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. 1971 Dec;4(6):663–673. doi: 10.1128/iai.4.6.663-673.1971

Immunity in Experimental Salmonellosis II. Basis for the Avirulence and Protective Capacity of gal E Mutants of Salmonella typhimurium

R Germanier 1, E Fürer 1
PMCID: PMC416371  PMID: 4949507

Abstract

Salmonella typhimurium strains which are deficient in uridine diphosphate (UDP)-galactose-4-epimerase (gal E mutants) owe their outstanding protective capacity when used as live vaccine to the fact that when galactose is supplied exogenously, such as occurs in vivo, smooth cell wall lipopolysaccharides are synthesized. The mutants lose most of their protective capacity when this phenotypic curing is prevented by a second mutation of the kind found in strains LT2M1A (deficient in galactokinase) or E32 (deficient in UDP-galactose-lipopolysaccharide transferase). Despite such phenotypic reversion, the gal E mutants are rendered avirulent as a result of galactose-induced bacteriolysis. Secondary mutants have been isolated which differ from each other with respect to the extent of galactose-induced lysis. The differences in galactose sensitivity are attributable to different activities of the other Leoloir pathway enzymes, namely, galactokinase and galactose-1-phosphate-uridyl transferase. The influence of these enzymes on lipopolysaccharide composition and galactose sensitivity and thus on virulence and immunogenicity of gal E mutants has been studied.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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