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...

Descripción completa

Detalles Bibliográficos
Autores: Palma Dovis, Leopoldo, Scott, David J., Harris, Gemma, Din, Salah-Ud, Williams, Thomas L., Roberts, Oliver J., Young, Mark T., Caballero Murillo, Primitivo, Berry, Colin
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2017
País:España
Institución:Universidad Pública de Navarra
Repositorio:Academica-e. Repositorio Institucional de la Universidad Pública de Navarra
OAI Identifier:oai:academica-e.unavarra.es:2454/26151
Acceso en línea:https://hdl.handle.net/2454/26151
Access Level:acceso abierto
Palabra clave:Vip3 toxin
Electron microscopy
Surface topology
id ES_ddc5a4f8c7f7ddf3ead4c4b7c4e655b1
oai_identifier_str oai:academica-e.unavarra.es:2454/26151
network_acronym_str ES
network_name_str España
repository_id_str
spelling The Vip3Ag4 insecticidal protoxin from bacillus thuringiensis adopts a tetrameric configuration that is maintained on proteolysisPalma Dovis, LeopoldoScott, David J.Harris, GemmaDin, Salah-UdWilliams, Thomas L.Roberts, Oliver J.Young, Mark T.Caballero Murillo, PrimitivoBerry, ColinVip3 toxinElectron microscopySurface topologyThe 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.The authors would like to thank the International Research Support Initiative Program Fellowship, Higher Education Commission of Pakistan for support to SUD. DJS is a Senior Molecular Biology and eutron Fellow supported by the Science and Technology Facilities Council (UK). GH is funded by the Medical Research Council (UK). Analytical services in the School of Chemistry, Cardiff University, were funded by EPSRC Grant number EP/L027240/1. Open access publishing was funded by Cardiff University.MDPIIdAB. Instituto de Agrobiotecnología / Agrobioteknologiako Institutua2017info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://hdl.handle.net/2454/26151reponame:Academica-e. Repositorio Institucional de la Universidad Pública de Navarrainstname:Universidad Pública de NavarraInglés© 2017 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license.https://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:academica-e.unavarra.es:2454/261512026-06-17T12:41:47Z
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 Dovis, Leopoldo
Vip3 toxin
Electron microscopy
Surface topology
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 Dovis, Leopoldo
Scott, David J.
Harris, Gemma
Din, Salah-Ud
Williams, Thomas L.
Roberts, Oliver J.
Young, Mark T.
Caballero Murillo, Primitivo
Berry, Colin
author Palma Dovis, Leopoldo
author_facet Palma Dovis, Leopoldo
Scott, David J.
Harris, Gemma
Din, Salah-Ud
Williams, Thomas L.
Roberts, Oliver J.
Young, Mark T.
Caballero Murillo, 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 Murillo, Primitivo
Berry, Colin
author2_role author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv IdAB. Instituto de Agrobiotecnología / Agrobioteknologiako Institutua
dc.subject.none.fl_str_mv Vip3 toxin
Electron microscopy
Surface topology
topic Vip3 toxin
Electron microscopy
Surface topology
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
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2454/26151
url https://hdl.handle.net/2454/26151
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.rights.none.fl_str_mv https://creativecommons.org/licenses/by/4.0/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv reponame:Academica-e. Repositorio Institucional de la Universidad Pública de Navarra
instname:Universidad Pública de Navarra
instname_str Universidad Pública de Navarra
reponame_str Academica-e. Repositorio Institucional de la Universidad Pública de Navarra
collection Academica-e. Repositorio Institucional de la Universidad Pública de Navarra
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869421890244706304
score 15,811543

Similares en LA Referencia