scholarly journals SpoT-Mediated Regulation and Amino Acid Prototrophy Are Essential for Pyocyanin Production During Parasitic Growth of Pseudomonas aeruginosa in a Co-culture Model System With Aeromonas hydrophila

2018 ◽  
Vol 9 ◽  
Author(s):  
Nina Jagmann ◽  
Bodo Philipp
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Aeromonas Hydrophila ◽  
Model System ◽  
Culture Model ◽  
Pyocyanin Production

THE AMINO ACID REQUIREMENTS FOR PYOCYANIN PRODUCTION

1947 ◽  
Vol 25c (4) ◽  
pp. 121-128 ◽  
Author(s):  
Margaret O. Burton ◽  
Blythe A. Eagles ◽  
Jack J. R. Campbell
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Synthetic Medium ◽  
Pigment Production ◽  
Salt Mixture ◽  
Pigment Formation ◽  
Amino Acid Requirements ◽  
Casamino Acids ◽  
Hydrolysed Casein ◽  
Pyocyanin Production

A medium consisting of acid-hydrolysed casein, glycerol, and a salt mixture has been shown to yield pyocyanin by Pseudomonas aeruginosa equal in amount to that obtained from glycerol peptone agar. The monoaminomonocarboxylic acids fraction obtained from casamino acids (Bacto) has been shown to be the source of nitrogen essential to pigment formation. Glycine, dl-alanine, dl-valine, or l-tyrosine have been shown to produce pyocyanin when employed as sole sources of nitrogen. The addition of l-leucine to media containing glycine or dl-alanine markedly increased pyocyanin formation. The addition of dl-phenylalanine to a synthetic medium inhibited pigment production. A synthetic medium consisting of dl-alanine or glycine at 0.4% concentration combined with 0.8% l-leucine, 1.0% glycerol, and a salt mixture has been shown to be the most suitable medium for pyocyanin production by five representative strains of Pseudomonas aeruginosa.

Up-regulating pyocyanin production by amino acid addition for early electrochemical identification of Pseudomonas aeruginosa

The Analyst ◽  
2014 ◽  
Vol 139 (17) ◽  
pp. 4241-4246 ◽  
Author(s):  
Hunter J. Sismaet ◽  
Thaddaeus A. Webster ◽  
Edgar D. Goluch
Keyword(s):  
Amino Acids ◽  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Electrochemical Detection ◽  
Detection Method ◽  
Acid Addition ◽  
Pyocyanin Production

A simple and rapid electrochemical detection method for Pseudomonas aeruginosa is demonstrated using amino acids as up-regulatory molecules for pyocyanin production.

Production of free amino acid fertilizer from tung meal by the newly isolated Pseudomonas aeruginosa LYT-4 strain with simultaneous potential biocontrol capacity

2020 ◽  
Vol 166 ◽  
pp. 245-252
Author(s):  
Jiangshan Ma ◽  
Huan Jiang ◽  
Peiwang Li ◽  
Changzhu Li ◽  
Rukuan Liu ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Free Amino Acid ◽  
Free Amino

scholarly journals GES-2, a Class A β-Lactamase fromPseudomonas aeruginosa with Increased Hydrolysis of Imipenem

2001 ◽  
Vol 45 (9) ◽  
pp. 2598-2603 ◽  
Author(s):  
Laurent Poirel ◽  
Gerhard F. Weldhagen ◽  
Thierry Naas ◽  
Christophe De Champs ◽  
Michael G. Dove ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Amino Acid Change ◽  
Blood Cultures ◽  
Class A ◽  
Omega Loop ◽  
Cephalosporin Resistance ◽  
Lactamase Gene ◽  
Hydrolysis Of

