This article focuses on bacteriophage P4 as a potential peptide displa
y phage by exploring the possibility of using the P4 capsid decoration
component, Psu, as a peptide carrier protein. Psu is non-essential fo
r 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 p62(c-myc) protein,
has been inserted into the SacI site. The Psu(c-myc) shows full capsid
binding activity and reacts with monoclonal antibodies directed again
st the c-myc peptide. These results pave the way for the further devel
opment of a peptide display system based on bacteriophage P4.