysis
title_fullStr The Vip3Ag4 insecticidal protoxin from Bacillus thuringiensis adopts a tetrameric configuration that is maintained on proteolysis
title_full_unstemmed The Vip3Ag4 insecticidal protoxin from Bacillus thuringiensis adopts a tetrameric configuration that is maintained on proteolysis
title_sort The Vip3Ag4 insecticidal protoxin from Bacillus thuringiensis adopts a tetrameric configuration that is maintained on proteolysis
dc.creator.none.fl_str_mv Palma, Leopoldo
Scott, David J.
Harris, Gemma
Din, Salah-Ud
Williams, Thomas L.
Roberts, Oliver J.
Young, Mark T.
Caballero, Primitivo
Berry, Colin
author Palma, Leopoldo
author_facet Palma, Leopoldo
Scott, David J.
Harris, Gemma
Din, Salah-Ud
Williams, Thomas L.
Roberts, Oliver J.
Young, Mark T.
Caballero, Primitivo
Berry, Colin
author_role author
author2 Scott, David J.
Harris, Gemma
Din, Salah-Ud
Williams, Thomas L.
Roberts, Oliver J.
Young, Mark T.
Caballero, Primitivo
Berry, Colin
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv BACILLUS THURINGIENSIS
VEGETATIVE INSECTICIDAL PROTEIN
TOXINS STRUCTURE
MODE OF ACTION
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
topic BACILLUS THURINGIENSIS
VEGETATIVE INSECTICIDAL PROTEIN
TOXINS STRUCTURE
MODE OF ACTION
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
description The Vip3 proteins produced during vegetative growth by strains of the bacterium Bacillus thuringiensis show insecticidal activity against lepidopteran insects with a mechanism of action that may involve pore formation and apoptosis. These proteins are promising supplements to our arsenal of insecticidal proteins, but the molecular details of their activity are not understood. As a first step in the structural characterisation of these proteins, we have analysed their secondary structure and resolved the surface topology of a tetrameric complex of the Vip3Ag4 protein by transmission electron microscopy. Sites sensitive to proteolysis by trypsin are identified and the trypsin-cleaved protein appears to retain a similar structure as an octomeric complex comprising four copies each of the ~65 kDa and ~21 kDa products of proteolysis. This processed form of the toxin may represent the active toxin. The quality and monodispersity of the protein produced in this study make Vip3Ag4 a candidate for more detailed structural analysis using cryo-electron microscopy.
publishDate 2017
dc.date.none.fl_str_mv 2017-05
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/11336/76942
Palma, Leopoldo; Scott, David J.; Harris, Gemma; Din, Salah-Ud; Williams, Thomas L.; et al.; The Vip3Ag4 insecticidal protoxin from Bacillus thuringiensis adopts a tetrameric configuration that is maintained on proteolysis; MDPI AG; Toxins; 9; 5; 5-2017
2072-6651
2072-6651
CONICET Digital
CONICET
url http://hdl.handle.net/11336/76942
identifier_str_mv Palma, Leopoldo; Scott, David J.; Harris, Gemma; Din, Salah-Ud; Williams, Thomas L.; et al.; The Vip3Ag4 insecticidal protoxin from Bacillus thuringiensis adopts a tetrameric configuration that is maintained on proteolysis; MDPI AG; Toxins; 9; 5; 5-2017
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/2072-6651/9/5/165
info:eu-repo/semantics/altIdentifier/doi/10.3390/toxins9050165
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 MDPI AG
publisher.none.fl_str_mv MDPI AG
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
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 15,81155

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