P-glycoprotein epitope mapping. II. The murine monoclonal antibody MM6.15 to human multidrug-resistant cells binds with three distinct loops in the MDR1-P-glycoprotein extracellular domain
✍ Scribed by Maurizio Cianfriglia; Giulia Romagnoli; Marina Tombesi; Francesca Poloni; Giuliana Falasca; Francesca Di Modugno; Maura Castagna; Alberto Chersi
- Publisher
- John Wiley and Sons
- Year
- 1995
- Tongue
- French
- Weight
- 980 KB
- Volume
- 61
- Category
- Article
- ISSN
- 0020-7136
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✦ Synopsis
A new murine monoclonal antibody (MAb), MM6.15, to human MDRl P-glycoprotein was found to be reactive in ELISA with synthetic peptides selected from the predicted sequences of the first, fourth and sixth extracellular loop of MDRI-Pglycoprotein. In order to precisely define the MM6. 15-binding site, a peptide library of overlapping 5-to 9-mer residues covering the entire sixth extracellular loop of both human and rodent class-I P-glycoproteins was synthesized on polyethylene pins and tested for MAb binding. The results of this ELISA demonstrated that the MAb MM6. I5 reacts only with human synthetic peptides and that the critical component of the MAb recognition is made up of the amino-acid sequence LVAHKL (residues 963-968 of the MDR I -P-glycoprotein) with histidine (H), lysine (K) and possibly leucine (L), key residues of this immunogenic domain.