scholarly journals Ambler Class A Extended-Spectrum β-Lactamases in Pseudomonas aeruginosa: Novel Developments and Clinical Impact

2003 ◽  
Vol 47 (8) ◽  
pp. 2385-2392 ◽  
Author(s):  
Gerhard F. Weldhagen ◽  
Laurent Poirel ◽  
Patrice Nordmann
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Clinical Impact ◽  
Class A ◽  
Extended Spectrum

Prevalence of Class A Extended-Spectrum β-Lactamases in Clinical Isolates of Acinetobacter baumannii and Pseudomonas aeruginosa

2006 ◽  
Vol 26 (1) ◽  
pp. 14-20 ◽  
Author(s):  
Se Jin Oh ◽  
Sang Uk Lee ◽  
Hyun Yong Hwang ◽  
Il Kwon Bae ◽  
Hyun Soo Jo ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Acinetobacter Baumannii ◽  
Clinical Isolates ◽  
Class A ◽  
Extended Spectrum

scholarly journals Identification of Novel VEB β-Lactamase Enzymes and Their Impact on Avibactam Inhibition

2016 ◽  
Vol 60 (5) ◽  
pp. 3183-3186 ◽  
Author(s):  
Sushmita D. Lahiri ◽  
Richard A. Alm
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Binding Pocket ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Content Type ◽  
Class A ◽  
Extended Spectrum ◽  
Class C

ABSTRACTCeftazidime-avibactam has activity againstPseudomonas aeruginosaandEnterobacteriaceaeexpressing numerous class A and class C β-lactamases, although the ability to inhibit many minor enzyme variants has not been established. Novel VEB class A β-lactamases were identified during characterization of surveillance isolates. The cloned novel VEB β-lactamases possessed an extended-spectrum β-lactamase phenotype and were inhibited by avibactam in a concentration-dependent manner. The residues that comprised the avibactam binding pocket were either identical or functionally conserved. These data demonstrate that avibactam can inhibit VEB β-lactamases.

scholarly journals PME-1, an Extended-Spectrum β-Lactamase Identified in Pseudomonas aeruginosa

2011 ◽  
Vol 55 (6) ◽  
pp. 2710-2713 ◽  
Author(s):  
Guo-Bao Tian ◽  
Jennifer M. Adams-Haduch ◽  
Tatiana Bogdanovich ◽  
Hong-Ning Wang ◽  
Yohei Doi
Keyword(s):  
Pseudomonas Aeruginosa ◽  
United Arab Emirates ◽  
Stenotrophomonas Maltophilia ◽  
Hydrolytic Activity ◽  
The United States ◽  
Amino Acid Identity ◽  
The Novel ◽  
Content Type ◽  
Class A ◽  
Extended Spectrum

ABSTRACTA novel extended-spectrum β-lactamase (ESBL) was identified in aPseudomonas aeruginosaclinical isolate obtained from a patient admitted to a hospital in Pennsylvania in 2008. The patient had a prolonged hospitalization in a hospital in Dubai, United Arab Emirates, before being transferred to the United States. The novel ESBL, designated PME-1 (Pseudomonas aeruginosaESBL 1), is a molecular class A, Bush-Jacoby-Medeiros group 2be enzyme and shared 50, 43, and 41% amino acid identity with the L2 β-lactamase ofStenotrophomonas maltophilia, CTX-M-9, and KPC-2, respectively. PME-1 conferred clinically relevant resistance to ceftazidime, cefotaxime, cefepime, and aztreonam inP. aeruginosaPAO1 but not to carbapenems. Purified PME-1 showed good hydrolytic activity against ceftazidime, cefotaxime, and aztreonam, while activity against carbapenems and cefepime could not be measured. PME-1 was inhibited well by β-lactamase inhibitors, including clavulanic acid, sulbactam, and tazobactam. TheblaPME-1gene was carried by an approximately 9-kb plasmid and flanked by tandem ISCR24elements.

scholarly journals Detection and characterization of class A extended-spectrum- -lactamase-producing Pseudomonas aeruginosa isolates in Belgian hospitals

2010 ◽  
Vol 65 (5) ◽  
pp. 866-871 ◽  
Author(s):  
Y. Glupczynski ◽  
P. Bogaerts ◽  
A. Deplano ◽  
C. Berhin ◽  
T. D. Huang ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Class A ◽  
Extended Spectrum

scholarly journals TLA-1: a New Plasmid-Mediated Extended-Spectrum β-Lactamase from Escherichia coli

2000 ◽  
Vol 44 (4) ◽  
pp. 997-1003 ◽  
Author(s):  
J. Silva ◽  
C. Aguilar ◽  
G. Ayala ◽  
M. A. Estrada ◽  
U. Garza-Ramos ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Infected Patient ◽  
Open Reading Frame ◽  
Amino Acid Residues ◽  
Reading Frame ◽  
E Coli ◽  
Class A ◽  
Extended Spectrum

