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  • Sirot, D  (11)
  • 1
    Online Resource
    Online Resource
    A complex mutant of TEM-1 beta-lactamase with mutations encountered in both IRT-4 and extended-spectrum TEM-15, produced by an Escherichia coli clinical isolate
    American Society for Microbiology ; 1997
    In:  Antimicrobial Agents and Chemotherapy Vol. 41, No. 6 ( 1997-06), p. 1322-1325
    Details
    In: Antimicrobial Agents and Chemotherapy, American Society for Microbiology, Vol. 41, No. 6 ( 1997-06), p. 1322-1325
    Abstract: Escherichia coli GR102 was isolated from feces of a leukemic patient. It expressed different levels of resistance to amoxicillin or ticarcillin plus clavulanate and to the various cephalosporins tested. The double-disk synergy test was weakly positive. Production of a beta-lactamase with a pI of 5.6 was transferred to E. coli HB101 by conjugation. The nucleotide sequence was determined by direct sequencing of the amplification products obtained by PCR performed with TEM gene primers. This enzyme differed from TEM-1 (blaT-1B gene) by four amino acid substitutions: Met-- 〉 Leu-69, Glu-- 〉 Lys-104, Gly-- 〉 Ser-238 and Asn-- 〉 Asp-276. The amino acid susbstitutions Leu-69 and Asp-276 are known to be responsible for inhibitor resistance of the IRT-4 mutant, as are Lys-104 and Ser-238 substitutions for hydrolytic activity of the extended-spectrum beta-lactamases TEM-15, TEM-4, and TEM-3. These combined mutations led to a mutant enzyme which conferred a level of resistance to coamoxiclav (MIC, 64 microg/ml) much lower than that conferred by IRT-4 (MIC, 2,048 microg/ml) but higher than that conferred by TEM-15 or TEM-1 (MIC, 16 microg/ml). In addition, the MIC of ceftazidime for E. coli transconjugant GR202 (1 microg/ml) was lower than that for E. coli TEM-15 (16 microg/ml) and higher than that for E. coli IRT-4 or TEM-1 (0.06 microg/ml). The MICs observed for this TEM-type enzyme were related to the kinetic constants Km and k(cat) and the 50% inhibitory concentration, which were intermediate between those observed for IRT-4 and TEM-15. In conclusion, this new type of complex mutant derived from TEM-1 (CMT-1) is able to confer resistance at a very low level to inhibitors and at a low level to extended-spectrum cephalosporins. CMT-1 received the designation TEM-50.
    Type of Medium: Online Resource
    ISSN: 0066-4804 , 1098-6596
    URL: Article
    DOI: 10.1128/AAC.41.6.1322
    RVK:
    XA 24552
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1997
    detail.hit.zdb_id: 1496156-8
    SSG: 12
    SSG: 15,3
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  • 2
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    First characterization of inhibitor-resistant TEM (IRT) beta-lactamases in Klebsiella pneumoniae strains
    American Society for Microbiology ; 1995
    In:  Antimicrobial Agents and Chemotherapy Vol. 39, No. 11 ( 1995-11), p. 2580-2582
    Details
    In: Antimicrobial Agents and Chemotherapy, American Society for Microbiology, Vol. 39, No. 11 ( 1995-11), p. 2580-2582
    Abstract: Two clinical strains of Klebsiella pneumoniae, TP 01 and TP 02, presented resistance to amoxicillin-clavulanate and were fully susceptible to cephalothin. These strains produced two beta-lactamases, SHV-1 and a TEM enzyme with a pI of 5.2. The previously described changes Arg-244-- 〉 Cys and Arg-244-- 〉 Ser in IRT-1 and IRT-2 (A. Belaaouaj, C. Lapoumeroulie, M. M. Caniça, G. Vedel, P. Nevot, R. Krishnamoorthy, and G. Paul, FEMS Microbiol. Lett. 120:75-80, 1994) were found in TEM enzymes from the TP 01 and TP 02 strains, respectively. This is the first report of inhibitor-resistant TEM (IRT) in species other than Escherichia coli from the family Enterobacteriaceae.
