Synthesis kinetics of poly(3-hydroxybutyrate) by using a Pseudomonas aeruginosa mutant strain grown on hexadecane

2016 ◽  
Vol 115 ◽  
pp. 171-178 ◽  
Author(s):  
Zulfiqar Ali Raza ◽  
Sharjeel Abid ◽  
Asma Rehman ◽  
Tanveer Hussain
2014 ◽  
Vol 58 (9) ◽  
pp. 5297-5305 ◽  
Author(s):  
Tiffany R. Keepers ◽  
Marcela Gomez ◽  
Chris Celeri ◽  
Wright W. Nichols ◽  
Kevin M. Krause

ABSTRACTAvibactam, a non-β-lactam β-lactamase inhibitor with activity against extended-spectrum β-lactamases (ESBLs), KPC, AmpC, and some OXA enzymes, extends the antibacterial activity of ceftazidime against most ceftazidime-resistant organisms producing these enzymes. In this study, the bactericidal activity of ceftazidime-avibactam against 18Pseudomonas aeruginosaisolates and 15Enterobacteriaceaeisolates, including wild-type isolates and ESBL, KPC, and/or AmpC producers, was evaluated. Ceftazidime-avibactam MICs (0.016 to 32 μg/ml) were lower than those for ceftazidime alone (0.06 to ≥256 μg/ml) against all isolates except for 2P. aeruginosaisolates (1blaVIM-positive isolate and 1blaOXA-23-positive isolate). The minimum bactericidal concentration/MIC ratios of ceftazidime-avibactam were ≤4 for all isolates, indicating bactericidal activity. Human serum and human serum albumin had a minimal effect on ceftazidime-avibactam MICs. Ceftazidime-avibactam time-kill kinetics were evaluated at low MIC multiples and showed time-dependent reductions in the number of CFU/ml from 0 to 6 h for all strains tested. A ≥3-log10decrease in the number of CFU/ml was observed at 6 h for allEnterobacteriaceae, and a 2-log10reduction in the number of CFU/ml was observed at 6 h for 3 of the 6P. aeruginosaisolates. Regrowth was noted at 24 h for some of the isolates tested in time-kill assays. These data demonstrate the potent bactericidal activity of ceftazidime-avibactam and support the continued clinical development of ceftazidime-avibactam as a new treatment option for infections caused byEnterobacteriaceaeandP. aeruginosa, including isolates resistant to ceftazidime by mechanisms dependent on avibactam-sensitive β-lactamases.


2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Weijia He ◽  
Huamei Yang ◽  
Xiang Wang ◽  
Hongmei Li ◽  
Qingli Dong

Abstract Quorum sensing (QS) can exist in food-related bacteria and potentially affect bacterial growth through acyl-homoserine lactones (AHLs). To verify the role of QS compounds in the cell-free supernatant, this study examined the effect of supernatant extracted from Pseudomonas aeruginosa culture on the growth kinetics of Salmonella Enteritidis. The results showed that the lag time (λ) of S. Enteritidis was apparently reduced (p < 0.05) under the influence of P. aeruginosa culture supernatant compared with the S. Enteritidis culture supernatant. HPLC-MS/MS test demonstrated that AHLs secreted by P. aeruginosa were mainly C14-HSL with a content of 85.71 μg/mL and a small amount of 3-oxo-C12-HSL. In addition, the commercially synthetic C14-HSL had positive effects on the growth of S. Enteritidis, confirming once again that the growth of S. Enteritidis was affected by AHL metabolized by other bacteria and the complexity of bacterial communication.


mSystems ◽  
2017 ◽  
Vol 2 (4) ◽  
Author(s):  
Yi-Wei Huang ◽  
Yu Wang ◽  
Yun Lin ◽  
Chin Lin ◽  
Yi-Tsung Lin ◽  
...  

