Evolution of plasmid-coded resistance to broad-spectrum cephalosporins

Kliebe, Christine; Nies, Berthold; Meyer, Joachim; Tolxdorff-Neutzling, Regina; Wiedemann, B.

doi:10.1128/aac.28.2.302

Cited by 355 publications

(203 citation statements)

References 22 publications

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“…Its substrate affinity for methoxyimino-cephalosporins but not cephamycins led to the assumption that it is another member of the emerging SHV p-lactamase family (Pitton, 1972;Kliebe et al, 1985;Jarlier et al, 1988;BurC et al, 1988;Gutmann et al, 1989); the hybridization and nucleotide sequence data presented above confirm this assumption. The small differences in the nucleotide sequence compared to the established SHV-2 sequence demonstrate that the new enzyme is a variant of this protein.…”

Section: Discussionsupporting

confidence: 52%

“…(1975) using TEM-1, TEM-2, PSE-1, PSE-2,OXA-l, SHV-1 and Enterobacter cloacae P99 chromosomal /. ?-lactamase as PI standards (Kliebe et al, 1985) and nitrocefin for visualization. Determination of specific CTX hydrolysis by single bands from IEF was carried out by cutting slabs containing these bands from the gel, placing them as a whole into the cuvette containing phosphate-buffered saline pH 7.2 and 75 ~M-CTX and performing the assays as described below.…”

Section: Methodsmentioning

confidence: 99%

“…For conjugation experiments a nalidixic-acid-resistant Escherichia coli mutant, W3110 (Kliebe et al, 1985), was used, and for transformation experiments an E. coli HB 101 derivative, DH5a (Gibco BRL). Strains were passaged on DST agar (Oxoid) containing 10 mg CTX 1-1 and 20 mg tobramycin 1-1 in the case of CTXR K .…”

Section: Methodsmentioning

confidence: 99%

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Molecular characterization of a new plasmid-encoded SHV-type -lactamase (SHV-2 variant) conferring high-level cefotaxime resistance upon Klebsiella pneumoniae

Podbielski¹,

Schönling²,

Melzer³

et al. 1991

Journal of General Microbiology

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Between 1986 and 1988, multiresistant Klebsieffa pneumonia strains exhibiting high-level cefotaxime resistance were isolated from patient specimens particularly of the intensive care units of the Aachen Technical University Hospital. The resistance gene responsible was shown to be encoded on a conjugative 66 kb plasmid designated pZMP1. The MIC values for cefotaxime of the original isolates and the transconjugants were > 128 mg 1-l and 64 mg I-', respectively. Isoelectric focusing of protein preparations from the transconjugants showed a p-lactamase with a PI of 7.6. A 3.6 kb BamHI fragment containing the p-lactamase gene was cloned into pLG339 resulting in the recombinant plasmid pZMP1-1. A restriction map of the cloned insert was established and PstI subfragments of the insert were further subcloned into pBGS18. The nucleotide sequence of the complete 3.6 kb fragment was determined. Within 3663 bp an open reading frame of 858 kb was found to show 99 % homology to the SHV-2 and -3 nucleotide sequences. The deduced amino acid sequence differed in one and two positions, respectively, from these established SHV enzymes. The 3' noncoding sequence exhibited nearly perfect homology to that of SHV-2, but the 5' upstream sequence showed homology of less than 50% to the corresponding SHV-2 sequence, indicating an altered promoter region of the variant SHV-enzyme. Kinetic analysis of the p-lactamase revealed a 5&100% elevated hydrolytic effectivity on cefotaxime in comparison to other SHV enzymes. Cefoxitin, ceftazidime, aztreonam and imipenem were not hydrolysed by the enzyme. The variant enzyme was inhibited by commonly available p-lactamase inhibitors. Clavulanic acid had the highest affinity for the enzyme and the greatest effectivity in blocking its action. Based on the genetic and kinetic data we propose to classify the enzyme as a new variant p-lactamase of the SHV-type and name it SHV-2a.