    Type of Medium: Online Resource
    ISSN: 0066-4804 , 1098-6596
    URL: Article
    DOI: 10.1128/AAC.39.11.2580
    RVK:
    XA 24552
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1995
    detail.hit.zdb_id: 1496156-8
    SSG: 12
    SSG: 15,3
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  • 3
    Online Resource
    Online Resource
    Prospective survey of colonization and infection caused by expanded-spectrum-beta-lactamase-producing members of the family Enterobacteriaceae in an intensive care unit
    American Society for Microbiology ; 1989
    In:  Journal of Clinical Microbiology Vol. 27, No. 12 ( 1989-12), p. 2887-2890
    Details
    In: Journal of Clinical Microbiology, American Society for Microbiology, Vol. 27, No. 12 ( 1989-12), p. 2887-2890
    Abstract: The occurrence of expanded-spectrum-beta-lactamase-producing strains was prospectively studied in 56 patients in an intensive care unit. Ten patients were infected or colonized; some of these patients had asymptomatic intestinal colonization. Four different expanded-spectrum beta-lactamases were identified and used as epidemiological markers to survey nosocomial infections.
    Type of Medium: Online Resource
    ISSN: 0095-1137 , 1098-660X
    URL: Article
    DOI: 10.1128/jcm.27.12.2887-2890.1989
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1989
    detail.hit.zdb_id: 1498353-9
    SSG: 12
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  • 4
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    Nucleotide sequences of CAZ-2, CAZ-6, and CAZ-7 beta-lactamase genes
    American Society for Microbiology ; 1992
    In:  Antimicrobial Agents and Chemotherapy Vol. 36, No. 9 ( 1992-09), p. 1817-1820
    Details
    In: Antimicrobial Agents and Chemotherapy, American Society for Microbiology, Vol. 36, No. 9 ( 1992-09), p. 1817-1820
    Abstract: CAZ-2, CAZ-6, and CAZ-7 are plasmid-mediated beta-lactamases that are markedly active against ceftazidime. The corresponding structural genes were amplified by the polymerase chain reaction. Nucleotide sequences were determined by direct sequencing of the amplified products. Analysis of the nucleotide and the deduced amino acid sequences showed that CAZ-2, CAZ-6, and CAZ-7 are derived from TEM-2 by three, four, and two amino acid substitutions, respectively. All these substitutions are located at positions 102, 162, 235, 236, and 237 (Sutcliffe numbering), which are known to extend the substrate range of beta-lactamases. These substitutions are Lys-102, Ser-162, and Ser-236 in CAZ-2; Lys-102, Ser-162, Thr-235, and Lys-237 in CAZ-6; and Lys-102 and His-162 in CAZ-7. These results indicate that the nucleotide sequence of CAZ-2 is identical to that of TEM-8. The nucleotide sequence of CAZ-7 possesses the two mutations described in TEM-16 by the oligotyping method. In contrast, the combination of mutations encountered in CAZ-6 has not yet been described, and this enzyme was designated TEM-24.
    Type of Medium: Online Resource
    ISSN: 0066-4804 , 1098-6596
    URL: Article
    DOI: 10.1128/AAC.36.9.1817
    RVK:
    XA 24552
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1992
    detail.hit.zdb_id: 1496156-8
    SSG: 12
    SSG: 15,3
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  • 5
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    Online Resource
    Identification of CTX-2, a novel cefotaximase from a Salmonella mbandaka isolate
    American Society for Microbiology ; 1991
    In:  Antimicrobial Agents and Chemotherapy Vol. 35, No. 7 ( 1991-07), p. 1498-1500
    Details
    In: Antimicrobial Agents and Chemotherapy, American Society for Microbiology, Vol. 35, No. 7 ( 1991-07), p. 1498-1500
    Abstract: A strain of Salmonella mbandaka isolated from the feces of an Algerian infant showed a reduced susceptibility to cefotaxime (MIC, 8 mg/liter). This strain produced two transferable beta-lactamases of pIs 5.3 and 5.6. The novel beta-lactamase with a pI of 5.3 inhibited by clavulanic acid showed cefotaxime hydrolysis and was therefore designated CTX-2.
    Type of Medium: Online Resource
    ISSN: 0066-4804 , 1098-6596
    URL: Article
    DOI: 10.1128/AAC.35.7.1498
    RVK:
    XA 24552
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1991
    detail.hit.zdb_id: 1496156-8
    SSG: 12
    SSG: 15,3
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  • 6
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    Online Resource
    Sequences of CAZ-3 and CTX-2 extended-spectrum beta-lactamase genes
    American Society for Microbiology ; 1994
    In:  Antimicrobial Agents and Chemotherapy Vol. 38, No. 10 ( 1994-10), p. 2452-2453
    Details
    In: Antimicrobial Agents and Chemotherapy, American Society for Microbiology, Vol. 38, No. 10 ( 1994-10), p. 2452-2453
    Abstract: The nucleotide sequences of blaTEM genes coding for the extended-spectrum beta-lactamases CAZ-3 and CTX-2 were determined. The gene for CAZ-3 is identical to blaTEM-12b. The gene for CTX-2 differs from characterized blaTEM genes for extended-spectrum beta-lactamases by a new combination of already known mutations. We propose for CTX-2 the designation TEM-25.