ABSTRACT Pseudomonas aeruginosa GW-1 was isolated in 2000 in South Africa from blood cultures of a 38-year-old female who developed nosocomial pneumonia. This isolate harbored a self-transferable ca. 100-kb plasmid that conferred an expanded-spectrum cephalosporin resistance profile associated with an intermediate susceptibility to imipenem. A β-lactamase gene, bla GES-2, was cloned from whole-cell DNA of P. aeruginosa GW-1 and expressed in Escherichia coli. GES-2, with a pI value of 5.8, hydrolyzed expanded-spectrum cephalosporins, and its substrate profile was extended to include imipenem compared to that of GES-1, identified previously in Klebsiella pneumoniae. GES-2 activity was less inhibited by clavulanic acid, tazobactam and imipenem than GES-1. The GES-2 amino acid sequence differs from that of GES-1 by a glycine-to-asparagine substitution in position 170 located in the omega loop of Ambler class A enzymes. This amino acid change may explain the extension of the substrate profile of the plasmid-encoded β-lactamase GES-2.

scholarly journals The amino acid sequence of cytochromes c-551 from three species of Pseudomonas

1973 ◽  
Vol 131 (3) ◽  
pp. 485-498 ◽  
Author(s):  
R. P. Ambler ◽  
Margaret Wynn
Keyword(s):  
Amino Acids ◽  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
Mitochondrial Cytochrome ◽  
Cytochromes C ◽  
Lending Library ◽  
Single Peptide

The amino acid sequences of the cytochromes c-551 from three species of Pseudomonas have been determined. Each resembles the protein from Pseudomonas strain P6009 (now known to be Pseudomonas aeruginosa, not Pseudomonas fluorescens) in containing 82 amino acids in a single peptide chain, with a haem group covalently attached to cysteine residues 12 and 15. In all four sequences 43 residues are identical. Although by bacteriological criteria the organisms are closely related, the differences between pairs of sequences range from 22% to 39%. These values should be compared with the differences in the sequence of mitochondrial cytochrome c between mammals and amphibians (about 18%) or between mammals and insects (about 33%). Detailed evidence for the amino acid sequences of the proteins has been deposited as Supplementary Publication SUP 50015 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973), 131, 5.

scholarly journals ampG Gene of Pseudomonas aeruginosa and Its Role in β-Lactamase Expression

2010 ◽  
Vol 54 (11) ◽  
pp. 4772-4779 ◽  
Author(s):  
Ying Zhang ◽  
Qiyu Bao ◽  
Luc A. Gagnon ◽  
Ann Huletsky ◽  
Antonio Oliver ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Transmembrane Protein ◽  
Amino Acid Identity ◽  
Clinical Isolates ◽  
Signal Molecules ◽  
Carbonyl Cyanide ◽  
Increased Sensitivity ◽  
Potential Strategy ◽  
High Level

ABSTRACT In enterobacteria, the ampG gene encodes a transmembrane protein (permease) that transports 1,6-GlcNAc-anhydro-MurNAc and the 1,6-GlcNAc-anhydro-MurNAc peptide from the periplasm to the cytoplasm, which serve as signal molecules for the induction of ampC β-lactamase. The role of AmpG as a transporter is also essential for cell wall recycling. Pseudomonas aeruginosa carries two AmpG homologues, AmpG (PA4393) and AmpGh1 (PA4218), with 45 and 41% amino acid sequence identity, respectively, to Escherichia coli AmpG, while the two homologues share only 19% amino acid identity. In P. aeruginosa strains PAO1 and PAK, inactivation of ampG drastically repressed the intrinsic β-lactam resistance while ampGh1 deletion had little effect on the resistance. Further, deletion of ampG in an ampD-null mutant abolished the high-level β-lactam resistance that is associated with the loss of AmpD activity. The cloned ampG gene is able to complement both the P. aeruginosa and the E. coli ampG mutants, while that of ampGh1 failed to do so, suggesting that PA4393 encodes the only functional AmpG protein in P. aeruginosa. We also demonstrate that the function of AmpG in laboratory strains of P. aeruginosa can effectively be inhibited by carbonyl cyanide m-chlorophenylhydrazone (CCCP), causing an increased sensitivity to β-lactams among laboratory as well as clinical isolates of P. aeruginosa. Our results suggest that inhibition of the AmpG activity is a potential strategy for enhancing the efficacy of β-lactams against P. aeruginosa, which carries inducible chromosomal ampC, especially in AmpC-hyperproducing clinical isolates.

