Literature DB >> 6841320

Streptococcus faecium ATCC 9790 penicillin-binding proteins and penicillin sensitivity are heavily influenced by growth conditions: proposal for an indirect mechanism of growth inhibition by beta-lactams.

R Fontana, P Canepari, G Satta, J Coyette.   

Abstract

The effects of variations in growth conditions on the penicillin response of Streptococcus faecium ATCC 9790 were studied. Changes in the growth temperature and medium composition were found to cause striking changes in the bacterial generation time, cellular penicillin sensitivity (minimum inhibitory concentration), sensitivity of peptidoglycan synthesis to inhibition by penicillin, rate of autolysis, and labeling pattern of penicillin-binding proteins. However, no constant relationship between these parameters and the minimum inhibitory concentration could be observed. Similar electrophoretic patterns for penicillin-binding proteins were observed in cells grown in different media at the optimal growth temperature. Inhibition of cell division by penicillin in cells grown at this temperature (but not at higher or lower temperatures) caused filamentation of the bacteria. In cells grown in a chemically defined medium at the optimal temperature (but not at temperatures above or below), complete inhibition of cell division was associated with only partial inhibition (34% after 150 min) of peptidoglycan synthesis. It is suggested that the status and physiological importance of individual penicillin-binding proteins in S. faecium are heavily influenced by growth conditions. Depending on the growth conditions, different penicillin-binding proteins may perform the cellular function, indispensible for bacterial growth.

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Year:  1983        PMID: 6841320      PMCID: PMC217545          DOI: 10.1128/jb.154.2.916-923.1983

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


  20 in total

1.  Tolerant response of Streptococcus sanguis to beta-lactams and other cell wall inhibitors.

Authors:  D Horne; A Tomasz
Journal:  Antimicrob Agents Chemother       Date:  1977-05       Impact factor: 5.191

2.  Inhibition of cell division of Escherichia coli by a new synthetic penicillin, piperacillin.

Authors:  K Iida; S Hirata; S Nakamuta; M Koike
Journal:  Antimicrob Agents Chemother       Date:  1978-08       Impact factor: 5.191

3.  A rapid, guantitative, and selective estimation of radioactively labeled peptidoglycan in gram-positive bacteria.

Authors:  D Boothby; L Daneo-Moore; G D Shockman
Journal:  Anal Biochem       Date:  1971-12       Impact factor: 3.365

4.  Penicillin: its basic site of action as an inhibitor of a peptide cross-linking reaction in cell wall mucopeptide synthesis.

Authors:  E M Wise; J T Park
Journal:  Proc Natl Acad Sci U S A       Date:  1965-07       Impact factor: 11.205

5.  Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine.

Authors:  D J Tipper; J L Strominger
Journal:  Proc Natl Acad Sci U S A       Date:  1965-10       Impact factor: 11.205

6.  Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12.

Authors:  B G Spratt
Journal:  Proc Natl Acad Sci U S A       Date:  1975-08       Impact factor: 11.205

7.  Relationship between the latent form and the active form of the autolytic enzyme of Streptococcus faecalis.

Authors:  H M Pooley; G D Shockman
Journal:  J Bacteriol       Date:  1969-11       Impact factor: 3.490

8.  Solubilization and isolation of the membrane-bound DD-carboxypeptidase of Streptococcus faecalis ATCC9790. Properties of the purified enzyme.

Authors:  J Coyette; J M Ghuysen; R Fontana
Journal:  Eur J Biochem       Date:  1978-07-17

9.  Effects of penicillin on macromolecular synthesis and surface growth of a tolerant streptococcus as studied by computer reconstruction methods.

Authors:  M L Higgins; T D McDowell; U B Sleytr; M Mychajlonka; G D Shockman
Journal:  J Bacteriol       Date:  1980-12       Impact factor: 3.490

10.  Autolytic defective mutant of Streptococcus faecalis.

Authors:  J B Cornett; B E Redman; G D Shockman
Journal:  J Bacteriol       Date:  1978-02       Impact factor: 3.490

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  11 in total

1.  Correlation of penicillin-induced lysis of Enterococcus faecium with saturation of essential penicillin-binding proteins and release of lipoteichoic acid.

Authors:  S al-Obeid; L Gutmann; R Williamson
Journal:  Antimicrob Agents Chemother       Date:  1990-10       Impact factor: 5.191

2.  Paradoxical response of Enterococcus faecalis to the bactericidal activity of penicillin is associated with reduced activity of one autolysin.

Authors:  R Fontana; M Boaretti; A Grossato; E A Tonin; M M Lleò; G Satta
Journal:  Antimicrob Agents Chemother       Date:  1990-02       Impact factor: 5.191

3.  Regulation of penicillin-binding protein activity: description of a methicillin-inducible penicillin-binding protein in Staphylococcus aureus.

Authors:  L Rossi; E Tonin; Y R Cheng; R Fontana
Journal:  Antimicrob Agents Chemother       Date:  1985-05       Impact factor: 5.191

Review 4.  Mechanisms of resistance of enterococci to beta-lactam antibiotics.

Authors:  R Fontana; P Canepari; M M Lleò; G Satta
Journal:  Eur J Clin Microbiol Infect Dis       Date:  1990-02       Impact factor: 3.267

5.  Identification of a streptococcal penicillin-binding protein that reacts very slowly with penicillin.

Authors:  R Fontana; R Cerini; P Longoni; A Grossato; P Canepari
Journal:  J Bacteriol       Date:  1983-09       Impact factor: 3.490

6.  Identification of a genetic element (psr) which negatively controls expression of Enterococcus hirae penicillin-binding protein 5.

Authors:  M Ligozzi; F Pittaluga; R Fontana
Journal:  J Bacteriol       Date:  1993-04       Impact factor: 3.490

7.  Transition from resistance to hypersusceptibility to beta-lactam antibiotics associated with loss of a low-affinity penicillin-binding protein in a Streptococcus faecium mutant highly resistant to penicillin.

Authors:  R Fontana; A Grossato; L Rossi; Y R Cheng; G Satta
Journal:  Antimicrob Agents Chemother       Date:  1985-11       Impact factor: 5.191

8.  Streptococcus faecium mutants that are temperature sensitive for cell growth and show alterations in penicillin-binding proteins.

Authors:  P Canepari; M M Lleò; R Fontana; G Satta
Journal:  J Bacteriol       Date:  1987-06       Impact factor: 3.490

9.  Overproduction of a low-affinity penicillin-binding protein and high-level ampicillin resistance in Enterococcus faecium.

Authors:  R Fontana; M Aldegheri; M Ligozzi; H Lopez; A Sucari; G Satta
Journal:  Antimicrob Agents Chemother       Date:  1994-09       Impact factor: 5.191

10.  Bacteriostatic and bactericidal activities of beta-lactams against Streptococcus (Enterococcus) faecium are associated with saturation of different penicillin-binding proteins.

Authors:  M M Lleó; P Canepari; G Cornaglia; R Fontana; G Satta
Journal:  Antimicrob Agents Chemother       Date:  1987-10       Impact factor: 5.191

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