We studied the role of membrane-derived oligosaccharides (MDOs) in sodium dodecyl sulfate (SDS) resistance by Escherichia coli. MDOs are also known as osmoregulated periplasmic glucans. Wild-type E. coli MC4100 grew in the presence of 10% SDS whereas isogenic mdoA and mdoB mutants could not grow above 0.5% SDS. Similarly, E. coli DF214, a mutant (pgi, zwf) unable to grow on glucose, exhibited conditional sensitivity to SDS in that it grew in gluconate and glucose or galactose but not in gluconate and mannose or sorbose. DF214 requires both gluconate and glucose/galactose because the gluconate is used for energy production, while glucose/galactose is used for MDO synthesis. Finally, the fate of E. coli cells subjected to SDS shock either during growth or when used as an inoculum is dependent on the presence or absence of sufficient MDOs. In both cases, cells grown under high-osmolarity (low-MDO) conditions were rapidly lysed by 5% SDS. Based on findings from a wild-type E. coli (MC4100), two mdo mutants and strain DF214 we conclude that MDOs are required for SDS resistance.
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http://dx.doi.org/10.1016/S0378-1097(03)00323-9 | DOI Listing |
Commun Biol
October 2024
Université Paris-Saclay, INRAE, AgroParisTech, Institut Jean-Pierre Bourgin (IJPB), 78000, Versailles, France.
This study investigates the presence and significance of phosphorylated oligosaccharides that accumulate during the interaction between Arabidopsis thaliana and Botrytis cinerea, a necrotrophic fungus that poses a major threat to crops worldwide. While previous research has extensively characterized cell wall-derived molecules during fungal infection, the role of plasma membrane-derived ones remains unclear. Here, we reveal the discovery of inositol phosphate glycans (IPGs) released during infection, originating from plant sphingolipids, specifically glycosylinositol phosphorylceramides (GIPC).
View Article and Find Full Text PDFFront Microbiol
January 2019
Department of Biomedical and Biotechnological Sciences, University of Catania, Catania, Italy.
Even though colistin-based treatment represents the antimicrobial-regimen backbone for the management of multidrug-resistant Gram-negative infections, colistin resistance is still rare, at least as a full resistance, in (). We investigated the genomics and transcriptomics of two clinical Extensively Drug Resistance (XDR) colistin-susceptible/resistant (COL-S/R) strain-pairs in which COL-resistance was developed after exposure to colistin therapy. The molecular characterization of the strains showed that all strains belonged to PFGE-A, ST-281, OXA-23 producers, Global Clone-II, and were resistant to imipenem, meropenem, ampicillin/sulbactam, ciprofloxacin, gentamicin, amikacin, trimethoprim/sulfamethoxazole, and susceptible to tigecycline, in agreement with NGS-acquired resistome.
View Article and Find Full Text PDFCellular iron homeostasis is critical for survival and growth. Bacteria employ a variety of strategies to sequester iron from the environment and to store intracellular iron surplus that can be utilized in iron-restricted conditions while also limiting the potential for the production of iron-induced reactive oxygen species (ROS). Here, we report that membrane-derived oligosaccharide (mdo) glucan, an intrinsic component of Gram-negative bacteria, sequesters the ferrous form of iron.
View Article and Find Full Text PDFJ Bacteriol
January 2018
Dipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, Milan, Italy
Nature
May 2013
School of Biochemistry and Immunology & School of Medicine, Trinity College Dublin, Dublin 2, Ireland.
Diacylglycerol kinase catalyses the ATP-dependent phosphorylation of diacylglycerol to phosphatidic acid for use in shuttling water-soluble components to membrane-derived oligosaccharide and lipopolysaccharide in the cell envelope of Gram-negative bacteria. For half a century, this 121-residue kinase has served as a model for investigating membrane protein enzymology, folding, assembly and stability. Here we present crystal structures for three functional forms of this unique and paradigmatic kinase, one of which is wild type.
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