Literature DB >> 2877048

Mutants of Streptococcus pneumoniae that contain a temperature-sensitive autolysin.

P García, E García, C Ronda, R Lopez, R Z Jiang, A Tomasz.   

Abstract

Two mutants of Streptococcus pneumoniae deficient in autolysin activity produced a protein that showed immunological identity with the N-acetyl-muramyl-L-alanyl-amidase present in the wild-type strain, when tested with antiserum obtained against this enzyme. The protein was produced by the mutant cultures grown either at 37 degrees C or at 30 degrees C, although only the cell extracts obtained at 30 degrees C showed significant cell wall hydrolysing activity. In contrast to the lysis resistance of these bacteria grown at 37 degrees C, mutant cultures grown at 30 degrees C exhibited significant degrees of autolysis when treated with detergent or cell wall inhibitors. Extracts of the mutant cultures contained a cell wall hydrolysing activity that was rapidly inactivated during incubation at 37 degrees C.

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Year:  1986        PMID: 2877048     DOI: 10.1099/00221287-132-5-1401

Source DB:  PubMed          Journal:  J Gen Microbiol        ISSN: 0022-1287


  4 in total

1.  Mechanism of pneumococcal cell wall degradation in vitro and in vivo.

Authors:  J Garcia-Bustos; A Tomasz
Journal:  J Bacteriol       Date:  1989-01       Impact factor: 3.490

2.  Insertional inactivation of the major autolysin gene of Streptococcus pneumoniae.

Authors:  A Tomasz; P Moreillon; G Pozzi
Journal:  J Bacteriol       Date:  1988-12       Impact factor: 3.490

3.  DNA probe for identification of Streptococcus pneumoniae.

Authors:  G Pozzi; M R Oggioni; A Tomasz
Journal:  J Clin Microbiol       Date:  1989-02       Impact factor: 5.948

4.  Functional genomics approach to identifying genes required for biofilm development by Streptococcus mutans.

Authors:  Zezhang T Wen; Robert A Burne
Journal:  Appl Environ Microbiol       Date:  2002-03       Impact factor: 4.792

  4 in total

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