Emergence in Spain of a Multidrug-Resistant Enterobacter cloacae Clinical Isolate Producing SFO-1 Extended-Spectrum β-Lactamase

Fernández, Ana; Pereira, Maria Jose; Suárez, José Manuel; Poza, Margarita; Treviño, Mercedes; Villalón, Pilar; Sáez-Nieto, Juan Antonio; Regueiro, Benito J.; Villanueva, Rosa; Bou, Germán

doi:10.1128/jcm.01872-10

Cited by 46 publications

(29 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Enterobacter cloacae has been increasingly recognized as a clinically significant nosocomial pathogen (29) . Quinolones are among the most commonly prescribed antimicrobials for the treatment of serious infections caused by E. cloacae and other members of the Enterobacteriaceae family.…”

Section: Discussionmentioning

confidence: 99%

High prevalence of plasmid-mediated quinolone resistance determinants in Enterobacter cloacae isolated from hospitals of the Qazvin, Alborz, and Tehran provinces, Iran

Peymani

Farivar

Najafipour

et al. 2016

Rev. Soc. Bras. Med. Trop.

View full text Add to dashboard Cite

Introduction: Plasmid-mediated quinolone resistance (PMQR) is a growing clinical concern worldwide. The main aims of this study were to detect qnr-encoding genes and to evaluate the clonal relatedness of qnr-positive Enterobacter cloacae isolates. Methods: A total of 116 E. cloacae isolates that were not susceptible to quinolone were obtained from seven hospitals in Tehran, five hospitals in Qazvin, and two hospitals in Karaj (Iran). Bacterial identification was performed using standard laboratory methods and API 20E strips. Quinolone resistance was determined using the Kirby-Bauer disk diffusion method according to the Clinical Laboratory Standards Institute (CLSI) guidelines. PCR and sequencing were employed to detect qnrA, qnrB, and qnrS genes, and clonal relatedness was assessed using the enterobacterial repetitive intergenic consensus (ERIC)-PCR method. Results: In total, 45 (38.8%) and 71 (61.2%) of isolates showed high-and low-level quinolone resistance, respectively, and qnr-encoding genes were detected in 70 (60.3%) of them. qnrB1 [45 (38.8%) isolates] was the most commonly detected gene, followed by qnrS1 [28 (24.1%) isolates] and qnrB4 [18 (15.5%) isolates] either alone or in combination with other genes. The results of the ERIC-PCR revealed that 53 (75.7%) qnr-positive isolates were genetically unrelated. Conclusions: This study describes, for the first time, the high prevalence of the qnrB1, qnrS1, and qnrB4 genes among E. cloacae isolates in Iran. The detection of qnr genes emphasizes the need for establishing tactful policies associated with infection control measures in hospital settings in Iran.

show abstract

Section: Discussionmentioning

confidence: 99%

High prevalence of plasmid-mediated quinolone resistance determinants in Enterobacter cloacae isolated from hospitals of the Qazvin, Alborz, and Tehran provinces, Iran

Peymani

Farivar

Najafipour

et al. 2016

Rev. Soc. Bras. Med. Trop.

View full text Add to dashboard Cite

show abstract

“…Until now, the only OXA-10-like lactamase described in Enterobacteriaceae was OXA-101 (38). The SFO-1 ␤-lactamase has been isolated only from Enterobacter cloacae (16,28), and because of its plasmid location, it could be transmitted to other bacteria. To our knowledge, no OXA-24 has so far been described in Enterobacteriaceae.…”

Section: Discussionmentioning

confidence: 99%

Expression of OXA-Type and SFO-1 β-Lactamases Induces Changes in Peptidoglycan Composition and Affects Bacterial Fitness

