Prevalence of carbapenem-hydrolyzing class D β-lactamase genes in Acinetobacter spp. isolates in China

Ji, Shujuan; Chen, Yan; Ruan, Zhi; Fu, Ying; J, Ji; Wang, H.; Yang, Yu

doi:10.1007/s10096-013-2037-z

Cited by 28 publications

(29 citation statements)

References 26 publications

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“…Mohajeri et al (2013) reported that blaOXA-51-like and blaOXA-23-like genes were the predominant mechanisms of resistance to imipenem in A. baumannii. However, certain results of previous studies appear to be inconsistent with those of our study (Jeannot et al, 2014;Ji et al, 2014;Xia et al, 2014;Mohajeri et al, 2015). One study reported that only blaOXA-23 and blaOXA-51 were amplified in 96.7% of the A. baumannii strains, while neither blaOXA-24 nor blaOXA-58 was amplified (Xia et al, 2014).…”

Section: Discussioncontrasting

confidence: 99%

“…Jeannot et al (2014) reported that blaOXA-23 and blaOXA-24 were the most frequently detected genes in isolated A. baumannii. Ji et al (2014) reported that blaOXA-24 and blaOXA-58 have emerged as potential threats for hospital outbreaks of multidrug-resistant A. baumannii. Mohajeri et al (2015) observed that blaOXA-23-like gene were the main genes of A. baumannii.…”

Section: Discussionmentioning

confidence: 99%

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Investigations on the genomic diversity of OXA from isolated Acinetobacter baumannii

Zhou

Wang

et al. 2015

Genet. Mol. Res.

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ABSTRACT. We distinguished the four OXA-type carbapenemase subgroup alleles present in 120 strains of Acinetobacter baumannii by using polymerase chain reaction (PCR) and investigated the distributions of the OXA subgroups in clinically isolated samples. Amplification of the OXA genes blaOXA-23, blaOXA-24, blaOXA-51, and blaOXA-58 was performed by multiplex PCR. Antibiotics susceptibility test was conducted for determine the sensitivity of the A. baumannii to clinical common used antibiotics by Kirby-Bauer method. Results revealed that 46 (51.69%) of the samples were positive for only the blaOXA51 gene and 41 (46.07%) were positive for both the blaOXA51 and blaOXA58 genes in the 89 isolates of A. baumannii. Among these, 45 were carbapenem-resistant and 44 carbapenem-sensitive. Strains containing either blaOXA51 or blaOXA58 showed resistance or sensitivity to carbapenems, respectively. A. baumannii isolated from intensive care units showed significantly higher resistance rate to Cefepime, Piperacillin-tazobactam, Amikacin, Ceftazidime, Cefotaxime, Sulfamethoxazole-trimethoprim, and Gentamicin than those isolated from other departments (P < 0.05). In conclusion, we found that the presence of blaOXA-51 and blaOXA-58 appears to convey a mechanism of resistance or sensitivity to carbapenems, respectively, in A. baumannii clinical isolates.

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Section: Discussioncontrasting

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Investigations on the genomic diversity of OXA from isolated Acinetobacter baumannii

Zhou

Wang

et al. 2015

Genet. Mol. Res.

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“…Acinetobacter isolates have shown a complex interaction of multiple mechanisms of resistance to carbapenems, with the production of naturally occurring oxacillinases (OXA) and the absence of PBP2 being most commonly observed; for some isolates, an additional downregulation of porin expression and subsequent reduction in carbapenem entry has been observed (138). The predominant oxacillinases (OXA-23, OXA-24 or -40, OXA-51, OXA-58, and OXA-143) are responsible for the majority of phenotypic resistance to carbapenems detected in the United States, Latin America, Europe, Asia, and in many parts of the world (31,(139)(140)(141)(142)(143)(144)(145)(146)(147)(148)(149)(150). OXA-23 is a plasmid-or transposonencoded ␤-lactamase, while OXA-51 is a chromosome-based enzyme and is intrinsic to Acinetobacter.…”

