Efficient epitope mapping by bacteriophage lambda surface display.

Abstract:

:A bacteriophage lambda surface expression system, lambda 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 1 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.

journal_name

Nat Biotechnol

journal_title

Nature biotechnology

authors

Kuwabara I,Maruyama H,Mikawa YG,Zuberi RI,Liu FT,Maruyama IN

doi

10.1038/nbt0197-74

subject

Has Abstract

pub_date

1997-01-01 00:00:00

pages

74-8

issue

1

eissn

1087-0156

issn

1546-1696

journal_volume

15

pub_type

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