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Acquired metallo-[beta]-lactamases (MBLs) belong to the families IMP, VIM, NDM, SPM, GIM, SIM, DIM, KHM, TMB, FIM, and AIM (1). IMP and VIM are the most common families. MBLs have [...]

Multidrug-resistant Achromobacter xylosoxidans was recovered from the sputum of a patient with cystic fibrosis. The VEB-1 extended-spectrum [beta]-lactamase was detected on a class 1 integron. This first report of a [...]

Objectives: To characterize the structure of a variant of Acinetobacter genomic island 1 (AGI1) in the Enterobacter cloacae clinical isolate EclC2185 responsible for an 8 year outbreak in Dijon University Hospital.Methods: The genome was sequenced (Miseq) and de novo assembled (Velvet). PCR and Sanger sequencing were performed to determine the sequence of the genomic island.Results: The new variant of AGI1 named AGI1-A (41.7 kb), located at the 3' end of the chromosomal trmE, was detected in an E. cloacae complex isolate identified as Enterobacter hormaechei subsp. oharae. The backbone of AGI1-A lacked A008, part of A025, A026 and the resolvase gene. Its MDR region (19.7 kb) contained two integrons followed by a hybrid transposon Tn502/Tn5053. The former integron was a typical In4-type class 1 integron carrying aadA1 and the latter integron carrying dfrA1 did not belong to a class described to date. The nucleotide sequence intI-dfrA1 was surrounded by a 78 bp imperfect repeat sequence in inverse orientation. An external circular form of AGI1-A was detected, suggesting potential mobility. AGI1-A was also detected in 15 isolates from the outbreak selected at random. They belonged to the ST114 high-risk clone.Conclusions: AGI1-A, a variant of AGI1 described in Acinetobacter baumannii, is the first genomic resistance island belonging to the Salmonella genomic island/Proteus genomic island/Acinetobacter genomic island family detected in E. cloacae. One might, therefore, fear for interspecies dissemination of genomic islands from this family. [ABSTRACT FROM AUTHOR]

Objectives: The objective of this study was to transfer the Salmonella genomic islands (GIs) SGI1 and SGI1-V and the Proteus GI PGI1-PmESC to clinical isolates of Enterobacteriaceae harbouring an A/C2 plasmid.Methods: The entire genetic structures of SGI1 and PGI1-PmESC from Salmonella Typhimurium and Proteus mirabilis, respectively, were characterized by PCR and DNA sequencing. Ten enterobacterial isolates from different species carrying blaTEM-24 on an A/C2 plasmid were used for the mobilization of SGI1: Escherichia coli, Enterobacter cloacae, Klebsiella pneumoniae, Proteus mirabilis, Enterobacter aerogenes, Citrobacter freundii, Klebsiella oxytoca, Proteus vulgaris, Providencia stuartii and Serratia marcescens. SGI1-V and PGI1-PmESC were transferred to E. aerogenes. Conjugation attempts were also performed using the wild strain E. aerogenes BOL and E. coli K-12 with or without pA/C2. Detection and location of the GI in the transconjugants were assessed by PCR targeting their junctions.Results: The multidrug resistance region of PGI1-PmESC contained a class 1 integron (aadB and aadA2) and regions deriving from transposon Tn501 and a hybrid Tn502/Tn5053 transposon, whereas SGI1 harboured the known determinants responsible for the pentaresistance. The transfer of SGI1 occurred from Salmonella Typhimurium to the 10 enterobacterial isolates, and transfer of SGI1-V and PGI1-PmESC occurred from P. mirabilis to E. aerogenes. In all transconjugants the GI was located at the 3'-end of trmE. SGI1 was also transferred to E. aerogenes BOL (pA/C2) and E. coli K-12 (pA/C2), but not to E. aerogenes BOL and E. coli K-12.Conclusions: This is the first known description of SGI1 mobilization into a broad range of enterobacterial species harbouring an A/C2 plasmid and the first demonstration of PGI1 movement. The A/C2 plasmid is responsible for the GI mobilization. [ABSTRACT FROM AUTHOR]

The use of fosfomycin has been limited in therapeutics in recent years. Because it has shown good antibacterial activity in vitro and clinical efficacy in some domains, it has been proposed as an alternative to current antimicrobial agents, which are subject to increasing resistance. This paper reviews the main properties of fosfomycin and the latest publications concerning multidrugresistant Enterobacteriaceae infections. In uncomplicated urinary tract infections, a single oral dose was found to be safe and effective. In complicated urinary tract infections, the same results were observed with several doses. In both cases, by using fosfomycin to treat infections, the use of carbapenems could be reduced, leading to lower costs and better microbial ecology. In severe infections, combinations with intravenous fosfomycin need to be explored further because its future activity may depend on choosing a good partner drug. Because of the fast evolution of microbial resistance, more studies are urgently needed. [ABSTRACT FROM AUTHOR]

Abstract: Eleven genotypically related Klebsiella pneumoniae isolates were obtained from 11 patients. All isolates were resistant to third-generation cephalosporins due to the production of SHV-2a extended-spectrum β-lactamase. Comparison of the outer membrane protein profiles revealed one isolate that lacked porins. This porin-deficient isolate was also resistant to cefoxitin (MIC 128μgml−1) and moxalactam (MIC 64μgml−1) and had elevated MIC of meropenem (2μgml−1) when compared to porin-expressing isolates (2–8, 4 and <0.06–0.125μgml−1, respectively). Higher MICs, associated with loss of porins in outer membrane, were also observed for cefotaxime (4–8-fold), cefepime (>2–16-fold), ciprofloxacin (4–16-fold), imipenem and aztreonam (2–16-fold), but there was no significant difference among MICs of ceftazidime. The porin-deficient mutant was probably selected in vivo during ofloxacin therapy. [Copyright &y& Elsevier]

We describe the first IMP metallo-beta-lactamase in Aeromonas caviae: IMP-19, which differed from IMP-2 by a single amino acid change (Arg to Ala at position 38). bla(IMP-19) was found within a class 1 integron located on a 35-kb plasmid. This is also the first description of an IMP producer in France.

Eighty-five extended-spectrum beta-lactamase-producing Enterobacteriaceae from a Slovak hospital have been studied. SHV-2a was predominant, but other variants have been detected, namely, SHV-5, SHV-12, TEM-12, TEM-15, and TEM-132, which differed from TEM-1 by amino acid substitutions R164H, E240K, and I173V and had kinetic properties similar to those of TEM-28.