    Type of Medium: Online Resource
    ISSN: 0066-4804 , 1098-6596
    URL: Article
    DOI: 10.1128/AAC.38.10.2452
    RVK:
    XA 24552
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1994
    detail.hit.zdb_id: 1496156-8
    SSG: 12
    SSG: 15,3
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  • 7
    Online Resource
    Online Resource
    Molecular characterization of nine different types of mutants among 107 inhibitor-resistant TEM beta-lactamases from clinical isolates of Escherichia coli
    American Society for Microbiology ; 1995
    In:  Antimicrobial Agents and Chemotherapy Vol. 39, No. 2 ( 1995-02), p. 427-430
    Details
    In: Antimicrobial Agents and Chemotherapy, American Society for Microbiology, Vol. 39, No. 2 ( 1995-02), p. 427-430
    Abstract: DNA-DNA hybridization and sequencing were performed to determine the molecular basis of resistance to clavulanic acid in 107 inhibitor-resistant TEM (IRT) enzymes produced by Escherichia coli clinical isolates. These beta-lactamases derived from TEM-1 enzyme focused at pI 5.2 (n = 68) or 5.4 (n = 39) and were very poorly inhibited by clavulanic acid compared with TEM-1 enzyme. Results showed that the amino acid sequences of 84 of the 107 enzymes differ from TEM-1 by one or two substitutions previously described: Arg-244-- 〉 Ser (IRT-2) in 22 strains, Met-69-- 〉 Leu (TEM-33) in 17 strains, Met-69-- 〉 Val (TEM-34) in 14 strains, Met-69-- 〉 Ile (IRT-3) in 6 strains, Met-69-- 〉 Leu associated with Asn-276-- 〉 Asp (IRT-4) in 13 strains, and Met-69-- 〉 Val associated with Asn-276-- 〉 Asp (TEM-36) in 12 strains. A new combination, Met-69-- 〉 Ile with Asn-276-- 〉 Asp, was found in 20 strains and was called IRT-8. Two IRT enzymes not previously described were characterized. The substitution Met-69-- 〉 Val associated with a novel substitution Arg-275-- 〉 Leu occurred in one strain. The combination Met-69-- 〉 Leu and Asn-276-- 〉 Asp was associated with the novel substitution Trp-165-- 〉 Arg in two strains. These two novel enzymes were called IRT-9 and IRT-10, respectively. The implication of these novel mutated positions, 165 and 275, in resistance to inactivation by clavulanate was supported by crystallographic data on the TEM-1 enzyme and results of site-directed mutagenesis. Molecular characterization of these mutants showed great diversity among the genes coding for inhibitor-resistant TEM enzymes produced by clinical E. coli isolates.
    Type of Medium: Online Resource
    ISSN: 0066-4804 , 1098-6596
    URL: Article
    DOI: 10.1128/AAC.39.2.427
    RVK:
    XA 24552
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1995
    detail.hit.zdb_id: 1496156-8
    SSG: 12
    SSG: 15,3
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  • 8
    Online Resource
    Online Resource
    Inhibitor-resistant TEM (IRT) beta-lactamases with different substitutions at position 244
    American Society for Microbiology ; 1997
    In:  Antimicrobial Agents and Chemotherapy Vol. 41, No. 11 ( 1997-11), p. 2547-2549
    Details
    In: Antimicrobial Agents and Chemotherapy, American Society for Microbiology, Vol. 41, No. 11 ( 1997-11), p. 2547-2549
    Abstract: A novel inhibitor-resistant TEM (IRT) beta-lactamase was detected in an Escherichia coli isolate resistant to amoxicillin-clavulanate and susceptible to cephalothin. The substrate and inhibitor profiles of this beta-lactamase were similar to those of IRT-1 and IRT-2. The novel IRT's bla gene was sequenced, and the deduced amino acid sequence showed the amino acid replacement Arg for His-244 of the TEM-1 sequence. Substitutions for Arg-244 have been reported in three TEM-1 mutants: IRT-1 (which corresponds to TEM-31) (Cys), IRT-2/TEM-30 (Ser), and TEM-41 (Thr). We designated this novel beta-lactamase, which corresponds to TEM-51, IRT-15.
