title: Total modification of the bacteriophage lambda tail tube major subunit protein with foreign peptides.
abstract: The bacteriophage lambda has been shown previously to tolerate a high multiplicity of peptide additions to the C-terminus of the major tail tube subunit protein (gpV, the product of the V gene). However, it was not clear whether all gpV copies within a functional virion could tolerate such modification. Complementation tests with phage bearing either V gene amber mutations or a precisely deleted V gene were used to test the extent of possible tail tube peptide display. Expression of plasmid-encoded gpV fused C-terminally with certain foreign peptides allowed rescue of such V gene-defective phage to essentially wild-type levels. After extensive purification such phage were shown by sensitive Western blotting to contain only the modified form of gpV. Peptide-modified gpV could also form indefinite tail tube polymeric structures (polytubes).
authors.affiliation: Queensland Cancer Fund Research Unit, Department of Pathology, Medical School, University of Queensland, Herston, Brisbane, Australia. iand@mail.kids.usyd.edu.au
authors.forename: I S
authors.initials: IS
authors.lastname: Dunn
mesh_terms: D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins; D010582:Bacteriophage lambda / Q000235:genetics* / Q000254:growth & development / Q000648:ultrastructure; D017353:Gene Deletion; D015870:Gene Expression; D005814:Genes, Viral; D005816:Genetic Complementation Test; D008969:Molecular Sequence Data; D009154:Mutation; D019151:Peptide Library; D011108:Polymers; D018272:Porins; D011991:Receptors, Virus / Q000235:genetics; D015678:Viral Structural Proteins / Q000235:genetics; D017376:Viral Tail Proteins / Q000737:chemistry / Q000235:genetics*
chemical_list: D001425:Bacterial Outer Membrane Proteins; D019151:Peptide Library; D011108:Polymers; D018272:Porins; D011991:Receptors, Virus; D015678:Viral Structural Proteins; D017376:Viral Tail Proteins; C016532:maltoporins