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 pep...

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Detalles Bibliográficos
Autores: Macías-León, Javier, Bermejo, I. A., Asín, A., García García, Ana Belén, Compañón, Ismael, Jiménez-Moreno, Ester, Coelho, Helena, Mangini, V., Albuquerque, I.S., Marcelo, Filipa, Asensio, Juan Luis, Bernardes, G. J. L., Joshi, H. J., Fiammengo, R., Blixt, O., Hurtado-Guerrero, Ramón, Corzana, Francisco
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2020
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/231221
Acceso en línea:http://hdl.handle.net/10261/231221
Access Level:acceso abierto
Descripción
Sumario: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. This journal is