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Section: Discussionsupporting

confidence: 52%

Section: Methodsmentioning

confidence: 99%

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Molecular characterization of a new plasmid-encoded SHV-type -lactamase (SHV-2 variant) conferring high-level cefotaxime resistance upon Klebsiella pneumoniae

Podbielski¹,

Schönling²,

Melzer³

et al. 1991

Journal of General Microbiology

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“…The first N-terminal amino acid degradations each yielded one residue with the sequence Ser-Pro-Gln-Pro-Leu-Glu-. Pure enzyme showed a specific activity of 600 U/mg and behaved as SHV-2 P-lactamase [7] in kinetic constants and analytical isoelectric focusing. The amino acid composition did not differ markedly from that of the SHV-1 protein [lo] and fitted well with that deduced from the amino acid sequence analysis.…”

Section: Resultsmentioning

confidence: 99%

“…The first report of transferrable resistance to cefotaxime in a few bacterial strains was published in 1983 [6]. Two years later, in one of these strains, the involvement of a plasmidmediated &lactamase capable of hydrolyzing cefotaxime and other third-generation cephalosporins was demonstrated [7]. This ,9-lactamase was named SHV-2, as it was closely related to a well-known SHV-1 enzyme, on the basis of biochemical studies and DNA hybridization.…”

Section: Introductionmentioning

confidence: 99%

Single amino acid substitution between SHV‐1 β‐lactamase and cefotaxime‐hydrolyzing SHV‐2 enzyme

et al. 1988

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SHV-2 fi-lactamase was purified from an overproducing variant of a clinical isolate of Escherichia coli resistant to cefotaxime. Pure protein was digested by trypsin and Lys-C endoproteinase. Proteolytic peptides, isolated by reverse-phase HPLC, were submitted to manual Edman degradation and aligned by homology with the sequence of SHV-1 b-lactamase. A putative amino acid sequence was deduced. Structural comparison revealed that SHV-2 differed from SHV-I by only one amino acid, Gly -+ Ser, at position 213 of the mature protein.p-Lactamase; Cefotaxime resistance; Amino acid sequence

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Klebsiella pneumoniae Carbapenemases in Enterobacteriaceae: History, Evolution, and Microbiology Concerns

Rapp

Urban

2012

Pharmacotherapy

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Since the discovery of penicillin 80 years ago, gram-negative bacteria have become proficient at evading the lethal activity of β-lactam antibiotics, principally through the production of β-lactamases. The rapid emergence of penicillinases in both gram-positive and gram-negative bacteria led to the development of cephalosporin β-lactam antibiotics, but production of plasmid-mediated extended-spectrum cephalosporinases (or extended-spectrum β-lactamases) and AmpC enzymes resulted in resistance to this drug class. Because carbapenems were the only β-lactam agents active against such extended-spectrum β-lactamase-producing strains, appropriate and inappropriate use soon resulted in Enterobacteriaceae resistance. As a result, two distinct types of carbapenemases-the metallo-β-lactamases and Klebsiella pneumoniae carbapenemases (KPCs)-were soon identified. The KPCs comprise 10 variants that differ from one another by one to three amino acid substitutions (KPC-2 to KPC-11). The KPC-producing Enterobacteriaceae are not only multidrug resistant but are also difficult to detect routinely in the clinical microbiology laboratory. Tigecycline, polymyxins (colistin and polymyxin B), and aminoglycosides are possible candidate therapies for infections caused by KPC-producing organisms, although well-conducted clinical trials are required to fully define their roles in patient management. The shortage of new antimicrobial agents on the immediate horizon suggests that enhanced adherence with infection prevention procedures and antimicrobial stewardship programs are needed to curb patient-to-patient transmission and to reduce the selection of multidrug-resistant bacteria.

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Evolution of plasmid-coded resistance to broad-spectrum cephalosporins

Cited by 355 publications

References 22 publications

Molecular characterization of a new plasmid-encoded SHV-type -lactamase (SHV-2 variant) conferring high-level cefotaxime resistance upon Klebsiella pneumoniae

Molecular characterization of a new plasmid-encoded SHV-type -lactamase (SHV-2 variant) conferring high-level cefotaxime resistance upon Klebsiella pneumoniae

Single amino acid substitution between SHV‐1 β‐lactamase and cefotaxime‐hydrolyzing SHV‐2 enzyme

Klebsiella pneumoniae Carbapenemases in Enterobacteriaceae: History, Evolution, and Microbiology Concerns

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