RELATION BETWEEN ADSORPTION OF DIPHTHERIA PHAGE AND ITS INACTIVATION BY AN OLEIC ACID-ACTIVATED INHIBITOR

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Abstract
An inhibitor of diphtheria phage B produced by exposing a sensitive strain of Corynebacterium diphtheriae to oleic acid was shown to be neutralized by an antiserum to the host cells. Neutralizing antibody was in turn adsorbed by heated cells of the host strain. These findings suggest that the inhibitor is derived from a surface component of the cells. Additional findings support the thesis that this material is identical with or related to phage receptor substance. First, all 12 diphtheria strains which were tested adsorbed phage and produced a phage inhibitor after treatment with oleic acid. Second, a strong parallel was shown in the effect of salts, temperature, and nonionic surface-active agents on both adsorption and inhibition. The specificity of the fatty acid requirement for inhibition was investigated and it was observed, within the limits of the compounds studied, that a high molecular weight, unsaturated fatty acid with a free carboxyl group is required. Both oleic and linoleic acid were effective. The role of lipid in inhibitor production was discussed in relation to the presence of lipids in phage receptor material.