Characteristics of a β-Iactamase produced by <i>Clostridium butyricum</i>

Hart, C. A.; Barr, Katie; Makin, T.; Brown, Peter J.; Cooke, R W I

doi:10.1093/jac/10.1.31

Cited by 20 publications

(7 citation statements)

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“…Production of f3-lactamases by other anaerobic bacteria has been less well studied, but enzyme production by Clostridium butyricum [20,21], Clostridium clostridioforme [22], Clostridium ramosum [23], Prevotella, Porphyromonas [24], and Fusobacterium [19,24] has been reported. Although only isolated strains of Clostridium appear to produce 0-lactamases, Prevotella, Porphyromonas, and fusobacteria produce these enzymes more frequently; Jacobs et al [17] and Appelbaum and coworkers [19] reported that 71%, 30%, and 41% of these strains, respectively, were /3-lactamase producers.…”

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confidence: 99%

Antimicrobial Resistance in Anaerobes

Rasmussen

Bush

Tally

1997

Clinical Infectious Diseases

160

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The development of antibiotic resistance in anaerobic bacteria has a tremendous impact on the selection of antimicrobial agents for empirical therapy. Susceptibility studies have documented the emergence of antimicrobial resistance and indicate distinct differences in resistance patterns related to individual hospitals, geographic regions, and antibiotic-prescribing regimens. Resistance to beta-lactam drugs, clindamycin, tetracyclines, and 5-nitroimidazoles (metronidazole) has been observed. The prime mechanism for resistance to beta-lactam agents is the production of beta-lactamases. Resistance to clindamycin is mediated by modification of the ribosome. Tetracycline resistance is mediated by both tetracycline efflux and ribosomal protection. 5-Nitroimidazole resistance appears to be caused by a combination of decreased antibiotic uptake and decreased nitroreductase activity. The level of chloramphenicol susceptibility remains quite high, whereas uniform resistance to aminoglycosides and quinolones is observed. Understanding the mechanisms of resistance is critical for both informed selection of antimicrobial therapy and the design of new antimicrobial agents.

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confidence: 99%

Antimicrobial Resistance in Anaerobes

Rasmussen

Bush

Tally

1997

Clinical Infectious Diseases

160

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“…When the B-lactams were combined with the inhibitors, their geometric mean MICs against the remaining 78 strains were reduced from 4.2 to 150.2 ,ug/ml to 0.2 to 12.9 ,ug/ml. The activity of the P-lactams combined with the P-lactamase inhibitors was significantly greater than that of the ,-lactams alone against all groups except B. fragilis homology group II, with 76 to 100% of the strains susceptible to ampicillin plus inhibitor and .90% susceptible to the other combinations.Although the antimicrobial susceptibility spectrum of anaerobes has remained relatively stable, P-lactamasemediated resistance to penicillin and other P-lactams has been described for species in the Bacteroides fragilis group and for other Bacteroides spp., Fusobacterium nucleatum, and Clostridium butyricum (3,7,15,18,19). Several studies have demonstrated that the ,-lactamase inhibitors clavulanate and sulbactam act synergistically in vitro with ,-lactams against P-lactamase-positive, but not P-lactamase-negative, anaerobic organisms (2,4,5,16,20,21).…”

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confidence: 99%

Comparative activity of beta-lactamase inhibitors YTR 830, clavulanate, and sulbactam combined with beta-lactams against beta-lactamase-producing anaerobes

