VIM and IMP metallo-β-lactamases and other extended-spectrum β-lactamases in Escherichia coli and Klebsiella pneumoniae from environmental samples in a Tunisian hospital

Chouchani, Chedly; Marrakchi, Rim; Ferchichi, Leila; Salabi, Allaaeddin El; Walsh, Timothy R.

doi:10.1111/j.1600-0463.2011.02793.x

Cited by 28 publications

(15 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Plasmid-encoded MBLs emerged in Japan in 1990 with the IMP family of enzymes (151) and in Italy in 1997 with the VIM ␤-lactamases (152), causing some to predict a global epidemic of multidrug-resistant MBL-producing Gram-negative bacteria. Although the IMP and VIM MBL families began to expand after 2000 (Table 3), outbreaks associated with these enzymes have tended to be small, limited in time, and localized to specific geographical regions (153)(154)(155)(156)(157).…”

Section: ␤-Lactamases In Gram-negative Bacteriamentioning

confidence: 99%

Past and Present Perspectives on β-Lactamases

Bush

2018

Antimicrob Agents Chemother

636

498

View full text Add to dashboard Cite

β-Lactamases, the major resistance determinant for β-lactam antibiotics in Gram-negative bacteria, are ancient enzymes whose origins can be traced back millions of years ago. These well-studied enzymes, currently numbering almost 2,800 unique proteins, initially emerged from environmental sources, most likely to protect a producing bacterium from attack by naturally occurring β-lactams. Their ancestors were presumably penicillin-binding proteins that share sequence homology with β-lactamases possessing an active-site serine. Metallo-β-lactamases also exist, with one or two catalytically functional zinc ions. Although penicillinases in Gram-positive bacteria were reported shortly after penicillin was introduced clinically, transmissible β-lactamases that could hydrolyze recently approved cephalosporins, monobactams, and carbapenems later became important in Gram-negative pathogens. Nomenclature is based on one of two major systems. Originally, functional classifications were used, based on substrate and inhibitor profiles. A later scheme classifies β-lactamases according to amino acid sequences, resulting in class A, B, C, and D enzymes. A more recent nomenclature combines the molecular and biochemical classifications into 17 functional groups that describe most β-lactamases. Some of the most problematic enzymes in the clinical community include extended-spectrum β-lactamases (ESBLs) and the serine and metallo-carbapenemases, all of which are at least partially addressed with new β-lactamase inhibitor combinations. New enzyme variants continue to be described, partly because of the ease of obtaining sequence data from whole-genome sequencing studies. Often, these new enzymes are devoid of any phenotypic descriptions, making it more difficult for clinicians and antibiotic researchers to address new challenges that may be posed by unusual β-lactamases.

show abstract

Section: ␤-Lactamases In Gram-negative Bacteriamentioning

confidence: 99%

Past and Present Perspectives on β-Lactamases

Bush

2018

Antimicrob Agents Chemother

636

498

View full text Add to dashboard Cite

show abstract

“…) and the hospital environment (Chouchani et al . ) over the last 5 years, it has not been until very recently when the first carbapenemase‐producing E. coli was detected in pets (Yousfi et al . ) and livestock animals (Braun et al .…”

Section: Esbl Plasmid‐mediated Ampc and Carbapenemase‐producing E Cmentioning

confidence: 99%

“…Considering carbapenemase production among E. coli isolates in the African continent, although many descriptions have been reported in humans (Robin et al 2010;Moquet et al 2011;Barguigua et al 2013;Leski et al 2013;Mushi et al 2014) and the hospital environment (Chouchani et al 2011) over the last 5 years, it has not been until very recently when the first carbapenemaseproducing E. coli was detected in pets (Yousfi et al 2016) and livestock animals (Braun et al 2016). The previously described study, conducted in different dairy cattle farms from Egypt, reported four E. coli strains harbouring bla OXA-48 and one carrying bla OXA-181 carbapenemase genes, all of them phenotypically resistant to meropenem and imipenem.…”

Section: Esbl Plasmid-mediated Ampc and Carbapenemase-producing E Cmentioning

confidence: 99%

Antibiotic resistance in Escherichia coli in husbandry animals: the African perspective

Alonso

Zarazaga

Sallem

et al. 2017

Letters in Applied Microbiology

133

106

View full text Add to dashboard Cite

In the last few years, different surveillances have been published in Africa, especially in northern countries, regarding antimicrobial resistance among husbandry animals. Information is still scarce, but the available data show a worrying picture. Although the highest resistance rates have been described against tetracycline, penicillins and sulphonamides, prevalence of plasmidmediated quinolone resistance genes and extended spectrum b-lactamase (ESBL) are being increasingly reported. Among ESBLs, the CTX-M-1 group was dominant in most African surveys. Within this group, CTX-M-15 was the main variant both in animals and humans, except in Tunisia where CTX-M-1 was more frequently detected among Escherichia coli from poultry. Certain bla CTX-M-15 -harbouring clones (ST131/B2 or ST405/D) are mainly identified in humans, but they have also been reported in livestock species from Tanzania, Nigeria or Tunisia. Moreover, several reports suggest an inter-host circulation of specific plasmids (e.g. bla CTX-M-1 -carrying IncI1/ST3 in Tunisia, IncY-and Incuntypeable replicons co-harbouring qnrS1 and bla CTX-M-15 in Tanzania and the worldwide distributed bla CTX-M-15 -carrying IncF-type plasmids). International trade of poultry meat seems to have contributed to the spread of other ESBL variants, such as CTX-M-14, and clones. Furthermore, first descriptions of OXA-48-and OXA-181-producing E. coli have been recently documented in cattle from Egypt, and the emergent plasmid-mediated colistin resistance mcr-1 gene has been also identified in chickens from Algeria, Tunisia and South Africa. These data reflect the urgent need of a larger regulation in the use of veterinary drugs and the implementation of surveillance programmes in order to decelerate the advance of antimicrobial resistance in this continent.

