Functional characterization of glucosamine-6-phosphate synthase (GlmS) in Salmonella enterica serovar Enteritidis
| Autor: | Ogi Okwumabua, Nicholas M. Eakley, Amin A. Fadl, Daniel C. Shippy, Alexis M. Bennett |
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| Rok vydání: | 2015 |
| Předmět: |
0301 basic medicine
Salmonella 030106 microbiology Mutant Detergents Virulence Salmonella infection Biology medicine.disease_cause Biochemistry Microbiology Bacterial cell structure beta-Lactamases 03 medical and health sciences Bacterial Proteins Drug Resistance Multiple Bacterial Genetics medicine Humans Molecular Biology Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) ATP synthase Cell Membrane Wild type General Medicine medicine.disease Anti-Bacterial Agents 030104 developmental biology Salmonella enteritidis Salmonella Infections biology.protein Cell envelope |
| Zdroj: | Archives of microbiology. 198(6) |
| ISSN: | 1432-072X |
| Popis: | Salmonella is a threat to public health due to consumption of contaminated food. Screening of a transposon library identified a unique mutant that was growth and host cell binding deficient. The objective of this study was to determine the functional role of glucosamine-6-phosphate synthase (GlmS) in the biology and pathogenesis of Salmonella. To examine this, we created a glmS mutant (ΔglmS) of Salmonella and examined the effect on cell envelope integrity, growth, metabolism, and pathogenesis. Our data indicated ΔglmS was defective in growth unless media were supplemented with D-glucosamine (D-GlcN). Examination of the bacterial cell envelope revealed that ΔglmS was highly sensitive to detergents, hydrophobic antibiotics, and bile salts compared to the wild type (WT). A release assay indicated that ΔglmS secreted higher amounts of β-lactamase than the WT in culture supernatant fractions. Furthermore, ΔglmS was attenuated in cell culture models of Salmonella infection. Taken together, this study determined an important role for GlmS in the pathogenesis and biology of Salmonella. |
| Databáze: | OpenAIRE |
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