scholarly journals The YebC Family Protein PA0964 Negatively Regulates the Pseudomonas aeruginosa Quinolone Signal System and Pyocyanin Production

2008 ◽  
Vol 190 (18) ◽  
pp. 6217-6227 ◽  
Author(s):  
Haihua Liang ◽  
Lingling Li ◽  
Zhaolin Dong ◽  
Michael G. Surette ◽  
Kangmin Duan
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Quorum Sensing ◽  
Virulence Factors ◽  
Response Regulator ◽  
Initial Study ◽  
Pfam Family ◽  
Swarming Motility ◽  
Sensing Systems ◽  
Family Protein ◽  
Pyocyanin Production

ABSTRACT Bacterial pathogenicity is often manifested by the expression of various cell-associated and secreted virulence factors, such as exoenzymes, protease, and toxins. In Pseudomonas aeruginosa, the expression of virulence genes is coordinately controlled by the global regulatory quorum-sensing systems, which includes the las and rhl systems as well as the Pseudomonas quinolone signal (PQS) system. Phenazine compounds are among the virulence factors under the control of both the rhl and PQS systems. In this study, regulation of the phzA1B1C1D1E1 (phzA1) operon, which is involved in phenazine synthesis, was investigated. In an initial study of inducing conditions, we observed that phzA1 was induced by subinhibitory concentrations of tetracycline. Screening of 13,000 mutants revealed 32 genes that altered phzA1 expression in the presence of subinhibitory tetracycline concentrations. Among them, the gene PA0964, designated pmpR ( p qsR-mediated P QS r egulator), has been identified as a novel regulator of the PQS system. It belongs to a large group of widespread conserved hypothetical proteins with unknown function, the YebC protein family (Pfam family DUF28). It negatively regulates the quorum-sensing response regulator pqsR of the PQS system by binding at its promoter region. Alongside phzA1 expression and phenazine and pyocyanin production, a set of virulence factors genes controlled by both rhl and the PQS were shown to be modulated by PmpR. Swarming motility and biofilm formation were also significantly affected. The results added another layer of regulation in the rather complex quorum-sensing systems in P. aeruginosa and demonstrated a clear functional clue for the YebC family proteins.

Possible antivirulent activity of some agents against clinical isolates of Pseudomonas aeruginosa

2021 ◽  
Vol 30 (2) ◽  
pp. 1-8
Author(s):  
Ahmad O. Rifai ◽  
Abeer M. Abd El-Aziz ◽  
Hany I. Kenawy
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Quorum Sensing ◽  
Virulence Factors ◽  
Therapeutic Target ◽  
Inhibitory Action ◽  
Antibacterial Agents ◽  
Mechanisms Of Resistance ◽  
Life Threatening ◽  
Pheniramine Maleate ◽  
Pyocyanin Production

Background: Pseudomonas aeruginosa has developed different mechanisms of resistance against antibiotics and became one of the most life-threatening pathogens. Fighting against its virulence Factors are an alternative therapeutic target. Objective: This study was directed towards the investigation of anti-quorum sensing activity and inhibitory action on virulence factors of different agents including antibacterial agents to which Pseudomonas aeruginosa isolates are resistant and non-antibacterial agents. Methodology: Anti-quorum sensing activity of ceftriaxone, ceftazidime (CAZ), cefepime (FEP), vancomycin (VA), paracetamol (PA), and pheniramine maleate (PHE) investigated as well as their ability to reduce other virulence factors including protease, hemolysin, and pyocyanin production. Results: This study showed that 3rd and 4th generations cephalosporins could be used as anti-quorum sensing agents effectively in the treatment of Pseudomonas aeruginosa infections, however, vancomycin, paracetamol, and pheniramine maleate had no effect on inhibiting the studied virulence factors. Conclusion: From our study we conclude that although cephalosporins at the used concentrations did not show anti-pseudomonal activity they were effective as anti virulent agents that could be utilized in therapeutically in controlling Pseudomonas aeruginosa infections.

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