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  • Sirot, J  (16)
  • 1
    Online Resource
    Online Resource
    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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  • 2
    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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  • 3
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    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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  • 4
    Online Resource
    Online Resource
    Clinical and bacteriological study of nosocomial infections due to Enterobacter aerogenes resistant to imipenem
    American Society for Microbiology ; 1993
    In:  Journal of Clinical Microbiology Vol. 31, No. 1 ( 1993-01), p. 123-127
    Details
    In: Journal of Clinical Microbiology, American Society for Microbiology, Vol. 31, No. 1 ( 1993-01), p. 123-127
    Abstract: Enterobacter aerogenes strains resistant to imipenem were isolated in 10 patients, 7 of whom had received imipenem-cilastatin. The strains were differentiated by biotype, antibiotype, and plasmid content. All of the strains overproduced a chromosomal cephalosporinase and lost a major outer membrane protein with a size of about 40 kDa. In 5 of the 10 patients, E. aerogenes strains resistant to extended-spectrum cephalosporin were isolated during the same stay. In three patients, the similarity between the imipenem-susceptible and -resistant strains suggests the occurrence of mutation and reversion in vivo. The combination imipenem-cilastatin has been critically important for use with multiresistant strains of Enterobacter spp., but its use increases the risk of selection of imipenem-resistant strains.
    Type of Medium: Online Resource
    ISSN: 0095-1137 , 1098-660X
    URL: Article
    DOI: 10.1128/jcm.31.1.123-127.1993
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1993
    detail.hit.zdb_id: 1498353-9
    SSG: 12
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  • 5
    Online Resource
    Online Resource
    R-plasmid-encoded adhesive factor in Klebsiella pneumoniae strains responsible for human nosocomial infections
    American Society for Microbiology ; 1992
    In:  Infection and Immunity Vol. 60, No. 1 ( 1992-01), p. 44-55
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 60, No. 1 ( 1992-01), p. 44-55
    Abstract: Klebsiella pneumoniae strains involved in hospital outbreaks of nosocomial infections, such as suppurative lesions, bacteremia, and septicemia, were resistant to multiple antibiotics including broad-spectrum cephalosporins. Epidemiologic investigations revealed that the reservoir for these K. pneumoniae strains was the gastrointestinal tracts of the patients. The study of the adherence ability of the strains reported here showed that these bacteria adhered to the microvilli of the Caco-2 cell line. This adhesion was mediated by a nonfimbrial protein with a molecular mass of 29,000 Da designated CF29K. Pretreatment of bacteria with antibodies raised against CF29K or Caco-2 cells with purified CF29K prevented the adhesion of K. pneumoniae strains to Caco-2 cells. CF29K immunologically cross-reacted with the CS31A surface protein of Escherichia coli strains involved in septicemia in calves. Genes encoding CF29K were located on a high-molecular-weight conjugative R plasmid, which transferred to E. coli K-12. Transconjugants expressed a large amount of CF29K protein and adhered to the brush border of Caco-2 cells. These findings show that K. pneumoniae strains were able to colonize the human intestinal tract through a plasmid-encoded 29,000-Da surface protein. Hybridization experiments indicated that the gene encoding resistance to broad-spectrum cephalosporins by the production of CAZ-1 enzyme and the gene encoding the adhesive property to intestinal cells were both located on a 20- to 22-kb EcoRI restriction DNA fragment. Genes encoding aerobactin and the ferric aerobactin receptor were also found on this R plasmid.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/iai.60.1.44-55.1992
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1992
    detail.hit.zdb_id: 1483247-1
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  • 6
    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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  • 7
    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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  • 8
    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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  • 9
    Online Resource
    Online Resource
    Resistance to Beta-Lactams in Enterobacteriaceae: Distribution of Phenotypes Related to Beta-Lactamase Production
    SAGE Publications ; 1986
    In:  Journal of International Medical Research Vol. 14, No. 4 ( 1986-07), p. 193-199
    Details
    In: Journal of International Medical Research, SAGE Publications, Vol. 14, No. 4 ( 1986-07), p. 193-199
    Abstract: Phenotypes of susceptibility to amoxycillin (Amo), ticarcillin (Tic), cephalothin (Ctn) were determined in 1366 isolates of Enterobacteriaceae by disk method and beta-lactamases were identified in 243 strains belonging to different phenotypes of amoxycillin-resistant strains. Amo R Tic R Ctn s strains (25%) were penicillinase producers and all of them were susceptible to the combination amoxicillin/clavulanic acid (Amo/CA) and ticarcillin/clavulanic acid (Tic/CA). Amo I/R Tic s Ctn R strains (12%) were cephalosporinase producers and resistance to Amo/CA was observed, except for Proteus vulgaris. Amo R Tic R Ctn R strains (18%) often produced two beta-lactamases (penicillinase and cephalosporinase) and they were resistant to Amo/CA; in this group, susceptibility to Tic/CA depends on the nature and the amount of the beta-lactamase produced, except for Serratia marcescens for which antibiotic resistance is probably due to other mechanisms. Tic/CA resistance was mainly found in Serratia marcescens (41%) and Enterobacter cloacae (36%).
    Type of Medium: Online Resource
    ISSN: 0300-0605 , 1473-2300
    URL: Article
    DOI: 10.1177/030006058601400405
    Language: English
    Publisher: SAGE Publications
    Publication Date: 1986
    detail.hit.zdb_id: 2082422-1
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  • 10
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    Online Resource
    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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