show abstract

“…While VIM-1-derived enzymes have been reported largely for Enterobacteriaceae from around the world, especially from Greece but also recently from Belgium (4), VIM-2 has been associated mostly with Pseudomonas aeruginosa (32). The occurrence of VIM-2 has nevertheless also been reported for clinical isolates of Enterobacteriaceae from Asia (17,24,39), Mexico (28), Argentina (16), and Tunisia (10). Moreover, a recent report showed the presence of VIM-2 in Enterobacter ludwigii isolated from sewage water of a hospital, highlighting the involvement of environmental bacteria as potential reservoirs for the dissemination of clinically relevant metallo-␤-lactamase resistance genes (37).…”

mentioning

confidence: 99%

Detection and Characterization of VIM-31, a New Variant of VIM-2 with Tyr224His and His252Arg Mutations, in a Clinical Isolate of Enterobacter cloacae

Bogaerts

Bebrone

Huang

et al. 2012

Antimicrob Agents Chemother

View full text Add to dashboard Cite

We report the first description of the metallo-␤-lactamase VIM-31, a new variant of VIM-2 with Tyr224His and His252Arg mutations, in Enterobacter cloacae 11236, which was isolated from blood specimens of a patient with colonic adenocarcinoma in Belgium. bla VIM-31 was found on a class 1 integron located on a self-transferable but not typeable 42-kb plasmid. Compared to values published elsewhere for VIM-2, the purified VIM-31 enzyme showed weaker catalytic efficiency against all the tested betalactam agents (except for ertapenem), resulting from lower k cat (except for ertapenem) and higher K m values for VIM-31. The worldwide spread of metallo-␤-lactamases (i.e., VIM, IMP, and NDM enzymes) in carbapenem-resistant Gram-negative bacteria presently constitutes a major public health issue.So far, 33 distinct bla VIM alleles have been described (www .lahey.org/Studies) for a variety of Gram-negative opportunistic pathogens, but only VIM-1, VIM-2, VIM-4, VIM-7, and VIM-27 enzymes (7,12,15,22,31) have been characterized biochemically and structurally. While VIM-1-derived enzymes have been reported largely for Enterobacteriaceae from around the world, especially from Greece but also recently from Belgium (4), VIM-2 has been associated mostly with Pseudomonas aeruginosa (32). The occurrence of VIM-2 has nevertheless also been reported for clinical isolates of Enterobacteriaceae from Asia (17, 24, 39), Mexico (28), Argentina (16), and Tunisia (10). Moreover, a recent report showed the presence of VIM-2 in Enterobacter ludwigii isolated from sewage water of a hospital, highlighting the involvement of environmental bacteria as potential reservoirs for the dissemination of clinically relevant metallo-␤-lactamase resistance genes (37). In many subclass B1 (e.g., IMP and NDM) and B2 (e.g., CphA) metallo-␤-lactamases, the amino acid at position 224 (a conserved Lys residue), close to the active site, plays an important role in substrate binding (2, 27). In the case of VIM enzymes, Lys224 is not present and is replaced by His224 in VIM-1 and by Tyr224 in VIM-2. The side chains of histidine and tyrosine residues are much shorter than that of a lysine residue, thereby preventing the interaction of these two amino acids with the carboxylate moiety (C 4 or C 3 ) of the substrate. For VIM enzymes, it is hypothesized that Arg228, with its long side chain, may replace Lys224 in interacting with the substrate (15,22).We report here the detection and characterization of VIM-31, a new variant of VIM-2 with Tyr224His and His252Arg mutations, in an Enterobacter cloacae clinical isolate recovered from an elderly patient in Belgium. MATERIALS AND METHODSBacterial strains and antimicrobial susceptibility. Enterobacter cloacae 11236 was recovered in June 2011 from blood culture specimens from a patient hospitalized in Brussels, Belgium. The isolate was identified to the species level by matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS) with a Microflex LT mass spectrometer (Bruker Daltonik GmbH, Leipzi...

show abstract

VIM and IMP metallo-β-lactamases and other extended-spectrum β-lactamases in Escherichia coli and Klebsiella pneumoniae from environmental samples in a Tunisian hospital

Cited by 28 publications

References 21 publications

Past and Present Perspectives on β-Lactamases

Past and Present Perspectives on β-Lactamases

Antibiotic resistance in Escherichia coli in husbandry animals: the African perspective

Detection and Characterization of VIM-31, a New Variant of VIM-2 with Tyr224His and His252Arg Mutations, in a Clinical Isolate of Enterobacter cloacae

Contact Info

Product

Resources

About