Phage display selection and analysis of Ab-binding epitopes.

David Enshell-Seijffers*, Jonathan M. Gershoni

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


The identification and characterization of B cell epitopes by combinatorial phage display peptide analyses is based on the principle that unique peptides can be affinity-purified from an enormous collection of random peptides. Moreover, once selected, the peptide sequence can be elucidated; filamentous bacteriophages have been genetically engineered to incorporate the DNA template corresponding to the peptide displayed on its surface. This unit begins with a discussion of some of the factors that distinguish available libraries. Protocols are then provided for affinity selection of antibody-specific phages, determination of phage titer, confirmation and amplification of positive phages, phage characterization, and construction of custom-tailored phages. The selection protocol in this unit is specific and designed for libraries that are used in the authors' laboratory and are based on the fth1 or fd-tet derived vectors. However, information is included for adapting these protocols to the specific requirements of other phage display libraries.

Original languageEnglish
Pages (from-to)Unit 9.8
JournalCurrent Protocols in Immunology
VolumeChapter 9
StatePublished - Nov 2002


Dive into the research topics of 'Phage display selection and analysis of Ab-binding epitopes.'. Together they form a unique fingerprint.

Cite this