Related Experiment Videos
Phosphorylation of methyl-alpha-D-glucopyranoside in polymyxin B-treated Salmonella typhimurium
Journal of Bacteriology
|December 1, 1969
Abstract:
Phosphoenolpyruvate-dependent phosphorylation of methyl-alpha-d-glucopyranoside in Salmonella typhimurium is increased by the membrane active polypeptide antibiotic polymyxin B whereas active transport ability is abolished.
Insights
Polymyxin B antibiotic enhances methyl-alpha-d-glucopyranoside phosphorylation in Salmonella typhimurium. However, the same antibiotic disrupts the bacteria's active transport capabilities.
Area of Science:
- Microbiology
- Bacterial Physiology
- Antibiotic Action
Background:
- Salmonella typhimurium utilizes phosphoenolpyruvate-dependent phosphotransferase systems for sugar uptake.
- Polypeptide antibiotics like polymyxin B can interact with bacterial membranes.
Purpose of the Study:
- To investigate the effect of polymyxin B on sugar transport and phosphorylation in Salmonella typhimurium.
- To elucidate the specific mechanisms by which polymyxin B influences bacterial nutrient uptake.
Main Methods:
- Bacterial cultures of Salmonella typhimurium were treated with polymyxin B.
- Phosphorylation rates of methyl-alpha-d-glucopyranoside were measured.
- Active transport assays were performed to assess nutrient uptake.
Main Results:
- Polymyxin B significantly increased the rate of phosphoenolpyruvate-dependent phosphorylation of methyl-alpha-d-glucopyranoside.
- Polymyxin B treatment abolished the active transport ability of Salmonella typhimurium for this sugar.
Conclusions:
- Polymyxin B differentially affects nutrient uptake pathways in Salmonella typhimurium.
- The membrane disruption by polymyxin B may lead to altered intracellular metabolic processes.