Abstract
Mutants of bacteriophage ϵ 15 were selected for their inability to produce the normal phage-induced O-antigen upon infection of Salmonella anatum. Most of the mutants found belonged to a class which not only failed to produce the phage-induced antigen but also stopped the formation of host antigen. Strains lysogenic for these mutants were shown by in vitro studies to be defective in the biosynthesis of O-antigen at the level of the polymerization of lipid-bound trisaccharide units. The isolation and characterization of temperature-sensitive mutants of this type confirmed that a bacteriophage protein was defective and that this protein was directly involved in the enzymic synthesis of O-antigen. It was concluded that ϵ 15 normally prevents the activity of the host polymerizing enzyme and replaces it with a bacteriophage enzyme. Analysis of the changes in O-antigen synthesis immediately after ϵ 15 infection indicated that the host polymerizing enzyme was inhibited, but no evidence for a diffusible inhibitor was found.
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