SUMMARY: The polysaccharide (PS) located outside the peptidoglycan layer in ATCC 27092 was found to inhibit the adsorption of PL-1 phage to cell wall preparations without inactivating free phage. Electron microscopic examination of adsorption mixtures showed that the phage were adsorbed to fragments of PS material in a tail-first orientation. Phage did not adsorb to isolated peptidoglycan. The PS was composed of -rhamnose, -glucose, -glucosamine and -galactosamine, with the hexosamines possibly in -acetylated form. Prior treatment of with haemagglutinin, an anti-human blood group B agglutinin that binds specifically to -rhamnose, resulted in a concentration-dependent inhibition of phage adsorption. Phage adsorption was inhibited partially by lectins specific for -glucose and -acetyl--glucosamine, but not by lectins specific for -acetyl--glucosamine or -acetyl--galactosamine. The inhibition of phage adsorption occurred immediately upon the addition of the effective lectins, and was reversed by the addition of the respective lectin inhibitors, α-phenyl galactoside or α-methyl glucoside. The results indicate that -rhamnosyl residues are the main determinants of the PL-1 phage receptor sites, while -glucosyl residues may be involved more indirectly.


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