In vitro mimicry of CaMBr1 tumor-associated antigen by synthetic oligosaccharides |
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| Authors: | Adobati Elena; Panza Luigi; Russo Giovanni; Colnaghi Maria I; Canevari Silvana |
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| Institution: | Divisione di Oncologia Sperimentale E, Istituto Nazionale per lo Studio e la Cura dci Tumori Via Venezian 1, 20133 Milano, Italy
1Dipartimento di Chimica Organica e Industriale, Università degli Studi Via Venezian 21, 20133 Milano, Italy |
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| Abstract: | The murine monoclonal antibody (Mab) MBr1, raised against thebreast cancer cell line MCF7, recognizes a saccharidic epitopeoverexpressed on a high percentage of human breast, ovary, andlung carcinomas. This antigen was originally identified on theimmunogen as a globo-series glycosphingolipid with an H-likedeterminant at its terminus (globo-H). We report here the biologicalcharacterization of the entire globo-H hexasaccharide and fivesynthetic oligosaccharides representing fragments of the entirestructure andlor different anomeric configurations. Using competitivebinding assays on live cells, we identified the residues andthe linkages essential for mimicry of the cellular antigensrecognized by Mab MBr1 on the breast carcinoma cell line MCF7and small cell lung cancer cell line POVD. The terminal tetrasaccharidicfragment of globo-H is the oligosaccharide that most resemblesthe MBr1-defined epitope both on glycolipids and on glycoproteins.This information will help in the rational design of a highlyspecific reagent for active specific immunotherapy of carcinomasoverexpressing the MBr1-defined antigen. CaMBr1 immunotherapy monoclonal antibody oligosaccharides tumor-associated antigen |
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