Display of Peptides and Proteins on the Surface of Bacteriophage λ

• Published in: Proceedings of the National Academy of Sciences - PNAS 1995-02, Vol.92 (5), p.1609-1613
• Main Authors: Sternberg, Nat, Hoess, Ronald H.
• Format: Article
• Language: English
• Subjects: Antibodies; Antigens, Surface; Bacteria; Bacteriophage lambda - ultrastructure; Bacteriophages; Base Sequence; Capsid; Capsid - ultrastructure; Capsid Proteins; Cells; Display devices; DNA; Gene Library; Genetic Vectors; Genomes; Libraries; Molecular Sequence Data; Oligodeoxyribonucleotides - chemistry; Peptides; Plasmids; Proteins; Recombinant Fusion Proteins - metabolism; Viral Proteins - chemistry; Viral Proteins - metabolism; Viruses
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.92.5.1609

The display of peptides or proteins on the surface of viruses is an important technology for studying peptides or proteins and their interaction with other molecules. Here we describe a display vehicle based on bacteriophage λ that incorporates a number of features distinct from other currently used display systems. Fusions of peptides or protein domains have been made to the amino terminus of the 11-kDa D protein of the λ capsid. These fusions assemble onto the viral capsid and appear to be accessible to ligand interactions, based on the ability of a monoclonal antibody to recognize an epitope fused to the D protein on phage heads. To produce large D fusion display libraries and yet avoid the cumbersome task of cloning many fragments into λ DNA, we have used the Cre-loxP site-specific recombination system in vivo to incorporate plasmids encoding the D fusions into the phage genome. Finally, we show that D fusion proteins can be added in vitro to phage lacking D protein and be assembled onto the viral capsid.