ABSTRACT Inducible expression of chromosomally encoded β-lactamase(s) is a key mechanism for β-lactam resistance in Enterobacter cloacae, Citrobacter freundii, Pseudomonas aeruginosa, and Stenotrophomonas maltophilia. The muropeptides produced during the peptidoglycan recycling pathway act as activator ligands for β-lactamase(s) induction. The muropeptides 1,6-anhydromuramyl pentapeptide and 1,6-anhydromuramyl tripeptide are the known activator ligands for ampC β-lactamase expression in E. cloacae. Here, we dissected the type of muropepetides for L1/L2 β-lactamase expression in an mrdA deletion mutant of S. maltophilia. Distinct from the findings with the ampC system, 1,6-anhydromuramyl tetrapeptide is the candidate for ΔmrdA-mediated β-lactamase expression in S. maltophilia. Our work extends the understanding of β-lactamase induction and provides valuable information for combating the occurrence of β-lactam resistance. Penicillin binding proteins (PBPs) are involved in peptidoglycan synthesis, and their inactivation is linked to β-lactamase expression in ampR–β-lactamase module–harboring Gram-negative bacteria. There are seven annotated PBP genes, namely, mrcA, mrcB, pbpC, mrdA, ftsI, dacB, and dacC, in the Stenotrophomonas maltophilia genome, and these genes encode PBP1a, PBP1b, PBP1c, PBP2, PBP3, PBP4, and PBP6, respectively. In addition, S. maltophilia harbors two β-lactamase genes, L1 and L2, whose expression is induced via β-lactam challenge. The impact of PBP inactivation on L1/L2 expression was assessed in this study. Inactivation of mrdA resulted in increased L1/L2 expression in the absence of β-lactam challenge, and the underlying mechanism was further elucidated. The roles of ampNG, ampD I (the homologue of Escherichia coli ampD), nagZ, ampR, and creBC in L1/L2 expression mediated by a ΔmrdA mutant strain were assessed via mutant construction and β-lactamase activity determinations. Furthermore, the strain ΔmrdA-mediated change in the muropeptide profile was assessed using liquid chromatography mass spectrometry (LC-MS). The mutant ΔmrdA-mediated L1/L2 expression relied on functional AmpNG, AmpR, and NagZ, was restricted by AmpDI, and was less related to the CreBC two-component system. Inactivation of mrdA significantly increased the levels of total and periplasmic N-acetylglucosaminyl-1,6-anhydro-N-acetylmuramyl-l-alanyl-d-glutamyl-meso-diamnopimelic acid-d-alanine (GlcNAc-anhMurNAc tetrapeptide, or M4N), supporting that the critical activator ligands for mutant strain ΔmrdA-mediated L1/L2 expression are anhMurNAc tetrapeptides. IMPORTANCE Inducible expression of chromosomally encoded β-lactamase(s) is a key mechanism for β-lactam resistance in Enterobacter cloacae, Citrobacter freundii, Pseudomonas aeruginosa, and Stenotrophomonas maltophilia. The muropeptides produced during the peptidoglycan recycling pathway act as activator ligands for β-lactamase(s) induction. The muropeptides 1,6-anhydromuramyl pentapeptide and 1,6-anhydromuramyl tripeptide are the known activator ligands for ampC β-lactamase expression in E. cloacae. Here, we dissected the type of muropepetides for L1/L2 β-lactamase expression in an mrdA deletion mutant of S. maltophilia. Distinct from the findings with the ampC system, 1,6-anhydromuramyl tetrapeptide is the candidate for ΔmrdA-mediated β-lactamase expression in S. maltophilia. Our work extends the understanding of β-lactamase induction and provides valuable information for combating the occurrence of β-lactam resistance.


2007 ◽  
Vol 35 (1) ◽  
pp. 12-19 ◽  
Author(s):  
Bharat Lodha ◽  
Praveena Bhat ◽  
M. Suresh Kumar ◽  
Atul N. Vaidya ◽  
Sandeep Mudliar ◽  
...  

