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Please use this identifier to cite or link to this item: http://hdl.handle.net/1942/4095

Title: Investigation and molecular mimicry of the antigen involved in the interaction between the monoclonal antibody 5D10 and the human breast cancer cell line MCF-7
Authors: Vandevyver, Caroline
Canarelli, Stephane
Bossen, Claudia
Fisch, Igor
Motmans, K.
Freitag, Ruth
Issue Date: 2007
Abstract: Monoclonal antibody (mAb) 5D10 is directed against the human breast cancer cell line MCF-7. Biochemical characterization of the antibody epitope was attempted and revealed a complex, most likely carbohydrate-linked nature, which prevented isolation and further studies of the interaction. A major goal of this work was to generate structural mimics of the 5D10 epitope to serve as putative substitutes in such studies. A peptide library displayed on filamentous phage was used to select for mimotope peptide sequences. All positive phage clones selected from the library displayed the amino acid sequence H2N-QMNPMYYR-CO2H. This peptide sequence, as well as a branched form of the peptide, was found to bind mAB 5D10. Moreover, both peptide sequences were able to inhibit the binding of 5D10 to the MCF-7 cells in a concentration-dependent manner, with an EC50 value in the range of 65 mu M. According to these results, random phage peptide libraries can serve to identify mimotopic peptides for unknown complex cell surface epitopes.
Notes: Ecole Polytech Fed Lausanne, Lab Biotechnol Chim, Lausanne, Switzerland. Univ Bayreuth, Chair Proc Biotechnol, D-95440 Bayreuth, Germany. Selexis SA, Plan Outes, Switzerland. Univ Hasselt, Biomed Res Inst, Diepenbeek, Belgium.VANDEVYVER, C, Ecole Polytech Fed Lausanne, Lab Biotechnol Chim, Lausanne, Switzerland.bioprozesstechnik@uni-bayreuth.de
URI: http://hdl.handle.net/1942/4095
Link to publication: http://doi.wiley.com/10.1002/bit.21276
ISI #: 000247158800007
ISSN: 0006-3592
Category: A1
Type: Journal Contribution
Validation: ecoom, 2008
Appears in Collections: Research publications

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