Research Article abstract
Nature Biotechnology 15, 74 - 78 (1997)
doi:10.1038/nbt0197-74
Efficient epitope mapping by bacteriophage 
surface display
Ichiro Kuwabara1, Hiroko Maruyama1, Y. Gi Mikawa3, Riaz I. Zuberi2, ,3, Fu-Tong Liu2, ,3 & Ichi N. Maruyama1, ,*
Abstract
A bacteriophage 
surface expression system, foo, was used for epitope mapping of human galectin-3. We constructed random epitope and peptide libraries and compared their efficiencies in the mapping. The galectin-3 cDNA was randomly digested by DNase I to make random epitope libraries. The libraries were screened by affinity selection using a microtiter plate coated with monoclonal antibodies. Direct DNA sequencing of the selected clones defined two distinct epitope sites consisting of nine and 11 amino-acid residues. Affinity selection of random peptide libraries recovered a number of sequences that were similar to each other but distinct from the galectin-3 sequence. These results demonstrate that a single affinity selection of epitope libraries with antibodies is able to define an epitope determinant as small as nine residues long and is more efficient in epitope mapping than random peptide libraries.
- 1Department of Cell Biology, The Scripps Research Institute, 10550 North Torrey Pines Rd., La Jolla, CA 92037.
- 2Departments of Molecular and Experimental Medicine, The Scripps Research Institute, 10550 North Torrey Pines Rd., La Jolla, CA 92037.
- 3Present addresses: (YGM) The Molecular Sciences Institute, 9894 Genesee Ave., 3rd Floor, La Jolla, CA 92037; (RIZ, FTL) La Jolla Institute for Allergy and Immunology, 10355 Science Center Dr., San Diego, CA 92121.
- *e-mail: ichi@scripps.edu
