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

^a Institute of Biocomputation and Physics of Complex Systems (BIFI), University of Zaragoza, Mariano Esquillor s/n, Campus Rio Ebro, Edificio I+D, Zaragoza, Spain
E-mail: rhurtado@bifi.es

^b Department of Chemistry, University of La Rioja, Logroño, Spain
E-mail: francisco.corzana@unirioja.es

^c UCIBIO, REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade NOVA de Lisboa, Portugal

^d Center for Biomolecular Nanotechnologies@UniLe, Istituto Italiano di Tecnologia (IIT), 73010 Arnesano, Lecce, Italy

^e Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Lisboa, Portugal

^f Instituto de Química Organica General, IQOG-CSIC, 28006 Madrid, Spain

^g Department of Chemistry, University of Cambridge, Cambridge, UK

^h Copenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, University of Copenhagen, Copenhagen, Denmark

ⁱ Laboratorio de Microscopías Avanzada (LMA), University of Zaragoza, Campus Rio Ebro, Edificio I+D, Zaragoza, Spain

^j Fundación ARAID, Zaragoza, Spain

Abstract

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.

Chemical Communications

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

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

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