Influence of Core Oligosaccharide of Lipopolysaccharide to Outer Membrane Behavior of Escherichia coli

Wang, Zhou; Wang, Jianli; Ren, Ge; Li, Ye; Wang, Xiaoyuan

doi:10.3390/md13063325

Cited by 100 publications

(88 citation statements)

References 41 publications

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“…Both flagella and LPS are located on the cell surface of bacteria and play important roles in biofilm formation, but their relationship with one another is not clear. Previously, we constructed the E. coli Δ waaC , Δ waaF , and Δ waaG mutant strains by deleting the waaC , waaF , or waaG gene, respectively, in the chromosome of the W3110 wild‐type strain . Compared to the W3110 strain, which synthesizes core‐lipid A, the Δ waaC , Δ waaF , and Δ waaG mutant strains synthesize shorter LPS without the outer‐core, that is, Kdo 2 ‐lipid A, Hep‐Kdo 2 ‐lipid A, and Hep 3 ‐Kdo 2 ‐lipid A, respectively (Fig.…”

Section: Resultsmentioning

confidence: 99%

Deletion of the genes waaC, waaF, or waaG in Escherichia coli W3110 disables the flagella biosynthesis

Wang

Ren

et al. 2016

J. Basic Microbiol.

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Flagella assembly was investigated in the Escherichia coli W3110 wild-type strain and ΔwaaF, ΔwaaC, and ΔwaaG mutant strains that only synthesize lipopolysaccharide with different lengths, using transmission electron microscopy and whole genome transcriptome profiling. Under the electron microscope, the flagella were observed on the cell surface of the W3110 strain but not the ΔwaaC, ΔwaaF, or ΔwaaG strains. Transcriptional profiling showed that 1382 genes in ΔwaaC, 526 genes in ΔwaaF, and 965genes in ΔwaaG were significantly regulated compared to the control W3110 strain. These genes were further analyzed by gene ontology and KEGG pathway. Although there were significant transcriptional differences among the ΔwaaC, ΔwaaF, and ΔwaaG strains, genes related to flagella assembly and bacterial chemotaxis (the linkage between the flagella and the environment) were significantly down-regulated in all three strains. The data demonstrated that flagella assembly in E. coli depends on the length of lipopolysaccharide.

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Section: Resultsmentioning

confidence: 99%

Deletion of the genes waaC, waaF, or waaG in Escherichia coli W3110 disables the flagella biosynthesis

Wang

Ren

et al. 2016

J. Basic Microbiol.

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“…In order to confirm that IPTG‐induced NanT expression increases Kdo‐N 3 incorporation, we attempted to detect Kdo‐N 3 ‐containing LPS species by MS analysis of bacterial extracts. E. coli Δ waaC was utilized because this strain produces only Kdo 2 ‐lipid A (deep‐rough LPS), which can be isolated by organic extraction (Brabetz et al, ; Raetz et al, ; Z. Wang et al, ). Previous attempts to confirm Kdo‐N 3 incorporation into Δ waaC employed matrix‐assisted laser desorption‐ionization time‐of‐flight (MALDI)‐MS, but the level of Kdo‐N 3 incorporation into Δ waaC LPS was below the limit of detection (Nilsson et al, ).…”

Section: Resultsmentioning

confidence: 99%

The sialic acid transporter NanT is necessary and sufficient for uptake of 3‐deoxy‐d‐manno‐oct‐2‐ulosonic acid (Kdo) and its azido analog in Escherichia coli

