title: Functional characterization of glucosamine-6-phosphate synthase (GlmS) in Salmonella enterica serovar Enteritidis.
abstract: 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.
authors.affiliation: Department of Animal Sciences, University of Wisconsin-Madison, 1675 Observatory Drive, Madison, WI, 53706, USA.
authors.forename: Alexis M
authors.initials: AM
authors.lastname: Bennett
authors.affiliation: Department of Animal Sciences, University of Wisconsin-Madison, 1675 Observatory Drive, Madison, WI, 53706, USA.
authors.forename: Daniel C
authors.initials: DC
authors.lastname: Shippy
authors.affiliation: Department of Animal Sciences, University of Wisconsin-Madison, 1675 Observatory Drive, Madison, WI, 53706, USA.
authors.forename: Nicholas
authors.initials: N
authors.lastname: Eakley
authors.affiliation: Wisconsin Veterinary Diagnostic Laboratory, University of Wisconsin-Madison, Madison, WI, 53706, USA.
authors.forename: Ogi
authors.initials: O
authors.lastname: Okwumabua
authors.affiliation: Department of Animal Sciences, University of Wisconsin-Madison, 1675 Observatory Drive, Madison, WI, 53706, USA. fadl@wisc.edu.
authors.forename: Amin A
authors.initials: AA
authors.lastname: Fadl
mesh_terms: D000900:Anti-Bacterial Agents / Q000494:pharmacology; D001426:Bacterial Proteins / Q000235:genetics*; D002462:Cell Membrane / Q000502:physiology; D003902:Detergents / Q000494:pharmacology; D024901:Drug Resistance, Multiple, Bacterial / Q000235:genetics; D005945:Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D012480:Salmonella Infections / Q000382:microbiology; D012477:Salmonella enteritidis / Q000201:enzymology / Q000235:genetics* / Q000378:metabolism / Q000472:pathogenicity*; D014774:Virulence / Q000235:genetics; D001618:beta-Lactamases / Q000378:metabolism*
chemical_list: D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D003902:Detergents; D005945:Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing); D001618:beta-Lactamases; C000731191:component S, glutamate mutase protein, Bacteria
keywords: Cell envelope integrity; GlmS; Metabolism; Salmonella; Virulence