Fernández

Pérez

Ayala

et al. 2012

Antimicrob Agents Chemother

Self Cite

View full text Add to dashboard Cite

b␤-Lactamases and penicillin-binding proteins (PBPs) have evolved from a common ancestor. ␤-Lactamases are enzymes that degrade ␤-lactam antibiotics, whereas PBPs are involved in the synthesis and processing of peptidoglycan, which forms an elastic network in the bacterial cell wall. This study analyzed the interaction between ␤-lactamases and peptidoglycan and the impact on fitness and biofilm production. A representative set of all classes of ␤-lactamases was cloned in the expression vector pBGS18 under the control of the CTX-M promoter and expressed in Escherichia coli MG1655. The peptidoglycan composition of all clones was evaluated, and quantitative changes were found in E. coli strains expressing OXA-24, OXA-10-like, and SFO-1 (with its upstream regulator AmpR) ␤-lactamases; the level of cross-linked muropeptides decreased, and their average length increased. These changes were associated with a statistically significant fitness cost, which was demonstrated in both in vitro and in vivo experiments. The observed changes in peptidoglycan may be explained by the presence of residual DD-endopeptidase activity in these ␤-lactamases, which may result in hydrolysis of the peptide cross bridge. The biological cost associated with these changes provides important data regarding the interaction between ␤-lactamases and the metabolism of peptidoglycan and may provide an explanation for the epidemiology of these ␤-lactamases in Enterobacteriaceae.

show abstract

“…The first example of probable gene transfer in this group is that of the gene encoding the ESBL SFO-1 in S. fonticola (71,126), followed by those in K. ascorbata and other Kluyvera species, the source of most CTX-M enzymes (48,49,124). The bla OXY gene was furthermore recently shown to be present on a plasmid in K. pneumoniae and K. oxytoca isolates (127).…”

Section: Enzymes Produced By Gram-negative Bacteriamentioning

confidence: 99%

A Structure-Based Classification of Class A β-Lactamases, a Broadly Diverse Family of Enzymes

Slama²,

et al. 2016

View full text Add to dashboard Cite

SUMMARYFor medical biologists, sequencing has become a commonplace technique to support diagnosis. Rapid changes in this field have led to the generation of large amounts of data, which are not always correctly listed in databases. This is particularly true for data concerning class A β-lactamases, a group of key antibiotic resistance enzymes produced by bacteria. Many genomes have been reported to contain putative β-lactamase genes, which can be compared with representative types. We analyzed several hundred amino acid sequences of class A β-lactamase enzymes for phylogenic relationships, the presence of specific residues, and cluster patterns. A clear distinction was first made between dd-peptidases and class A enzymes based on a small number of residues (S70, K73, P107, 130SDN132, G144, E166, 234K/R, 235T/S, and 236G [Ambler numbering]). Other residues clearly separated two main branches, which we named subclasses A1 and A2. Various clusters were identified on the major branch (subclass A1) on the basis of signature residues associated with catalytic properties (e.g., limited-spectrum β-lactamases, extended-spectrum β-lactamases, and carbapenemases). For subclass A2 enzymes (e.g., CfxA, CIA-1, CME-1, PER-1, and VEB-1), 43 conserved residues were characterized, and several significant insertions were detected. This diversity in the amino acid sequences of β-lactamases must be taken into account to ensure that new enzymes are accurately identified. However, with the exception of PER types, this diversity is poorly represented in existing X-ray crystallographic data.

show abstract

Emergence in Spain of a Multidrug-Resistant Enterobacter cloacae Clinical Isolate Producing SFO-1 Extended-Spectrum β-Lactamase

Cited by 46 publications

References 46 publications

High prevalence of plasmid-mediated quinolone resistance determinants in Enterobacter cloacae isolated from hospitals of the Qazvin, Alborz, and Tehran provinces, Iran

High prevalence of plasmid-mediated quinolone resistance determinants in Enterobacter cloacae isolated from hospitals of the Qazvin, Alborz, and Tehran provinces, Iran

Expression of OXA-Type and SFO-1 β-Lactamases Induces Changes in Peptidoglycan Composition and Affects Bacterial Fitness

A Structure-Based Classification of Class A β-Lactamases, a Broadly Diverse Family of Enzymes

Contact Info

Product

Resources

About