2021 ◽  
Author(s):  
Bobby Chettri ◽  
Ningombam Anjana Singha ◽  
Arvind Kumar Singh

Abstract We report kinetics of Assam crude oil degradation by Pseudomonas aeruginosa AKS1 and Bacillus sp. AKS2, both isolated from Assam refinery sediments. The isolates exhibited appreciable degrees of hydrophobicity, emulsification index and biosurfactant production. Crude oil degradation efficiency of isolates was assessed in (1) liquid medium amended with 1% v/v crude oil and (2) microcosm sediments (125 mg crude oil/ 10 g sand). In liquid culture, the biodegradation rate (k) and half-life (t1/2) values were found to be 0.0383 day -1 and 18.09 days for P. aeruginosa AKS1, and 0.0204 day -1 and 33.97 days in case of Bacillus sp. AKS2. In microcosm sand sediments, the estimated biodegradation rate (k) and half-life (t 1/2) values were 0.0138 day -1 and 50 days for P. aeruginosa AKS1, and 0.0113 day -1 and 61.34 days in case of Bacillus sp. AKS2. The level of nutrient treatment in microcosm sand sediment was 125 µg N & 62.5 µg P/g sediment in case of P. aeruginosa AKS1 and 375 µg N & 37.5 µg P/g sediment in case of Bacillus sp. AKS2. In microcosms without inorganic nutrients, biodegradation rate (k) and half-life (t1/2) values were found to be 0.0069 day -1 and 100 days for P. aeruginosa AKS1 and for Bacillus sp. AKS2, the respective values were found to be 0.0046 day -1 and 150.68 days. Our data provides important information for predictive hydrocarbon degradation in liquid medium and contaminated sediments.


2014 ◽  
Vol 0 (1(25)) ◽  
pp. 45-52
Author(s):  
Мухліс Абедалабас ◽  
М. Б. Галкін ◽  
Є. Ю. Пахомова ◽  
Т. О. Філіпова

2016 ◽  
Vol 216 ◽  
pp. 548-558 ◽  
Author(s):  
Bobby Chettri ◽  
Arghya Mukherjee ◽  
James S. Langpoklakpam ◽  
Dhrubajyoti Chattopadhyay ◽  
Arvind K. Singh

1996 ◽  
Vol 40 (3) ◽  
pp. 739-742 ◽  
Author(s):  
M Ozaki ◽  
K Komori ◽  
M Matsuda ◽  
R Yamaguchi ◽  
T Honmura ◽  
...  

The uptake of NM394, a new quinolone, by and its subsequent elution from human polymorphonuclear leukocytes were studied and compared with those of ofloxacin and ciprofloxacin. The kinetics of the uptake of NM394 was similar to that of ciprofloxacin. The maximum intracellular-to-extracellular concentration ratio was 12.3, compared with 8.6 for ciprofloxacin and 4.9 for ofloxacin at the extracellular concentration of 20 micrograms/ml. The elution of NM394 from human polymorphonuclear leukocytes occurs relatively slowly; 5 min after the removal of extracellular NM394, nearly 100% still remained in polymorphonuclear leukocytes, compared with ofloxacin, which was so rapidly eluted that only 12% remained. The uptake of NM394 was significantly decreased at 4 degrees C and by the presence of NaCN but was not affected by the presence of L-glycine, L-leucine, L-serine, adenosine, or NaF. NM394 showed intracellular activity at a concentration of 0.1 microgram/ml that significantly reduced the number of phagocytosed Pseudomonas aeruginosa cells with 2 h of incubation. These results suggest that uptake of NM394 by human polymorphonuclear leukocytes occurs via an active transport system differing from that of ofloxacin, whose uptake is affected by the presence of L-glycine and L-leucine, and that once accumulated, NM394 remains intracellularly active and participates in protection against bacterial infection.


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