1887

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 (31000) than that of the pneumococcal hydrolase (35000). This appears to be the first description of a phage-associated murein hydrolase activity in pneumococci.

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/content/journal/micro/10.1099/00221287-129-2-489
1983-02-01
2024-04-26
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References

  1. Briles E. B., Tomasz A. 1973; Pneumococcal Forssman antigen: a choline-containing lipoteichoic acid. Journal of Biological Chemistry 248:6394–6397
    [Google Scholar]
  2. Garcia E., Rojo J. M., Garcia P., Ronda C"LOPEZ, Tomasz A. 1982; Preparation of antiserum against the pneumococcal autolysin-inhibition of autolysin activity and some autolytic processes by the antibody. FEMS Microbiology Letters 14:133–136
    [Google Scholar]
  3. Hill J. R., Wannamaker L. W. 1981; Identification of a lysin associated with a bacteriophage (A25) virulent for Group A streptococci. Journal of Bacteriology 145:696–703
    [Google Scholar]
  4. Höltje J. V., Tomasz A. 1975; Biological effects of lipoteichoic acids. Journal of Bacteriology 124:1023–1027
    [Google Scholar]
  5. Höltje J. V., Tomasz A. 1976; Purification of the pneumococcal N-acetyl-muramyl-l-alanine amidase to biochemical homogeneity. Journal of Biological Chemistry 251:4199–4207
    [Google Scholar]
  6. Lacks S. 1970; Mutants of Diplococcus pneumoniae that lack deoxyribonucleases and other activities possibly pertinent to genetic transformation. Journal of Bacteriology 101:373–383
    [Google Scholar]
  7. Lopez R., Ronda C., Tomasz A., Portoles A. 1977; Properties of “diplophage”: a lipid- containing bacteriophage. Journal of Virology 24:201–210
    [Google Scholar]
  8. Mosser J. L., Tomasz A. 1970; Choline containing teichoic acid as a structural component of pneumococcal cell wall and its role in sensitivity to lysis by an autolytic enzyme. Journal of Biological Chemistry 245:287–298
    [Google Scholar]
  9. Ronda C., Lopez R., Tapia A., Tomasz A. 1977; Role of the pneumococcal autolysin (murein hydrolase) in the release of progeny bacteriophage and in the bacteriophage-induced lysis of the host cells. Journal of Virology 21:366–374
    [Google Scholar]
  10. Tomasz A. 1966; A model for the mechanism controlling the expression of competent state in pneumococcus culture. Journal of Bacteriology 91:1050–1061
    [Google Scholar]
  11. Tomasz A. 1970; Cellular metabolism in genetic transformation of pneumococci: requirement for protein synthesis during induction of competence. Journal of Bacteriology 101:860–871
    [Google Scholar]
  12. Tomasz A. 1979; The mechanism of the irreversible antimicrobial effects of penicillins: how the beta- lactam antibiotics kill and lyse bacteria. Annual Review of Microbiology 33:113–137
    [Google Scholar]
  13. Tomasz A., Waks S. 1975; Mechanism of action of penicillin: triggering of the pneumococcal autolytic enzyme by inhibitors of cell wall synthesis. Proceedings of the National Academy of Sciences of the United States of America 72:4162–4166
    [Google Scholar]
  14. Tomasz A., Westphal M., Briles E. B., Fletcher P. 1975; On the physiological functions of teichoic acids. Journal of Supramolecular Structure 3:1–16
    [Google Scholar]
  15. Weber K., Pringle J. R., Osborn M. 1972; Measurement of molecular weights by electrophoresis on SDS-acrylamide gel. Methods in Enzym- ology 26C:3–27
    [Google Scholar]
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