Molybdenum Binding by Pseudomonas aeruginosa

1986 ◽  
Vol 39 (8) ◽  
pp. 1205 ◽  
Author(s):  
S Stojkovski ◽  
RJ Magee ◽  
J Liesegang
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Uronic Acid ◽  
Extracellular Polysaccharide ◽  
Uronic Acids ◽  
Negative Bacterium ◽  
Molybdenum Complex ◽  
Gram Negative ◽  
Pseudomonas Aeruginosa Pao1 ◽  
Polysaccharide Layer

The uptake of molybdenum by certain bacteria hinders its role as a trace metal in the micronutrients for plant growth. The binding of molybdenum by the Gram-negative bacterium Pseudomonas aeruginosa, PAO1, has been investigated. A molybdenum complex of uronic acid, which forms in the extracellular polysaccharide layer (slime), was isolated and characterized by a variety of techniques. Comparisons with 'mimic' compounds of uronic acids suggest that Pseudomonas aeruginosa, PAO1, produces a binuclear, di-oxo-bridged magnesium salt MgMo2O4(C6H8O7)2.5H2O; this indicates the important role of uronic acids in metallic uptake by bacteria.

scholarly journals MexAB-OprM Efflux Pump Interaction with the Peptidoglycan of Escherichia coli and Pseudomonas aeruginosa

2021 ◽  
Vol 22 (10) ◽  
pp. 5328
Author(s):  
Miao Ma ◽  
Margaux Lustig ◽  
Michèle Salem ◽  
Dominique Mengin-Lecreulx ◽  
Gilles Phan ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Aeruginosa ◽  
Cell Division ◽  
Membrane Proteins ◽  
Outer Membrane ◽  
Efflux Pump ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Active Efflux

One of the major families of membrane proteins found in prokaryote genome corresponds to the transporters. Among them, the resistance-nodulation-cell division (RND) transporters are highly studied, as being responsible for one of the most problematic mechanisms used by bacteria to resist to antibiotics, i.e., the active efflux of drugs. In Gram-negative bacteria, these proteins are inserted in the inner membrane and form a tripartite assembly with an outer membrane factor and a periplasmic linker in order to cross the two membranes to expulse molecules outside of the cell. A lot of information has been collected to understand the functional mechanism of these pumps, especially with AcrAB-TolC from Escherichia coli, but one missing piece from all the suggested models is the role of peptidoglycan in the assembly. Here, by pull-down experiments with purified peptidoglycans, we precise the MexAB-OprM interaction with the peptidoglycan from Escherichia coli and Pseudomonas aeruginosa, highlighting a role of the peptidoglycan in stabilizing the MexA-OprM complex and also differences between the two Gram-negative bacteria peptidoglycans.

LYSOZYME SENSITIVITY OF THE CELL WALL OF PSEUDO-MONAS AERUGINOSA: FURTHER EVIDENCE FOR THE ROLE OF THE NON-PEPTIDOGLYCAN COMPONENTS IN CELL WALL RIGIDITY

1966 ◽  
Vol 12 (1) ◽  
pp. 105-108 ◽  
Author(s):  
K. Jane Carson ◽  
R. G. Eagon
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Cell Wall ◽  
Electron Micrographs ◽  
Cell Walls ◽  
Gram Negative Bacteria ◽  
Normal Cells ◽  
Thin Sections ◽  
Gram Negative ◽  
Cell Wall Rigidity

Electron micrographs of thin sections of normal cells of Pseudomonas aeruginosa showed the cell walls to be convoluted and to be composed of two distinct layers. Electron micrographs of thin sections of lysozyme-treated cells of P. aeruginosa showed (a) that the cell walls lost much of their convoluted nature; (b) that the layers of the cell walls became diffuse and less distinct; and (c) that the cell walls became separated from the protoplasts over extensive cellular areas. These results suggest that the peptidoglycan component of the unaltered cell walls of P. aeruginosa is sensitive to lysozyme. Furthermore, it appears that the peptidoglycan component is not solely responsible for the rigidity of the cell walls of Gram-negative bacteria.

scholarly journals Draft Genome Sequences of Two Pseudomonas aeruginosa Isolates from the Female Urogenital Tract

