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Isolation of antigenic mimics of MDR1‐P‐glycoprotein by phage‐displayed peptide libraries
Author(s) -
Poloni Francesca,
Romagnoli Giulia,
Cianfriglia Maurizio,
Felici Franco
Publication year - 1995
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910610522
Subject(s) - epitope , glycoprotein , monoclonal antibody , biology , peptide library , antigen , microbiology and biotechnology , peptide , transmembrane protein , phage display , extracellular , peptide sequence , antibody , biochemistry , gene , genetics , receptor
To identify an MC57 epitope which is more efficiently expressed on inactivated forms of P‐glycoprotein we utilized peptide libraries displayed on filamentous phage. Using this technology, we selected specific phage clones blocking the binding of the murine monoclonal (MAb) MC57 with live human multi‐drug‐resistant (MDR) cells, and sequenced and analyzed their DNA. The results we obtained indicate that MAb MC57 epitope could be formed by 2 regions localized on the predicted fourth and sixth extracellular loops of the current 12‐transmembrane‐domain model predicted for MDR1‐P‐glycoprotein. Surprisingly, a third region, defined by residues 800–807 of the MDR1‐P‐glycoprotein sequence and postulated to be intracellular, was also identified as a putative part of the MC57 epitope. This finding adds weight to the interesting hypothesis that a P‐glycoprotein structure different from the current model may exist. © 1995 Wiley‐Liss, Inc .