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The receptor for phage M-1 was present in the exopolysaccharide (EPS) of Rhizobium japonicum D211. The EPS was a heteropolysaccharide consisting of glucose, galactose, glucuronic acid, and glucosamine units. These monosaccharides prevented phage-cell attachment indicating that they may mimick the receptor. Phage-cell attachment was either stimulated or inhibited by Mg2+ and Ca2+ depending upon their concentration. An enzyme which depolymerized the exopolysaccharide releasing oligosaccharides was detected in the phage-infected cell lysates. A comparison of the properties of adsorption and those of the depolymerase enzyme indicated that the latter was a component of the phage and appeared to be involved in the phage-receptor interaction.
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Dandekar et al. (1978) studied this question.
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