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. Peptidemodified gpV could also form indefinite tail tube polymeric structures (polytubes).

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