2020 ◽  
Vol 9 (1) ◽  
Author(s):  
Genevieve Johnson ◽  
Carine R. Mores ◽  
Alan J. Wolfe ◽  
Catherine Putonti
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Environmental Conditions ◽  
Draft Genome ◽  
Urogenital Tract ◽  
Negative Bacterium ◽  
Genome Sequences ◽  
Gram Negative ◽  
Content Type

Pseudomonas aeruginosa is a Gram-negative bacterium that has the ability to survive in and readily adapt to a variety of environmental conditions. Here, we report 2 genome sequences of P. aeruginosa strains, UMB1046 and UMB5686, isolated from the female urogenital tract.

Metal binding by Pseudomonas aeruginosa PAO1 is influenced by growth of the cells as a biofilm

1999 ◽  
Vol 45 (7) ◽  
pp. 616-622 ◽  
Author(s):  
S Langley ◽  
T J Beveridge
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Metal Binding ◽  
Gram Negative Bacteria ◽  
Binding Properties ◽  
Gram Negative ◽  
Pseudomonas Aeruginosa Pao1

The metal-binding properties of Pseudomonas aeruginosa PAO1 biofilms were investigated using four metals (Cu, Fe, Au, and La). All but one of the metals (i.e., Cu) were bound by the biofilms in amounts that were significantly greater than those bound by planktonically grown cells of the same strain. Lanthanum precipitation appeared to be limited to the base of the biofilms and was not promoted by a shift in lipopolysaccharide production by the cells.Key words: metal binding, biofilms, Gram-negative bacteria, bioremediation.

scholarly journals Draft Genome Sequence of a Pseudomonas aeruginosa Strain Able To Decompose N , N -Dimethyl Formamide

2016 ◽  
Vol 4 (1) ◽  
Author(s):  
Lingyue Yan ◽  
Ming Yan ◽  
Lin Xu ◽  
Li Wei ◽  
Liting Zhang
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Genome Sequence ◽  
Draft Genome ◽  
Carbon Sources ◽  
Draft Genome Sequence ◽  
Dimethyl Formamide ◽  
Organic Chemicals ◽  
Negative Bacterium ◽  
High Concentration ◽  
Gram Negative

Pseudomonas aeruginosa is a Gram-negative bacterium, which uses a variety of organic chemicals as carbon sources. Here, we report the genome sequence of the Cu1510 isolate from wastewater containing a high concentration of N , N -dimethyl formamide.

scholarly journals Draft Genome Sequences of Pseudomonas aeruginosa Isolates from Wounded Military Personnel: TABLE 1 

2016 ◽  
Vol 4 (4) ◽  
Author(s):  
Brock A. Arivett ◽  
Dave C. Ream ◽  
Steven E. Fiester ◽  
Destaalem Kidane ◽  
Luis A. Actis
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Military Personnel ◽  
Draft Genome ◽  
Multidrug Resistant ◽  
Negative Bacterium ◽  
Genome Sequences ◽  
Gram Negative ◽  
Hospital Acquired Infections ◽  
Extensive Drug Resistance ◽  
Hospital Acquired

Pseudomonas aeruginosa , a Gram-negative bacterium that causes severe hospital-acquired infections, is grouped as an ESKAPE ( Enterococcus faecium, Staphylococcus aureus, Klebsiella pneumoniae, Acinetobacter baumannii, Pseudomonas aeruginosa , and Enterobacter species) pathogen because of its extensive drug resistance phenotypes and effects on human health worldwide. Five multidrug resistant P. aeruginosa strains isolated from wounded military personnel were sequenced and annotated in this work.

scholarly journals Deletion of algK in Mucoid Pseudomonas aeruginosa Blocks Alginate Polymer Formation and Results in Uronic Acid Secretion

1998 ◽  
Vol 180 (3) ◽  
pp. 634-641 ◽  
Author(s):  
Sumita Jain ◽  
Dennis E. Ohman
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Uronic Acid ◽  
Growth Defect ◽  
Uronic Acids ◽  
Alginate Production ◽  
Polymer Formation ◽  
Gentamicin Resistance ◽  
New Gene ◽  
Small Colony ◽  
Mutant Phenotypes

