The bacteriophage receptor sites of Staphylococcus aureus

Abstract

This investigation involves an attempt to determine the chemical nature of the bacteriophage receptor site of Staphylococcus aureus. Cell walls of the propagating strain of phage 77 were isolated by sonic oscillation and density-gradient centrifugation. They were further disintegrated by sonic oscillation and fractionated. Fractions were tested for phage-inactivating ability and attachment of phage. Particles of approx. 200 mμ diameter were isolated which were capable of both inactivation and attachment.

Chemical analysis of these particles indicated no nucleic acid, protein or polysaccharide. The amino acids glycine, lysine, alanine and glutamic acid were found by paper chromatography. Muramic acid and N-acetylglucosamine were also found. These findings indicate that the phage receptor site of the Staphylococcus cell wall is a mucopeptide. Teichoic acid has not been implicated. Inactivating ability was destroyed by heat and trichloroacetic acid. It was enhanced by trypsin (EC 3.4.4.4.) and lysozyme (EC 3.2.1.17).