    Type of Medium: Online Resource
    ISSN: 0066-4804 , 1098-6596
    URL: Article
    DOI: 10.1128/AAC.41.11.2547
    RVK:
    XA 24552
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1997
    detail.hit.zdb_id: 1496156-8
    SSG: 12
    SSG: 15,3
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  • 9
    Online Resource
    Online Resource
    Novel extended-spectrum TEM-type beta-lactamase from an Escherichia coli isolate resistant to ceftazidime and susceptible to cephalothin
    American Society for Microbiology ; 1997
    In:  Antimicrobial Agents and Chemotherapy Vol. 41, No. 3 ( 1997-03), p. 715-716
    Details
    In: Antimicrobial Agents and Chemotherapy, American Society for Microbiology, Vol. 41, No. 3 ( 1997-03), p. 715-716
    Abstract: A novel extended-spectrum TEM-type beta-lactamase was detected in an Escherichia coli isolate which was resistant to ceftazidime and susceptible to cephalothin. The corresponding bla gene was sequenced. The deduced amino acid sequence showed the following three amino acid replacements with respect to the TEM-2 sequence: Glu-- 〉 Lys-104, Arg-- 〉 Ser-164, and Glu-- 〉 Lys-240. Since it confers a ceftazidimase-type resistance phenotype, we propose for this novel enzyme the designation CAZ-9, corresponding to TEM-46 in the sequential numbering scheme of TEM beta-lactamases.
    Type of Medium: Online Resource
    ISSN: 0066-4804 , 1098-6596
    URL: Article
    DOI: 10.1128/AAC.41.3.715
    RVK:
    XA 24552
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1997
    detail.hit.zdb_id: 1496156-8
    SSG: 12
    SSG: 15,3
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  • 10
    Online Resource
    Online Resource
    Translocation of antibiotic resistance determinants including an extended-spectrum beta-lactamase between conjugative plasmids of Klebsiella pneumoniae and Escherichia coli
    American Society for Microbiology ; 1991
    In:  Antimicrobial Agents and Chemotherapy Vol. 35, No. 8 ( 1991-08), p. 1576-1581
    Details
    In: Antimicrobial Agents and Chemotherapy, American Society for Microbiology, Vol. 35, No. 8 ( 1991-08), p. 1576-1581
    Abstract: The extended-spectrum beta-lactamase CAZ-7, derived from TEMs, was produced by two different strains of the family Enterobacteriaceae, Klebsiella pneumoniae and Escherichia coli, isolated from the same patient. Both isolates were resistant to amikacin. In addition, the K. pneumoniae strain was TEM-1 producing and resistant to gentamicin. An E. coli HB101 transconjugant obtained from K. pneumoniae, selected on ceftazidime, showed that CAZ-7 and amikacin resistance were encoded by an 85-kb Inc7 or M plasmid, while an E. coli HB101 transconjugant obtained from E. coli under the same conditions showed that CAZ-7 and amikacin resistance were encoded by a greater than 150-kb Inc6 or C plasmid. Two other E. coli HB101 transconjugants obtained from K. pneumoniae, selected on gentamicin or chloramphenicol, showed that TEM-1 and gentamicin resistance could be encoded either by a greater than 150-kb Inc6 or C plasmid or by an 85-kb Inc7 or M plasmid. It was hypothesized that the genes for beta-lactam and aminoglycoside resistances were located on translocatable sequences. EcoRI digestion and hybridizations obtained with blatem, aacA4, and IS15 probes demonstrated that the CAZ-7 gene, amikacin resistance gene, and IS15 element were clustered on an approximately 20-kb fragment common to 85- and greater than 150-kb plasmids. E. coli HB101 transconjugants from K. pneumoniae and E. coli isolates were used to obtain translocations of CAZ-7 and amikacin resistance and of TEM-1 and gentamicin resistance between the 85- and greater than 150-kb plasmids. This study shows a typical example of in vivo gene dissemination involving transposable elements which translocate multiresistance genes, including an extended-spectrum beta-lactamase.
    Type of Medium: Online Resource
    ISSN: 0066-4804 , 1098-6596
    URL: Article
    DOI: 10.1128/AAC.35.8.1576
    RVK:
    XA 24552
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1991
    detail.hit.zdb_id: 1496156-8
    SSG: 12
    SSG: 15,3
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