A phage-associated murein hydrolase in Streptococcus pneumoniae infected with bacteriophage Dp-1. Academic Article uri icon

Overview

abstract

  • A phage-associated murein hydrolase activity capable of degrading pneumococcal cell walls was isolated and purified to homogeneity from the phage-induced lysate of an autolysis-defective pneumococcal mutant infected with the bacteriophage Dp-1. Some properties of the enzyme resembled those of the wild-type (host) pneumococcal murein hydrolase: cell walls prepared from ethanolamine-grown pneumococci were resistant to the enzyme; the activity was inhibited by the Forssman antigen and was sensitive to proteolytic enzymes. The phage-associated enzyme was not inhibited by antiserum prepared against the purified pneumococcal murein hydrolase; the activity was stimulated by reducing agents and was partially inhibited by cardiolipin. The subunit molecular weight of the phage-associated enzyme was somewhat smaller (31 000) than that of the pneumococcal hydrolase (35 000). This appears to be the first description of a phage-associated murein hydrolase activity in pneumococci.

publication date

  • February 1, 1983

Research

keywords

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

Identity

Scopus Document Identifier

  • 0020695156

Digital Object Identifier (DOI)

  • 10.1099/00221287-129-2-489

PubMed ID

  • 6132961

Additional Document Info

volume

  • 129

issue

  • 2