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 of peptide...

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Detalhes bibliográficos
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 documento: Artigo
Estado:Accepted version
Data de publicação:2020
País:España
Recursos:Universidad de Zaragoza
Repositório:Zaguán. Repositorio Digital de la Universidad de Zaragoza
OAI Identifier:oai:zaguan.unizar.es:108329
Acesso em linha:http://zaguan.unizar.es/record/108329
Nível de acesso:Acesso aberto
Descrição
Resumo: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.