BEL β-trefoil: A novel lectin with antineoplastic properties in king bolete (Boletus edulis) mushrooms

Autores
Bovi, Michele; Cenci, Lucia; Perduca, Massimiliano; Capaldi, Stefano; Carrizo Garcia, Maria Elena; Civiero, Laura; Chiarelli, Laurent R.; Galliano, Monica; Monaco, Hugo L.
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A novel lectin was purified from the fruiting bodies of king bolete mushrooms (Boletus edulis, also called porcino, cep or penny bun). The lectin was structurally characterized i.e its amino acid sequence and three-dimensional structure were determined. The new protein is a homodimer and each protomer folds as β-trefoil domain and therefore we propose the name Boletus edulis lectin (BEL) β-trefoil to distinguish it from the other lectin that has been described in these mushrooms. The lectin has potent anti-proliferative effects on human cancer cells, which confers to it an interesting therapeutic potential as an antineoplastic agent. Several crystal forms of the apoprotein and of complexes with different carbohydrates were studied by X-ray diffraction. The structure of the apoprotein was solved at 1.12 Å resolution. The interaction of the lectin with lactose, galactose, N-acetylgalactosamine and T-antigen disaccharide, Galβ1-3GalNAc, was examined in detail. All the three potential binding sites present in the β-trefoil fold are occupied in at least one crystal form and are described in detail in this paper. No important conformational changes are observed in the lectin when comparing its co-crystals with carbohydrates with those of the ligand-free protein.
Fil: Bovi, Michele. Universita Di Verona; Italia
Fil: Cenci, Lucia. Universita Di Verona; Italia
Fil: Perduca, Massimiliano. Universita Di Verona; Italia
Fil: Capaldi, Stefano. Universita Di Verona; Italia
Fil: Carrizo Garcia, Maria Elena. Universidad Catolica de Córdoba. Facultad de Medicina. Departamento de Química Biologica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Civiero, Laura. Università di Padova; Italia
Fil: Chiarelli, Laurent R.. Università di Pavia; Italia
Fil: Galliano, Monica. Università di Pavia; Italia
Fil: Monaco, Hugo L.. Universita Di Verona; Italia
Materia
Boletus Edulis
Lectin
Beta Trefoil
Crystal Structure
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:11336/24989
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/24989
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling BEL β-trefoil: A novel lectin with antineoplastic properties in king bolete (Boletus edulis) mushroomsBovi, MicheleCenci, LuciaPerduca, MassimilianoCapaldi, StefanoCarrizo Garcia, Maria ElenaCiviero, LauraChiarelli, Laurent R.Galliano, MonicaMonaco, Hugo L.Boletus EdulisLectinBeta TrefoilCrystal Structurehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1A novel lectin was purified from the fruiting bodies of king bolete mushrooms (Boletus edulis, also called porcino, cep or penny bun). The lectin was structurally characterized i.e its amino acid sequence and three-dimensional structure were determined. The new protein is a homodimer and each protomer folds as β-trefoil domain and therefore we propose the name Boletus edulis lectin (BEL) β-trefoil to distinguish it from the other lectin that has been described in these mushrooms. The lectin has potent anti-proliferative effects on human cancer cells, which confers to it an interesting therapeutic potential as an antineoplastic agent. Several crystal forms of the apoprotein and of complexes with different carbohydrates were studied by X-ray diffraction. The structure of the apoprotein was solved at 1.12 Å resolution. The interaction of the lectin with lactose, galactose, N-acetylgalactosamine and T-antigen disaccharide, Galβ1-3GalNAc, was examined in detail. All the three potential binding sites present in the β-trefoil fold are occupied in at least one crystal form and are described in detail in this paper. No important conformational changes are observed in the lectin when comparing its co-crystals with carbohydrates with those of the ligand-free protein.Fil: Bovi, Michele. Universita Di Verona; ItaliaFil: Cenci, Lucia. Universita Di Verona; ItaliaFil: Perduca, Massimiliano. Universita Di Verona; ItaliaFil: Capaldi, Stefano. Universita Di Verona; ItaliaFil: Carrizo Garcia, Maria Elena. Universidad Catolica de Córdoba. Facultad de Medicina. Departamento de Química Biologica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Civiero, Laura. Università di Padova; ItaliaFil: Chiarelli, Laurent R.. Università di Pavia; ItaliaFil: Galliano, Monica. Università di Pavia; ItaliaFil: Monaco, Hugo L.. Universita Di Verona; ItaliaOxford University Press2012-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/24989Bovi, Michele; Cenci, Lucia; Perduca, Massimiliano; Capaldi, Stefano; Carrizo Garcia, Maria Elena; et al.; BEL β-trefoil: A novel lectin with antineoplastic properties in king bolete (Boletus edulis) mushrooms; Oxford University Press; Glycobiology; 23; 5; 12-2012; 578-5920959-6658CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1093/glycob/cws164info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/glycob/article-lookup/doi/10.1093/glycob/cws164info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:01:16Zoai:ri.conicet.gov.ar:11336/24989instacron: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:34982025-09-03 10:01:16.899CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv BEL β-trefoil: A novel lectin with antineoplastic properties in king bolete (Boletus edulis) mushrooms
title BEL β-trefoil: A novel lectin with antineoplastic properties in king bolete (Boletus edulis) mushrooms
spellingShingle BEL β-trefoil: A novel lectin with antineoplastic properties in king bolete (Boletus edulis) mushrooms
Bovi, Michele
Boletus Edulis
Lectin
Beta Trefoil
Crystal Structure
title_short BEL β-trefoil: A novel lectin with antineoplastic properties in king bolete (Boletus edulis) mushrooms
title_full BEL β-trefoil: A novel lectin with antineoplastic properties in king bolete (Boletus edulis) mushrooms
title_fullStr BEL β-trefoil: A novel lectin with antineoplastic properties in king bolete (Boletus edulis) mushrooms
title_full_unstemmed BEL β-trefoil: A novel lectin with antineoplastic properties in king bolete (Boletus edulis) mushrooms
title_sort BEL β-trefoil: A novel lectin with antineoplastic properties in king bolete (Boletus edulis) mushrooms
dc.creator.none.fl_str_mv Bovi, Michele
Cenci, Lucia
Perduca, Massimiliano
Capaldi, Stefano
Carrizo Garcia, Maria Elena
Civiero, Laura
Chiarelli, Laurent R.
