Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibody

The molecular basis of antibody 5E5, which recognizes the entire GalNAc unit as a primary epitope is disclosed. The antibody''s contacts with the peptide are mostly limited to two residues, allowing it to show some degree of promiscuity. These findings open the door to the chemical design...

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Autores: Macías-León, J., Bermejo, I.A., Asín, A., García-García, A., Compañón, I., Jiménez-Moreno, E., Coelho, H., Mangini, V., Albuquerque, I.S., Marcelo, F., Asensio, J.L., Bernardes, G.J.L., Joshi, H.J., Fiammengo, R., Blixt, O., Hurtado-Guerrero, R., Corzana, F.
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2020
País:España
Institución:Universidad de Zaragoza
Repositorio:Zaguán. Repositorio Digital de la Universidad de Zaragoza
OAI Identifier:oai:zaguan.unizar.es:108329
Acceso en línea:http://zaguan.unizar.es/record/108329
Access Level:acceso abierto
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spelling Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibodyMacías-León, J.Bermejo, I.A.Asín, A.García-García, A.Compañón, I.Jiménez-Moreno, E.Coelho, H.Mangini, V.Albuquerque, I.S.Marcelo, F.Asensio, J.L.Bernardes, G.J.L.Joshi, H.J.Fiammengo, R.Blixt, O.Hurtado-Guerrero, R.Corzana, F.The molecular basis of antibody 5E5, which recognizes the entire GalNAc unit as a primary epitope is disclosed. The antibody''s contacts with the peptide are mostly limited to two residues, allowing it to show some degree of promiscuity. These findings open the door to the chemical design of peptide-mimetics for developing efficient anti-cancer vaccines and diagnostic tools.2020info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersionapplication/pdfhttp://zaguan.unizar.es/record/108329reponame:Zaguán. Repositorio Digital de la Universidad de Zaragozainstname:Universidad de ZaragozaInglésinfo:eu-repo/grantAgreement/ES/AEI/BFU2016-75633-Pinfo:eu-repo/grantAgreement/ES/AEI/CTQ2013-44367-C2-2-Pinfo:eu-repo/grantAgreement/ES/AEI/PID2019-105451GB-I00info:eu-repo/grantAgreement/ES/AEI/PID2019-107476GB-I00info:eu-repo/grantAgreement/ES/AEI/RTI-2018-099592-B-C21info:eu-repo/semantics/openAccessoai:zaguan.unizar.es:1083292026-05-29T13:59:51Z
dc.title.none.fl_str_mv Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibody
title Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibody
spellingShingle Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibody
Macías-León, J.
title_short Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibody
title_full Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibody
title_fullStr Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibody
title_full_unstemmed Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibody
title_sort Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibody
dc.creator.none.fl_str_mv Macías-León, J.
Bermejo, I.A.
Asín, A.
García-García, A.
Compañón, I.
Jiménez-Moreno, E.
Coelho, H.
Mangini, V.
Albuquerque, I.S.
Marcelo, F.
Asensio, J.L.
Bernardes, G.J.L.
Joshi, H.J.
Fiammengo, R.
Blixt, O.
Hurtado-Guerrero, R.
Corzana, F.
author Macías-León, J.
author_facet Macías-León, J.
Bermejo, I.A.
Asín, A.
García-García, A.
Compañón, I.
Jiménez-Moreno, E.
Coelho, H.
Mangini, V.
Albuquerque, I.S.
Marcelo, F.
Asensio, J.L.
Bernardes, G.J.L.
Joshi, H.J.
Fiammengo, R.
Blixt, O.
Hurtado-Guerrero, R.
Corzana, F.
author_role author
author2 Bermejo, I.A.
Asín, A.
García-García, A.
Compañón, I.
Jiménez-Moreno, E.
Coelho, H.
Mangini, V.
Albuquerque, I.S.
Marcelo, F.
Asensio, J.L.
Bernardes, G.J.L.
Joshi, H.J.
Fiammengo, R.
Blixt, O.
Hurtado-Guerrero, R.
Corzana, F.
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
description The molecular basis of antibody 5E5, which recognizes the entire GalNAc unit as a primary epitope is disclosed. The antibody''s contacts with the peptide are mostly limited to two residues, allowing it to show some degree of promiscuity. These findings open the door to the chemical design of peptide-mimetics for developing efficient anti-cancer vaccines and diagnostic tools.
publishDate 2020
dc.date.none.fl_str_mv 2020
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://zaguan.unizar.es/record/108329
url http://zaguan.unizar.es/record/108329
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv info:eu-repo/grantAgreement/ES/AEI/BFU2016-75633-P
info:eu-repo/grantAgreement/ES/AEI/CTQ2013-44367-C2-2-P
info:eu-repo/grantAgreement/ES/AEI/PID2019-105451GB-I00
info:eu-repo/grantAgreement/ES/AEI/PID2019-107476GB-I00
info:eu-repo/grantAgreement/ES/AEI/RTI-2018-099592-B-C21
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv
publisher.none.fl_str_mv
dc.source.none.fl_str_mv reponame:Zaguán. Repositorio Digital de la Universidad de Zaragoza
instname:Universidad de Zaragoza
instname_str Universidad de Zaragoza
reponame_str Zaguán. Repositorio Digital de la Universidad de Zaragoza
collection Zaguán. Repositorio Digital de la Universidad de Zaragoza
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