Skip to main content

Molecular Characteristics of the Cell Wall Lytic Enzymes Coded by Pneumococcal Phages

  • Chapter
Bacterial Growth and Lysis

Abstract

The biochemical characteristics of the enzymes postulated to participate in the lysis of Streptococcus pneumonioe infected by phages have been studied in our laboratory in some detail (García et al., 1984, 1987; Romero et al., 1990). Independently of their enzymatic specificity, either amidases or lysozymes, most of the lytic enzymes found in pneumococcus and its bacteriophages share important properties, especially the absolute requirement for choline-containing teichoic acid in cell wall substrate (a peculiar characteristic of the pneumococcal peptidoglycan) for activity (Höltje and Tomasz, 1975). It has been postulated that this choline dependence of the pneumococcal lysins may have served as an element of selective pressure during evolution that should have preserved the structures of these enzymes (García et al., 1988 a).

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 169.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 219.00
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 219.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Bernheimer, H.P. (1977) Lysogeny in pneumococci freshly isolated from man. Science 195, 66–68.

    Article  PubMed  CAS  Google Scholar 

  • Campbell, A. (1988) Phage evolution and speciation. in The bacteriophages (Calendar, R., Ed.), pp. I–I4. Plenum Publishing Corp., New York.

    Google Scholar 

  • Chu, C-P. Kariyama, R., Daneo-Moore, L. and Shockman, G. (1992) Cloning and sequence analysis of the muramidase-2 gene from Enterococcus hirae. J. Bacteriol. 174, 1619–1625.

    PubMed  CAS  Google Scholar 

  • Croux, C. and García, J.L. (1991) Sequence of the lye gene encoding the autolytic lysozyme of Clostridium acetobutylicum ATCC824: comparison with other lytic enzymes. Gene 104,25–31.

    Article  PubMed  CAS  Google Scholar 

  • Diaz, E., Lopez, R. and García, J.L. (1992) EJ-I: a myoviridae, temperate bacteriophage of Streptococcus pneumoniae. Submitted for publication.

    Google Scholar 

  • García, E., García, J.L., García, P., Arrarás, A., Sánchez-Puelles, J. M. and Lopez, R. (1988 a) Molecular evolution of lytic enzymes of Streptococcus pneumoniae and its bacteriophages. Proc. Natl. Acad. Sci. USA. 85, 914–918.

    Article  PubMed  Google Scholar 

  • García, J.L., García, E., Sánchez-Puelles, J.M. and Lopez, R. (1988 b) Identification of a lytic enzyme of Clostridium acetobutylicum that degrades choline-containing pneumococcal cell walls. FEMS Microbiol. Lett. 52, 133–138.

    Article  Google Scholar 

  • García, J.L., García, E., Arrarás A., García, P., Ronda, C. and R. López. (1987) Cloning, purification and biochemical characterization of the pneumococcal bacteriophage Cp-I lysin. J. Virol. 61, 2573–2580.

    PubMed  Google Scholar 

  • García, P., Méndez, E., García, E., Ronda, C. and Lopez, R. (1984) Biochemical characterization of a murein hydrolase induced by bacteriophage Dp-1 in Streptococcus pneumoniae: comparative study between bacteriophage-associated lysin and the host amidase. J. Bacteriol. 159, 793–796.

    PubMed  Google Scholar 

  • García, P., García, J.L., García, E. and Lopez, R. (1986) Nucleotide sequence and expression of the pneumococcal autolysin gene from its own promoter in Escherichia coli. Gene 43, 265–272.

    Article  PubMed  Google Scholar 

  • García, P., García, J.L., García, E., Sánchez-Puelles, J.M. and Lopez, R. (1990) Modular organization of the lytic enzymes of Streptococcus pneumoniae and its bacteriophages. Gene 86, 81–88.

    Article  PubMed  Google Scholar 

  • Höltje, J.V. and Tomasz, A. (1976) Purification of the pneumococcal N-acetylmuramyl-L-alanine amidase to biochemical homogeneity. J. Biol. Chem. 251, 4199–4207.

    PubMed  Google Scholar 

  • Höltje, J.V. and Tomasz, A. (1976) Purification of the pneumococcal N-acetylmuramyl-L-alanine amidase to biochemical homogeneity. J. Biol. Chem. 251, 4199–4207.

    PubMed  Google Scholar 

  • Landy, A. (1989) Dynamic, structural, and regulatory aspects of site-specific recombination. Ann. Rev. Biochem. 58, 913–949.

    Article  PubMed  CAS  Google Scholar 

  • Lee, C.Y. and Buranen, S.L. (1989) Extent of the DNA sequence required in integration if staphylococcal bacteriophage L54a. J. Bacteriol. 171, 1652–1657.

    PubMed  CAS  Google Scholar 

  • Rausch, H. and Lehmann, M. (1991) Structural analysis of the actinophage C3I attachment site. Nucl. Acids Res. 19, 5187–5189.

    Article  PubMed  CAS  Google Scholar 

  • Romero, A., Lopez, R. and García, P. (1990 a) Characterization of the pneumococcal bacteriophage HB-3 amidase: Cloning and expression in Escherichia coli. J. Virol. 64, 137–142.

    PubMed  CAS  Google Scholar 

  • Romero, A., Lopez, R. and García, P. (1990 b) Sequence of the Streptococcus pneumoniae bacteriophage reveals high homology with the mayor host autolysin. J. Bacteriol. 172, 5064–5070.

    PubMed  CAS  Google Scholar 

  • Romero, A., Lopez, R. and García, P. (1992) The insertion site of the temperate phage HB746 is located near the phage remnant in the pneumococcal host chromosome. J. Virol. 66 (in press).

    Google Scholar 

  • Stroynowsky, I.T. (1981) Distribution of bacteriophage 3T homologous deoxyribonucleic acid sequences in Bacillus subtilis 168, related bacteriophages, and other Bacillus species. J. Bacteriol. 148, 91–100.

    Google Scholar 

  • Wang, X., Wilkinson, B.J. and Jayaswal, R.K. (1991) Sequence analysis of a Staphylococcus aureus gene encoding a peptidoglycan hydrolase activity. Gene 102, 105–109.

    Article  PubMed  CAS  Google Scholar 

  • Yother, J. and Briles, D.E. (1992) Structural properties and evolutionary relationships of PspA, a surface protein of Streptococcus pneumoniae, as revealed by sequence analysis. J. Bacteriol. 174, 601–609.

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1993 Springer Science+Business Media New York

About this chapter

Cite this chapter

García, P. et al. (1993). Molecular Characteristics of the Cell Wall Lytic Enzymes Coded by Pneumococcal Phages. In: de Pedro, M.A., Höltje, JV., Löffelhardt, W. (eds) Bacterial Growth and Lysis. Federation of European Microbiological Societies Symposium Series, vol 65. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9359-8_31

Download citation

  • DOI: https://doi.org/10.1007/978-1-4757-9359-8_31

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4757-9361-1

  • Online ISBN: 978-1-4757-9359-8

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics