Abstract
Abstract The temperate Salmonella phage ϵ15 and a soluble protein present at late times in ϵ15-infected cells can cleave the phage receptor site on the surface of sensitive cells. The phage receptor, a heteropolysaccharide containing mannose, rhamnose, and galactose is degraded by the specific cleavage of rhamnosylgalactose linkages. The products are a series of oligosaccharides. The soluble protein, purified from phage-infected cell lysates, has properties expected of a component of the phage tail. It adsorbs specifically to phage-sensitive cells, it interacts with anti-ϵ15 phage serum blocking its action on ϵ15 phage, and it contains a single polypeptide component which corresponds to one of the major polypeptides present in the ϵ15 virion by the criterion of SDS-acrylamide gel electrophoresis.
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