Role of galactosyltransferase activity in phage sensitivity and nodulation competitiveness of Rhizobium meliloti.

A stock culture of Rhizobium meliloti 102F51 contains colonies of two distinct phenotypes (Handelsman et al., J. Bacteriol. 157:703-707, 1984); one colony type is agglutinated by high dilutions of the alfalfa agglutinin, is sensitive to phage F20, and is resistant to phage 16B, and the other is agglutinated only by low dilutions of the alfalfa agglutinin, is resistant to phage F20, and is sensitive to phage 16B. Cells of the latter phenotype have an inner-membrane-bound galactosyltransferase activity that transfers galactose from UDP-galactose to a water-insoluble anionic polymer. This enzymatic activity is absent in cells of the first phenotype. All of the phage 16B-resistant mutants selected from a sensitive strain were agglutinated by high dilutions of the alfalfa agglutinin, were sensitive to phage F20, and lacked galactosyltransferase activity. The galactose-containing polymer prepared in vitro was immunologically cross-reactive with the cell surface.