Galliano, Monica
Monaco, Hugo L.
author Bovi, Michele
author_facet Bovi, Michele
Cenci, Lucia
Perduca, Massimiliano
Capaldi, Stefano
Carrizo Garcia, Maria Elena
Civiero, Laura
Chiarelli, Laurent R.
Galliano, Monica
Monaco, Hugo L.
author_role author
author2 Cenci, Lucia
Perduca, Massimiliano
Capaldi, Stefano
Carrizo Garcia, Maria Elena
Civiero, Laura
Chiarelli, Laurent R.
Galliano, Monica
Monaco, Hugo L.
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Boletus Edulis
Lectin
Beta Trefoil
Crystal Structure
topic Boletus Edulis
Lectin
Beta Trefoil
Crystal Structure
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv A novel lectin was purified from the fruiting bodies of king bolete mushrooms (Boletus edulis, also called porcino, cep or penny bun). The lectin was structurally characterized i.e its amino acid sequence and three-dimensional structure were determined. The new protein is a homodimer and each protomer folds as β-trefoil domain and therefore we propose the name Boletus edulis lectin (BEL) β-trefoil to distinguish it from the other lectin that has been described in these mushrooms. The lectin has potent anti-proliferative effects on human cancer cells, which confers to it an interesting therapeutic potential as an antineoplastic agent. Several crystal forms of the apoprotein and of complexes with different carbohydrates were studied by X-ray diffraction. The structure of the apoprotein was solved at 1.12 Å resolution. The interaction of the lectin with lactose, galactose, N-acetylgalactosamine and T-antigen disaccharide, Galβ1-3GalNAc, was examined in detail. All the three potential binding sites present in the β-trefoil fold are occupied in at least one crystal form and are described in detail in this paper. No important conformational changes are observed in the lectin when comparing its co-crystals with carbohydrates with those of the ligand-free protein.
Fil: Bovi, Michele. Universita Di Verona; Italia
Fil: Cenci, Lucia. Universita Di Verona; Italia
Fil: Perduca, Massimiliano. Universita Di Verona; Italia
Fil: Capaldi, Stefano. Universita Di Verona; Italia
Fil: Carrizo Garcia, Maria Elena. Universidad Catolica de Córdoba. Facultad de Medicina. Departamento de Química Biologica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Civiero, Laura. Università di Padova; Italia
Fil: Chiarelli, Laurent R.. Università di Pavia; Italia
Fil: Galliano, Monica. Università di Pavia; Italia
Fil: Monaco, Hugo L.. Universita Di Verona; Italia
description A novel lectin was purified from the fruiting bodies of king bolete mushrooms (Boletus edulis, also called porcino, cep or penny bun). The lectin was structurally characterized i.e its amino acid sequence and three-dimensional structure were determined. The new protein is a homodimer and each protomer folds as β-trefoil domain and therefore we propose the name Boletus edulis lectin (BEL) β-trefoil to distinguish it from the other lectin that has been described in these mushrooms. The lectin has potent anti-proliferative effects on human cancer cells, which confers to it an interesting therapeutic potential as an antineoplastic agent. Several crystal forms of the apoprotein and of complexes with different carbohydrates were studied by X-ray diffraction. The structure of the apoprotein was solved at 1.12 Å resolution. The interaction of the lectin with lactose, galactose, N-acetylgalactosamine and T-antigen disaccharide, Galβ1-3GalNAc, was examined in detail. All the three potential binding sites present in the β-trefoil fold are occupied in at least one crystal form and are described in detail in this paper. No important conformational changes are observed in the lectin when comparing its co-crystals with carbohydrates with those of the ligand-free protein.
publishDate 2012
dc.date.none.fl_str_mv 2012-12
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/11336/24989
Bovi, Michele; Cenci, Lucia; Perduca, Massimiliano; Capaldi, Stefano; Carrizo Garcia, Maria Elena; et al.; BEL β-trefoil: A novel lectin with antineoplastic properties in king bolete (Boletus edulis) mushrooms; Oxford University Press; Glycobiology; 23; 5; 12-2012; 578-592
0959-6658
CONICET Digital
CONICET
url http://hdl.handle.net/11336/24989
identifier_str_mv Bovi, Michele; Cenci, Lucia; Perduca, Massimiliano; Capaldi, Stefano; Carrizo Garcia, Maria Elena; et al.; BEL β-trefoil: A novel lectin with antineoplastic properties in king bolete (Boletus edulis) mushrooms; Oxford University Press; Glycobiology; 23; 5; 12-2012; 578-592
0959-6658
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1093/glycob/cws164
info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/glycob/article-lookup/doi/10.1093/glycob/cws164
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 Oxford University Press
publisher.none.fl_str_mv Oxford University Press
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 13.13397

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