ABSTRACT Escherichia coli R170, isolated from the urine of an infected patient, was resistant to expanded-spectrum cephalosporins, aztreonam, ciprofloxacin, and ofloxacin but was susceptible to amikacin, cefotetan, and imipenem. This particular strain contained three different plasmids that encoded two β-lactamases with pIs of 7.0 and 9.0. Resistance to cefotaxime, ceftazidime, aztreonam, trimethoprim, and sulfamethoxazole was transferred by conjugation from E. coli R170 to E. coli J53-2. The transferred plasmid, RZA92, which encoded a single β-lactamase, was 150 kb in length. The cefotaxime resistance gene that encodes the TLA-1 β-lactamase (pI 9.0) was cloned from the transconjugant by transformation to E. coli DH5α. Sequencing of thebla TLA-1 gene revealed an open reading frame of 906 bp, which corresponded to 301 amino acid residues, including motifs common to class A β-lactamases: 70SXXK,130SDN, and 234KTG. The amino acid sequence of TLA-1 shared 50% identity with the CME-1 chromosomal class A β-lactamase from Chryseobacterium(Flavobacterium) meningosepticum; 48.8% identity with the VEB-1 class A β-lactamase from E. coli; 40 to 42% identity with CblA of Bacteroides uniformis, PER-1 of Pseudomonas aeruginosa, and PER-2 ofSalmonella typhimurium; and 39% identity with CepA ofBacteroides fragilis. The partially purified TLA-1 β-lactamase had a molecular mass of 31.4 kDa and a pI of 9.0 and preferentially hydrolyzed cephaloridine, cefotaxime, cephalothin, benzylpenicillin, and ceftazidime. The enzyme was markedly inhibited by sulbactam, tazobactam, and clavulanic acid. TLA-1 is a new extended-spectrum β-lactamase of Ambler class A.

scholarly journals Detection of extended spectrum beta-lactamase genes in Pseudomonas aeruginosa isolated from patients in rural Eastern Cape Province, South Africa

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Mojisola C. Hosu ◽  
Sandeep D. Vasaikar ◽  
Grace E. Okuthe ◽  
Teke Apalata
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Antimicrobial Resistance ◽  
Multidrug Resistant ◽  
High Rate ◽  
Infection Prevention And Control ◽  
Beta Lactamase ◽  
Eastern Cape ◽  
Extended Spectrum Beta Lactamase ◽  
Extended Spectrum ◽  
Resistance Patterns

AbstractThe proliferation of extended spectrum beta-lactamase (ESBL) producing Pseudomonas aeruginosa represent a major public health threat. In this study, we evaluated the antimicrobial resistance patterns of P. aeruginosa strains and characterized the ESBLs and Metallo- β-lactamases (MBL) produced. Strains of P. aeruginosa cultured from patients who attended Nelson Mandela Academic Hospital and other clinics in the four district municipalities of the Eastern Cape between August 2017 and May 2019 were identified; antimicrobial susceptibility testing was carried out against thirteen clinically relevant antibiotics using the BioMérieux VITEK 2 and confirmed by Beckman autoSCAN-4 System. Real-time PCR was done using Roche Light Cycler 2.0 to detect the presence of ESBLs; blaSHV, blaTEM and blaCTX-M genes; and MBLs; blaIMP, blaVIM. Strains of P. aeruginosa demonstrated resistance to wide-ranging clinically relevant antibiotics including piperacillin (64.2%), followed by aztreonam (57.8%), cefepime (51.5%), ceftazidime (51.0%), piperacillin/tazobactam (50.5%), and imipenem (46.6%). A total of 75 (36.8%) multidrug-resistant (MDR) strains were observed of the total pool of isolates. The blaTEM, blaSHV and blaCTX-M was detected in 79.3%, 69.5% and 31.7% isolates (n = 82), respectively. The blaIMP was detected in 1.25% while no blaVIM was detected in any of the strains tested. The study showed a high rate of MDR P. aeruginosa in our setting. The vast majority of these resistant strains carried blaTEM and blaSHV genes. Continuous monitoring of antimicrobial resistance and strict compliance towards infection prevention and control practices are the best defence against spread of MDR P. aeruginosa.

scholarly journals Detection of Extended-Spectrum β-Lactamases in Clinical Isolates of Pseudomonas aeruginosa

2006 ◽  
Vol 50 (9) ◽  
pp. 2990-2995 ◽  
Author(s):  
Xiaofei Jiang ◽  
Zhe Zhang ◽  
Min Li ◽  
Danqiu Zhou ◽  
Feiyi Ruan ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Multidrug Resistant ◽  
Clinical Isolates ◽  
Screening Methods ◽  
Extended Spectrum ◽  
Pcr Product ◽  
Amoxicillin Clavulanate ◽  
Synergy Test ◽  
Esbl Producers ◽  
Disk Test

ABSTRACT With the occurrence of extended-spectrum β-lactamases (ESBLs) in Pseudomonas aeruginosa being increasingly reported worldwide, there is a need for a reliable test to detect ESBLs in clinical isolates of P. aeruginosa. In our study, a total of 75 clinical isolates of P. aeruginosa were studied. Nitrocefin tests were performed to detect the β-lactamase enzyme; isoelectric focusing electrophoresis, PCR, and PCR product sequencing were designed to further characterize the contained ESBLs. Various ESBL-screening methods were designed to compare the reliabilities of detecting ESBLs in clinical isolates of P. aeruginosa whose β-lactamases were well characterized. Thirty-four of 36 multidrug-resistant P. aeruginosa clinical isolates were positive for ESBLs. bla VEB-3 was the most prevalent ESBL gene in P. aeruginosa in our study. Among the total of 34 isolates that were considered ESBL producers, 20 strains were positive using conventional combined disk tests and 10 strains were positive using a conventional double-disk synergy test (DDST) with amoxicillin-clavulanate, expanded-spectrum cephalosporins, aztreonam, and cefepime. Modifications of the combined disk test and DDST, which consisted of shorter distances between disks (20 mm instead of 30 mm) and the use of three different plates that contained cloxacillin (200 μg/ml) alone, Phe-Arg β-naphthylamide dihydrochloride (MC-207,110; 20 μg/ml) alone, and both cloxacillin (200 μg/ml) and MC-207,110 (20 μg/ml) increased the sensitivity of the tests to 78.8%, 91.18%, 85.29%, and 97.06%.

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