Literature DB >> 2783690

Physiological studies of the regulation of beta-lactamase expression in Pseudomonas maltophilia.

S Rosta1, H Mett.   

Abstract

The kinetics of beta-lactamase induction in Pseudomonas maltophilia IID1275/873 were investigated. Upon induction with beta-lactam antibiotics, a correlation was seen between the increase in specific beta-lactamase activity and the generation time, as well as the concentration of inducer in the medium. The specific beta-lactamase activity increased slowly within the first 0.5 generation and then more rapidly; it decreased regularly after about 2 generations of growth in the presence of inducer. This decrease could presumably be attributed to the continuous breakdown of inducer by beta-lactamases in the culture medium. In a chemostat culture with continuous supply of fresh inducer-containing medium, the specific beta-lactamase activity could be stabilized at a high level over several generations. Removal of the beta-lactam after a certain induction time showed that a short exposure of the bacteria to inducer caused induction kinetics comparable to those resulting from continuous exposure of the cells to inducer. The two beta-lactamases of P. maltophilia, L1 and L2, were induced simultaneously under various experimental conditions.

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Year:  1989        PMID: 2783690      PMCID: PMC209612          DOI: 10.1128/jb.171.1.483-487.1989

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  19 in total

1.  Activity of beta-lactam antibiotics against Pseudomonas aeruginosa carrying R plasmids determining different beta-lactamases.

Authors:  G A Jacoby; L Sutton
Journal:  Antimicrob Agents Chemother       Date:  1979-08       Impact factor: 5.191

2.  Acetylornithinase of Escherichia coli: partial purification and some properties.

Authors:  H J VOGEL; D M BONNER
Journal:  J Biol Chem       Date:  1956-01       Impact factor: 5.157

3.  Induction of beta-lactamases in gram-negative bacilli.

Authors:  R Wise; J P Ashby; L J Piddock
Journal:  J Antimicrob Chemother       Date:  1987-11       Impact factor: 5.790

4.  Outer membrane permeability and beta-lactamase content in Pseudomonas maltophilia clinical isolates and laboratory mutants.

Authors:  H Mett; S Rosta; B Schacher; R Frei
Journal:  Rev Infect Dis       Date:  1988 Jul-Aug

5.  A spectrophotometric assay of beta-lactamase action on penicillins.

Authors:  S G Waley
Journal:  Biochem J       Date:  1974-06       Impact factor: 3.857

6.  Mutant of Pseudomonas aeruginosa 18S that synthesizes type Id beta-lactamase constitutively.

Authors:  F Flett; N A Curtis; M H Richmond
Journal:  J Bacteriol       Date:  1976-09       Impact factor: 3.490

7.  Purification and properties of inducible penicillin beta-lactamase isolated from Pseudomonas maltophilia.

Authors:  Y Saino; F Kobayashi; M Inoue; S Mitsuhashi
Journal:  Antimicrob Agents Chemother       Date:  1982-10       Impact factor: 5.191

8.  Penicillin-binding proteins, porins and outer-membrane permeability of carbenicillin-resistant and -susceptible strains of Pseudomonas aeruginosa.

Authors:  D M Livermore
Journal:  J Med Microbiol       Date:  1984-10       Impact factor: 2.472

9.  Comparison of glycine enhancement with cefoxitin induction of class 1 beta-lactamase production in Enterobacter cloacae ATCC 13047.

Authors:  B J Gatus; S M Bell; A S Jimenez
Journal:  J Antimicrob Chemother       Date:  1988-02       Impact factor: 5.790

10.  Interaction of the novel penem CGP 31 608 and its enantiomer with type Id beta-lactamase and penicillin-binding proteins.

Authors:  H Mett; B Schacher; P Schneider; O Zak
Journal:  Eur J Clin Microbiol       Date:  1987-12       Impact factor: 3.267

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  4 in total

1.  Plasmid location and molecular heterogeneity of the L1 and L2 beta-lactamase genes of Stenotrophomonas maltophilia.

Authors:  M B Avison; C S Higgins; C J von Heldreich; P M Bennett; T R Walsh
Journal:  Antimicrob Agents Chemother       Date:  2001-02       Impact factor: 5.191

2.  Induction of L1 and L2 beta-lactamases of Stenotrophomonas maltophilia.

Authors:  Rouh-Mei Hu; Kuang-Jay Huang; Lii-Tzu Wu; Ying-Ju Hsiao; Tsuey-Ching Yang
Journal:  Antimicrob Agents Chemother       Date:  2007-12-17       Impact factor: 5.191

3.  Sequence analysis and enzyme kinetics of the L2 serine beta-lactamase from Stenotrophomonas maltophilia.

Authors:  T R Walsh; A P MacGowan; P M Bennett
Journal:  Antimicrob Agents Chemother       Date:  1997-07       Impact factor: 5.191

Review 4.  Microbiological and clinical aspects of infection associated with Stenotrophomonas maltophilia.

Authors:  M Denton; K G Kerr
Journal:  Clin Microbiol Rev       Date:  1998-01       Impact factor: 26.132

  4 in total

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