Nilsson

Prathapam

Grove

et al. 2018

Molecular Microbiology

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3-Deoxy-d-manno-oct-2-ulosonic acid (Kdo) is an essential component of lipopolysaccharides (LPS) in the Gram-negative bacterial outer membrane. Metabolic labeling of Escherichia coli LPS with 8-azido-3,8-dideoxy-d-manno-oct-2-ulosonic acid (Kdo-N ) has been reported but is inefficient. For optimization, it is important to understand how exogenous Kdo-N enters the cytoplasm. Based on similarities between Kdo and sialic acids, we proposed and verified that the sialic acid transporter NanT imports exogenous Kdo-N into E. coli. We demonstrated that E. coli ΔnanT were not labeled with Kdo-N , while expression of NanT in the ΔnanT mutant restored Kdo-N incorporation. Induced NanT expression in a strain lacking Kdo biosynthesis led to higher exogenous Kdo incorporation and restoration of full-length core-LPS, suggesting that NanT also transports Kdo. While Kdo-N incorporation was observed in strains having NanT, it was not detected in Pseudomonas aeruginosa and Acinetobacter baumannii, which lack nanT. However, heterologous expression of E. coli NanT in P. aeruginosa enabled Kdo-N incorporation and labeling, though this led to abnormal morphology and growth arrest. NanT seems to define which bacteria can be labeled with Kdo-N , provides opportunities to enhance Kdo-N labeling efficiency and spectrum, and raises the possibility of Kdo biosynthetic bypass where exogenous Kdo is present, perhaps even in vivo.

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“…The waaP gene encodes a kinase that phosphorylates HepI, and deletion of waaP increases susceptibility to hydrophobic drugs . This is most likely due to a loss of the stabilising effect on the LPS layer of the interaction between phosphate groups with Mg 2+ and Ca 2+ .…”

Section: Resultsmentioning

confidence: 99%

On the Antibacterial Activity of Azacarboxylate Ligands: Lowered Metal Ion Affinities for Bis‐amide Derivatives of EDTA do not mean Reduced Activity

Mulla

Beecroft

Pál

et al. 2018

Chemistry A European J

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EDTA is widely used as an inhibitor of bacterial growth, affecting the uptake and control of metal ions by microorganisms. We describe the synthesis and characterisation of two symmetrical bis-amide derivatives of EDTA, featuring glycyl or pyridyl substituents: AmGly and AmPy . Metal ion affinities (logK) have been evaluated for a range of metals (Mg , Ca , Fe , Mn , Zn ), revealing less avid binding compared to EDTA. The solid-state structures of AmGly and of its Mg complex have been determined crystallographically. The latter shows an unusual 7-coordinate, capped octahedral Mg centre. The antibacterial activities of the two ligands and of EDTA have been evaluated against a range of health-relevant bacterial species, three Gram negative (Escherichia coli, Pseudomonas aeruginosa and Klebsiella pneumoniae) and a Gram positive (Staphylococcus aureus). The AmPy ligand is the only one that displays a significant inhibitory effect against K. pneumoniae, but is less effective against the other organisms. AmGly exhibits a more powerful inhibitory effect against E. coli at lower concentrations than EDTA (<3 mm) or AmPy , but loses its efficacy at higher concentrations. The growth inhibition of EDTA and AmGly on mutant E. coli strains with defects in outer-membrane lipopolysaccharide (LPS) structures has been assessed to provide insight into the unexpected behaviour. Taken together, the results contradict the assumption of a simple link between metal ion affinity and antimicrobial efficacy.

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Influence of Core Oligosaccharide of Lipopolysaccharide to Outer Membrane Behavior of Escherichia coli

Cited by 100 publications

References 41 publications

Deletion of the genes waaC, waaF, or waaG in Escherichia coli W3110 disables the flagella biosynthesis

Deletion of the genes waaC, waaF, or waaG in Escherichia coli W3110 disables the flagella biosynthesis

The sialic acid transporter NanT is necessary and sufficient for uptake of 3‐deoxy‐d‐manno‐oct‐2‐ulosonic acid (Kdo) and its azido analog in Escherichia coli

On the Antibacterial Activity of Azacarboxylate Ligands: Lowered Metal Ion Affinities for Bis‐amide Derivatives of EDTA do not mean Reduced Activity

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