Mutants of Streptococcus pneumoniae that contain a temperature-sensitive autolysin. Academic Article uri icon

Overview

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.

publication date

  • May 1, 1986

Research

keywords

  • Amidohydrolases
  • N-Acetylmuramoyl-L-alanine Amidase
  • Streptococcus pneumoniae

Identity

Scopus Document Identifier

  • 0022626478

Digital Object Identifier (DOI)

  • 10.1099/00221287-132-5-1401

PubMed ID

  • 2877048

Additional Document Info

volume

  • 132

issue

  • 5