Section: Antibiotic Resistance Drives Outcomesmentioning

confidence: 99%

Clinical and Pathophysiological Overview of Acinetobacter Infections: a Century of Challenges

et al. 2017

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SUMMARY Acinetobacter is a complex genus, and historically, there has been confusion about the existence of multiple species. The species commonly cause nosocomial infections, predominantly aspiration pneumonia and catheter-associated bacteremia, but can also cause soft tissue and urinary tract infections. Community-acquired infections by Acinetobacter spp. are increasingly reported. Transmission of Acinetobacter and subsequent disease is facilitated by the organism's environmental tenacity, resistance to desiccation, and evasion of host immunity. The virulence properties demonstrated by Acinetobacter spp. primarily stem from evasion of rapid clearance by the innate immune system, effectively enabling high bacterial density that triggers lipopolysaccharide (LPS)–Toll-like receptor 4 (TLR4)-mediated sepsis. Capsular polysaccharide is a critical virulence factor that enables immune evasion, while LPS triggers septic shock. However, the primary driver of clinical outcome is antibiotic resistance. Administration of initially effective therapy is key to improving survival, reducing 30-day mortality threefold. Regrettably, due to the high frequency of this organism having an extreme drug resistance (XDR) phenotype, early initiation of effective therapy is a major clinical challenge. Given its high rate of antibiotic resistance and abysmal outcomes (up to 70% mortality rate from infections caused by XDR strains in some case series), new preventative and therapeutic options for Acinetobacter spp. are desperately needed.

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“…Some superbugs accurately catalyze the hydrolysis of the β-lactam ring in β-lactam antibiotics through their target enzyme, TEM-1 β-lactamases, and thereby lead to the antibiotics losing efficacy against them (1). The recognition and binding of TEM-1 β-lactamase with the antibiotics is a precondition for the hydrolysis of the antibiotics (2).…”

Section: Introductionmentioning

confidence: 99%

Spectroscopic analysis and docking simulation on the recognition and binding of TEM-1 β-lactamase with β-lactam antibiotics

Yang

Bian

2017

Experimental and Therapeutic Medicine

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Abstract.The interaction between TEM-1 β-lactamase and antibiotics is very important in the hydrolysis of antibiotics. In the present study, the recognition and binding of TEM-1 β-lactamase with three β-lactam antibiotics, including penicillin G, cefalexin and cefoxitin, was investigated by fluorescence and ultraviolet-visible absorption spectra in combination with molecular docking in the temperature range of 278-288 K and under simulated physiological conditions. The results demonstrated that the fluorescence emissions of TEM-1 β-lactamase were extinguished by static quenching and the energy of TEM-1 β-lactamase was transferred in a non-radioactive manner. The binding of TEM-1 β-lactamase with the three antibiotics was a spontaneously exothermic process, with binding constants of 1.41x10 7 , 7.81x10 6 and 5.43x10 4 at 278 K. Furthermore, binding was driven by enthalpy change and the binding forces between them were mainly hydrogen bonding and Van der Waals forces. A TEM-1 β-lactamase only bound with one antibiotic at a time and the binding capacity between them was closely associated with the functional groups and flexibility in the antibiotics. In addition, a conformational change occurred in the TEM-1 β-lactamases when they bound with the three antibiotics and TEM-1 β-lactamase-antibiotic complexes were formed. The present study provided an insight into the recognition and binding of TEM-1 β-lactamase with β-lactam antibiotics, which may be helpful for designing a novel substrate for TEM-1 β-lactamase and developing novel antibiotics that are resistant to the enzyme.

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Prevalence of carbapenem-hydrolyzing class D β-lactamase genes in Acinetobacter spp. isolates in China

Cited by 28 publications

References 26 publications

Investigations on the genomic diversity of OXA from isolated Acinetobacter baumannii

Investigations on the genomic diversity of OXA from isolated Acinetobacter baumannii

Clinical and Pathophysiological Overview of Acinetobacter Infections: a Century of Challenges

Spectroscopic analysis and docking simulation on the recognition and binding of TEM-1 β-lactamase with β-lactam antibiotics

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