Journal
MICROBIOLOGY-SGM
Volume 155, Issue -, Pages 3403-3410Publisher
MICROBIOLOGY SOC
DOI: 10.1099/mic.0.029553-0
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Funding
- BBSRC Applied Genomics Link
- BBSRC Project
- BBSRC [BB/E002943/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/E002943/1] Funding Source: researchfish
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The enzyme phosphoglucomutase (Pgm) catalyses the interconversion of glucose 1-phosphate and glucose 6-phosphate and contributes to glycolysis and the generation of sugar nucleotides for biosynthesis. To assess the role of this enzyme in the biology of the pathogen Salmonella enterica serovar Typhimurium we have characterized a pgm deletion mutant in strain SL1344. Compared to SL1344, SL1344 pgm had impaired growth in vitro, was deficient in the ability to utilize galactose as a carbon source and displayed reduced O-antigen polymer length. The mutant was also more susceptible to antimicrobial peptides and showed decreased fitness in the mouse typhoid model. The in vivo phenotype of SL1344 pgm indicated a role for pgm in the early stages of infection, most likely through deficient C-antigen production. Although pgm mutants in other pathogens have potential as live attenuated vaccine strains, SL1344 pgm was not sufficiently attenuated for such use.
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