Properties of a Salmonella typhimurium mutant with an incomplete deficiency of uridinediphosphogalactose-4-epimerase.

A galactose-negative mutant, nonleaky in respect to fermentation and utilization, isolated from a smooth Salmonella typhimurium strain by phage selection and inferred deficient of uridine diphosphate (UDP)-galactose-epimerase, was used for experiments on relation of somatic lipopolysaccharide (LPS) character to virulence. Extracts of induced mutant cells retained ca. 1% of wild-type epimerase activity and had only ca. 5% of wild-type kinase and uridyl transferase activities; also, some cultural properties of the mutant differed from those of mutants with complete defects of epimerase only. The mutant was not galactose sensitive, presumably because of its kinase defect. Although the mutant had the phage pattern (including C21-sensitivity) of an epimerase mutant, it was susceptible to transduction by phage P22 and was O-agglutinable, even when grown on defined medium; its LPS must therefore contain some O polymer, including endogenous galactose, resulting from residual epimerase activity. Growth on galactose-supplemented medium restored smooth phage sensitivity; since the mutant was partly inducible this may result, at least in part, from increased endogenous production of UDP-galactose. The mutant was made galactose positive by introduction of an F'-gal(+) plasmid. Base-change and frame-shift mutagens did not increase the frequency of reversion above the spontaneous rate. An insertion into the operator-promoter region of the gal operon seems the most likely mechanism of the mutation.