Appelbaum¹,

Jacobs²,

Spangler³

et al. 1986

Antimicrob Agents Chemother

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The in vitro activities of the P-lactamase inhibitors YTR 830, clavulanate, and sulbactam combined with six P-lactams against 88 ,-lactamase-producing anaerobes were determined. When combined with the ,-lactams, the three ,-lactamase inhibitors showed no synergy against the 10 Bacteroides fragilis homology group II strains. When the B-lactams were combined with the inhibitors, their geometric mean MICs against the remaining 78 strains were reduced from 4.2 to 150.2 ,ug/ml to 0.2 to 12.9 ,ug/ml. The activity of the P-lactams combined with the P-lactamase inhibitors was significantly greater than that of the ,-lactams alone against all groups except B. fragilis homology group II, with 76 to 100% of the strains susceptible to ampicillin plus inhibitor and .90% susceptible to the other combinations.Although the antimicrobial susceptibility spectrum of anaerobes has remained relatively stable, P-lactamasemediated resistance to penicillin and other P-lactams has been described for species in the Bacteroides fragilis group and for other Bacteroides spp., Fusobacterium nucleatum, and Clostridium butyricum (3,7,15,18,19). Several studies have demonstrated that the ,-lactamase inhibitors clavulanate and sulbactam act synergistically in vitro with ,-lactams against P-lactamase-positive, but not P-lactamase-negative, anaerobic organisms (2,4,5,16,20,21). YTR 830 is a new ,-lactamase inhibitor (1) with activity comparable to that of clavulanate and superior to that of sulbactam against ,1-lactamase-producing members of the family Enterobacteriaceae (6, 10). The purpose of this study was to compare the in vitro activities of six P-lactams (ampicillin, ticarcillin, mezlocillin, piperacillin, apalcillin, and cefoperazone) The presence of 3-lactamase was detected by a chromogenic cephalosporin method on growth from enriched blood agar plates by using nitrocefin disks (BBL Microbiology Systems, Cockeysville, Md.), in accordance with standard practice (4, 10). Organisms were stored at -70°C in thioglycolateglycerol (85:15, vol/vol) and were subcultured on enriched blood agar plates before testing.Laboratory reference powders of the following agents were used: ticarcillin and clavulanate (Beecham Laboratories, Bristol, Tenn.); mezlocillin (Miles Laboratories, Inc., West Haven, Conn.); piperacillin (Lederle Laboratories, Pearl River, N.Y.); apalcillin (Wyeth Laboratories, Philadelphia, Pa.); cefoperazone and sulbactam (Pfizer Inc., New York, N.Y.); ampicillin (Bristol-Myers Laboratories, Wallingford, Conn.); cefoxitin (Merck Sharpe & Dohme, West Point, Pa.); and YTR 830 (Taiho Pharmaceuticals, Tokyo, Japan). The powders were dissolved and diluted in accordance with the instructions of the manufacturers, and the potency of the agents was checked by determination of the MICs for quality control strains.Susceptibility testing of the isolates was performed by agar dilution on Wilkins-Chalgren agar (Difco Laboratories, Detroit, Mich.) (14,17). Plates contained serial doubling dilutions of the 3-lactams (ampicillin, 0.125 to 256 ,ug/...

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“…Sykes and Smith classified the enzyme from C. clostridiiformis as class II P-lactamase (26). It has been reported that the substrate profile of the enzyme from C. butyricum resembles that of the enzyme from C. clostridiiformis (2,8). Weinrich and Del Bene, however, stated that the enzyme from C. clostridiiformis was unusual since it was not affected by any of the inhibitors cloxacillin, cefoxitin, and pCMB (29).…”

Section: Discussionmentioning

confidence: 99%

“…Hart et al (8) reported a molecular weight of 80,000, which may represent an aggregated form of the enzyme. The isoelectric point of the purified enzyme was 4.4, and similar values have been reported by other investigators (2,8).…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of a new beta-lactamase from Clostridium butyricum

Kesado

Lindqvist

Hedberg

et al. 1989

Antimicrob Agents Chemother

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A highly penicillin-resistant j-lactamase-producing strain of Clostridium butyricum, strain NBL 3, was isolated. The specific activity of the unpurified ,I-lactamase was 0.29 U/mg of protein. The enzyme was purified 1,130-fold by QAE Zetaprep, Sephacryl S-300, and Mono Q column passages. The purified enzyme was judged homogeneous by sodium dodecyl sulfate gradient gel electrophoresis and fast protein liquid chromatography. The enzyme hydrolyzed phenoxymethylpenicillin, benzylpenicillin, ampicillin, and carbenicillin more rapidly than piperacillin and cephaloridine. Cephalothin, cephalexin, cefoxitin, moxalactam, cefotaxime, and imipenem were only slightly hydrolyzed, at less than 1% the rate for phenoxymethylpenicillin. The enzyme was inhibited by clavulanic acid, sulbactam, tazobactam, and p-chloromercuribenzoate. The molecular weight was determined by gel filtration and sodium dodecyl sulfate gradient gel electrophoresis to be 32,000. The isoelectric point was 4.4. Aspartic acid-asparagine, glutamic acid-glutamine, leucine, lysine, alanine, and serine dominated the amino acid composition.

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Characteristics of a β-Iactamase produced by Clostridium butyricum

Cited by 20 publications

References 0 publications

Antimicrobial Resistance in Anaerobes

Antimicrobial Resistance in Anaerobes

Comparative activity of beta-lactamase inhibitors YTR 830, clavulanate, and sulbactam combined with beta-lactams against beta-lactamase-producing anaerobes

Purification and characterization of a new beta-lactamase from Clostridium butyricum

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