Epitope Mapping of the Monoclonal Antibody MM12.10 to External MDR1 P-Glycoprotein Domain by Synthetic Peptide Scanning and Phage Display Technologies
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G. Romagnoli
Abstract
Epitope mapping of MDR1-P-glycoprotein using specific monoclonal antibodies (mAbs) may help in delineating P-glycoprotein topology and hence in elucidating the relationship between its structural organization and drug-efflux pump function. In this work, by using synthetic peptide scanning and phage display technologies, the binding sites of the mAb MM12.10, a novel antibody to intact human multidrug resistant (MDR) cells, were studied. The results we obtained confirm that two regions localized on the predicted fourth and sixth loops are indeed external and that MDR1 peptides covering the inner domain of the current 12 transmembrane segment (TMs) model of Pglycoprotein could form part of the MM12.10 epitope.
Copyright ©1999 by Walter de Gruyter GmbH & Co. KG
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Articles in the same Issue
- Biosynthesis of Glycosylphosphatidylinositols in Mammals and Unicellular Microbes
- Activation of DNA Replication in Yeast by Recruitment of the RNA Polymerase II Transcription Complex
- On the Role of Symmetrical and Asymmetrical Chaperonin Complexes in Assisted Protein Folding
- Regulation of Cathepsin B Activity by Cysteine and Related Thiols
- Epitope Mapping of the Monoclonal Antibody MM12.10 to External MDR1 P-Glycoprotein Domain by Synthetic Peptide Scanning and Phage Display Technologies
- Molecular Mimicry between a Monoclonal Antibody and One Subunit of Crotoxin, a Heterodimeric Phospholipase A2 Neurotoxin
- Enzyme-Linked Immunosorbent Assay for the Measurement of JNK Activity in Cell Extracts
- Mitochondrial DNA Acts as Potential Promoter of the Baculovirus RNA Polymerase
- In Vitro Phosphorylation of Purified Glycosylphos-phatidylinositol-Specific Phospholipase D
- Cathepsin S and Cruzipain Are Inhibited by Equistatin from Actinia equina
- Lipopeptides as Dimerization Inhibitors of HIV-1 Protease
