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Infecciones bacterianas

Outbreak of ertapenem-resistant Enterobacter cloacae urinary tract infections due to a contaminated ureteroscope.

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Outbreak of ertapenem-resistant Enterobacter cloacae urinary tract infections due to a contaminated ureteroscope.

J Hosp Infect. 2013 Aug 15;

Authors: Chang CL, Su LH, Lu CM, Tai FT, Huang YC, Chang KK

Abstract
BACKGROUND: Outbreaks of urinary tract infections (UTIs) due to contaminated ureteroscopes have been rarely reported.
AIM: To report such an outbreak at a regional teaching hospital in southern Taiwan.
METHODS: From October to December 2010, ertapenem-resistant Enterobacter cloacae were identified from urine cultures of 15 patients who had undergone ureteroscopy prior to the infection. Three batches of surveillance cultures were obtained from the environmental objects and healthcare workers related to the procedures. Pulsed-field gel electrophoresis (PFGE) was used for bacterial typing. Antimicrobial susceptibility was assessed by disc diffusion and E-test methods. Polymerase chain reaction and sequencing were used to analyse β-lactamase genes.
FINDINGS: A total of 70 specimens were obtained during the first surveillance operation. One ertapenem-resistant E. cloacae was isolated from a ureteroscope. Although the disinfection protocols for ureteroscopes were revised and implemented, seven additional UTI cases were identified thereafter. The pathogen was identified from two subsequent surveillance cultures and was not eliminated until ethylene oxide sterilization was added to the disinfection protocol. PFGE revealed that all 15 isolates from the patients and the three isolates from the ureteroscope shared a common pattern with minor variance. Most isolates were resistant to gentamicin, levofloxacin, ceftriaxone, ceftazidime, and ertapenem. All isolates were susceptible to amikacin, imipenem, and meropenem. SHV-12 and IMP-8 genes were simultaneously identified in 16 of the 18 isolates.
CONCLUSION: The outbreak of ertapenem-resistant E. cloacae was caused by a contaminated ureteroscope and was terminated by the implementation of a revised disinfection protocol for ureteroscopes.

PMID: 23954065 [PubMed – as supplied by publisher]

Pharmacological characteristics of ertapenem.

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[Pharmacological characteristics of ertapenem.]

Klin Mikrobiol Infekc Lek. 2013 Mar;19(1):8-10

Authors: Urbánek K, Suchánková H

Abstract
Ertapenem is a broad-spectrum bactericidal carbapenem antibiotic. It differs from the other substances of this group by the absence of action against Gram-negative non-fermenting bacilli and by a long elimination half-life, which allows once-daily administration. It is administered once daily in a dose of 1 gram intravenously. Ertapenem is generally well-tolerated, with the most common side effects being diarrhea and phlebitis at the injection site. It is used for the treatment of community-acquired pneumonia, intra-abdominal and gynecological infections, and skin and soft tissue infections, including diabetic foot.

PMID: 23945830 [PubMed – as supplied by publisher]

Chemical shift perturbations induced by the acylation of Enterococcus faecium L,D-transpeptidase catalytic cysteine with ertapenem.

Chemical shift perturbations induced by the acylation of Enterococcus faecium L,D-transpeptidase catalytic cysteine with ertapenem.

Biomol NMR Assign. 2013 Aug 2;

Authors: Lecoq L, Bougault C, Triboulet S, Dubée V, Hugonnet JE, Arthur M, Simorre JP

Abstract
Penicillin-binding proteins were long considered as the only peptidoglycan cross-linking enzymes and one of the main targets of β-lactam antibiotics. A new class of transpeptidases, the L,D-transpeptidases, has emerged in the last decade. In most Gram-negative and Gram-positive bacteria, these enzymes generally have nonessential roles in peptidoglycan synthesis. In some clostridiae and mycobacteria, such as Mycobacterium tuberculosis, they are nevertheless responsible for the major peptidoglycan cross-linking pathway. L,D-Transpeptidases are thus considered as appealing new targets for the development of innovative therapeutic approaches. Carbapenems are currently investigated in this perspective as they are active on extensively drug-resistant M. tuberculosis and represent the only β-lactam class inhibiting L,D-transpeptidases. The molecular basis of the enzyme selectivity for carbapenems nevertheless remains an open question. Here we present the backbone and side-chain (1)H, (13)C, (15)N NMR assignments of the catalytic domain of Enterococcus faecium L,D-transpeptidase before and after acylation with the carbapenem ertapenem, as a prerequisite for further structural and functional studies.

PMID: 23907322 [PubMed – as supplied by publisher]