Efficient epitope mapping by bacteriophage λ surface display

Ichiro Kuwabara, Hiroko Maruyama, Y. Gi Mikawa, Riaz I. Zuberi, Fu-Tong Liu, Ichi N. Maruyama

Research output: Contribution to journalArticlepeer-review

35 Scopus citations


A bacteriophage λ surface expression system, λfoo, 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.

Original languageEnglish (US)
Pages (from-to)74-78
Number of pages5
JournalNature Biotechnology
Issue number1
StatePublished - 1997


  • animal lectin
  • fusion protein
  • human galectin-3
  • phage surface expression

ASJC Scopus subject areas

  • Microbiology


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