title: Peptide presentation by bacteriophage P4.
abstract: This article focuses on bacteriophage P4 as a potential peptide display phage by exploring the possibility of using the P4 capsid decoration component, Psu, as a peptide carrier protein. Psu is non-essential for P4 growth but it enhances the stability of the P4 capsid by binding to its exterior. We have constructed a unique SacI cloning site in the beginning of the psu gene. This site changes the third amino acid of Psu from Ser to Leu. This substitution does not destroy the binding of Psu to the P4 capsid. A synthetic oligonucleotide encoding a 10-amino acid peptide whose sequence is part of the human p62c-myc protein, has been inserted into the SacI site. The Psuc-myc shows full capsid binding activity and reacts with monoclonal antibodies directed against the c-myc peptide. These results pave the way for the further development of a peptide display system based on bacteriophage P4.
authors.affiliation: Institute of Biology, University of Oslo, Norway.
authors.forename: B H
authors.initials: BH
authors.lastname: Lindqvist
authors.forename: S
authors.initials: S
authors.lastname: Naderi
mesh_terms: D000595:Amino Acid Sequence; D001435:Bacteriophages / Q000235:genetics*; D001483:Base Sequence; D002213:Capsid / Q000235:genetics; D036022:Capsid Proteins; D003001:Cloning, Molecular; D016679:Genome, Viral; D008969:Molecular Sequence Data; D016271:Proto-Oncogene Proteins c-myc / Q000096:biosynthesis*; D011994:Recombinant Proteins / Q000096:biosynthesis*
chemical_list: D036022:Capsid Proteins; D016271:Proto-Oncogene Proteins c-myc; D011994:Recombinant Proteins; C074513:polarity suppression factor, bacteriophage P4