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Epitope mapping of anti‐human transferrin monoclonal antibodies: potential uses for transferrin–transferrin receptor interaction studies
Author(s) -
Perera Yasser,
García Darién,
Guirola Osmany,
Huerta Vivian,
García Yanet,
Muñoz Yasmiana
Publication year - 2008
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.878
Subject(s) - transferrin , epitope , transferrin receptor , monoclonal antibody , antigen , biochemistry , chemistry , glycoprotein , receptor , antibody , epitope mapping , microbiology and biotechnology , biology , genetics
Abstract Human transferrin (hTf) is an 80 kDa glycoprotein involved in iron transport from the absorption sites to the sites of storage and utilization. Additionally, transferrin also plays a relevant role as a bacteriostatic agent preventing uncontrolled bacterial growth in the host. In this work we describe a well‐characterized Mabs panel in terms of precise epitope localization and estimate affinity for the two major hTf isoforms. We found at least four antigenic regions in the hTf molecule, narrowed down the interacting antigen residues within three of such regions, and located them on a molecular model of hTf. Two of the antigenic regions partially overlap with previously described transferrin‐binding sites for both human receptor (antigenic region I: containing amino acid residues from Asp‐69 to Asn‐76 at the N‐lobe) and bacterial receptors from two pathogenic species (antigenic region III: amino acid residues from Leu‐665 to Ser‐672 at the C‐lobe). Hence, such monoclonal antibodies (Mabs) could be used as an additional tool for conformational studies and/or the characterization of the interaction between hTf and both types of receptor molecules. Copyright © 2008 John Wiley & Sons, Ltd.