ABSTRACT Chronic pulmonary infection with Pseudomonas aeruginosais a common and serious problem in patients with cystic fibrosis (CF). The P. aeruginosa isolates from these patients typically have a mucoid colony morphology due to overproduction of the exopolysaccharide alginate, which contributes to the persistence of the organisms in the CF lung. Most of the alginate biosynthetic genes are clustered in the algD operon, located at 34 min on the chromosome. Alginate biosynthesis begins with the formation of an activated monomer, GDP-mannuronate, which is known to occur via the products of the algA, algC, andalgD genes. Polymannuronate forms in the periplasm, but the gene products involved in mannuronate translocation across the inner membrane and its polymerization are not known. One locus of the operon which remained uncharacterized was a new gene called algKbetween alg44 and algE. We sequencedalgK from the mucoid CF isolate FRD1 and expressed it inEscherichia coli, which revealed a polypeptide of the predicted size (52 kDa). The sequence of AlgK showed an apparent signal peptide characteristic of a lipoprotein. AlgK-PhoA fusion proteins were constructed and shown to be active, indicating that AlgK has a periplasmic subcellular localization. To test the phenotype of an AlgK− mutant, the algK coding sequence was replaced with a nonpolar gentamicin resistance cassette to avoid polar effects on genes downstream of algK that are essential for polymer formation. The algKΔ mutant was nonmucoid, demonstrating that AlgK was required for alginate production. Also, AlgK− mutants demonstrated a small-colony phenotype on L agar, suggesting that the loss of AlgK also caused a growth defect. The mutant phenotypes were complemented by a plasmid expressingalgK in trans. When the algKΔ mutation was placed in an algJ::Tn501background, where algA was not expressed due to polar transposon effects, the growth defect was not observed. AlgK− mutants appeared to accumulate a toxic extracellular product, and we hypothesized that this could be an unpolymerized alginate precursor. High levels of low-molecular-weight uronic acid were produced by the AlgK− mutant. When AlgK−culture supernatants were subjected to dialysis, high levels of uronic acids diffused out of the dialysis sac, and no uronic acids were detectable after extensive dialysis. In contrast, the mucoid wild-type strain produced only polymerized uronic acids (i.e., alginate), whereas the algKΔ algJ::Tn501 mutant produced no uronic acids. Thus, the alginate pathway in an AlgK− mutant was blocked after transport but at a step before polymerization, suggesting that AlgK plays an important role in the polymerization of mannuronate to alginate.

The influence of fluid shear and AlCl3 on the material properties of Pseudomonas aeruginosa PAO1 and Desulfovibrio sp. EX265 biofilms

2001 ◽  
Vol 43 (6) ◽  
pp. 113-120 ◽  
Author(s):  
P. Stoodley ◽  
A. Jacobsen ◽  
B. C. Dunsmore ◽  
B. Purevdorj ◽  
S. Wilson ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Shear Stress ◽  
Material Properties ◽  
Extracellular Polysaccharide ◽  
Relative Strength ◽  
Aluminium Chloride ◽  
Shear Stresses ◽  
Fluid Shear ◽  
Pseudomonas Aeruginosa Pao1 ◽  
Lower Shear

An understanding of the material properties of biofilms is important when describing how biofilms physically interact with their environment. In this study, aerobic biofilms of Pseudomonas aeruginosa PAO1 and anaerobic sulfate-reducing bacteria (SRB) biofilms of Desulfovibrio sp. EX265 were grown under different fluid shear stresses (τg) in a chemostat recycle loop. Individual biofilm microcolonies were deformed by varying the fluid wall shear stress (τw). The deformation was quantified in terms of strain (ε), and the relative strength of the biofilms was assessed using an apparent elastic coefficient (Eapp) and residual strain (εr) after three cycles of deformation. Aluminium chloride (AlCl3) was then added to both sets of biofilm and the tests repeated. Biofilms grown under higher shear were more rigid and had a greater yield shear stress than those grown under lower shear. The addition of AlCl3 resulted in a significant increase in Eapp and also increased the yield point. We conclude that the strength of the biofilm is in part dependent on the shear under which the biofilm was grown and that the material properties of the biofilm may be manipulated through cation cross-linking of the extracellular polysaccharide (EPS) slime matrix.

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