Advertisement

Penicillin-Binding Proteins 1A and 3 in Streptococcus Pneumoniae: What are Essential PBP’s?

  • Regine Hakenbeck
  • Heinz Ellerbrok
  • Christiane Martin
  • Gioavanna Morelli
  • Cordelia Schuster
  • Anatol Severin
  • Alex Tomasz
Part of the Federation of European Microbiological Societies Symposium Series book series (FEMS, volume 65)

Abstract

Penicillin-binding proteins (PBPs) exist in every penicillin-susceptible bacterial species. One of the primary steps in the mechanism of action of β-lactams that finally lead to growth inhibition, lysis and death of the cell, is the interaction of penicillin with PBPs, the target enzymes for this group of antibiotics. Penicillin, believed to structurally resemble the actual substrate of PBPs — the C-terminal D-Ala-D-Ala moiety of muropentapeptides — becomes covalently bound to a serine residue located in the active site of all PBPs. This penicilloyl-PBP complex is enzymatically inactive, and therefore correct assembly of the murein layer which is vital for cell growth can no longer be ensured (for review, see Ghuysen, 1991).

Keywords

Streptococcus Pneumoniae Laboratory Mutant Murein Layer Interspecies Recombinational Event Essential PBPs 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Chen, J.-D. and Morrison, D.A. (1988) Construction and properties of a new insertion vector, pJDC9, that is protected by transcriptional terminators and useful for cloning of DNA from Streptococcus pneumoniae. Gene 64, 155–164.PubMedCrossRefGoogle Scholar
  2. Ghuysen, J.-M. (1991) Serine β-lactamases and penicillin-binding proteins. Annu. Rev. Microbiol. 45, 37–67.PubMedCrossRefGoogle Scholar
  3. Laible, G., Spratt, B.G. and Hakenbeck, R. (1991) Interspecies recombinational events during the evolution of altered PBP 2x genes in penicillin-resistant clinical isolates of Streptococcus pneumoniae. Mol. Microbiol. 5, 1993–2002.PubMedCrossRefGoogle Scholar
  4. Laible, G. and Hakenbeck, R. (1987) Penicillin-binding proteins in β-lactam resistant laboratory mutants of Streptococcus pneumoniae. Mol. Microbiol. 1, 355–363.PubMedCrossRefGoogle Scholar
  5. Laitinen, H. and Tomasz, A. (1990) Changes in composition of peptidoglycan during maturation of the cell wall in pneumococcl J. Bacteriol. 172, 5961–5967.Google Scholar
  6. Martin, C, Bliese, T. and Hakenbeck, R. (1992) Nucleotide sequences of genes encoding penicillin binding proteins from Streptococcus pneumoniae and Streptococcus oralis with high homology to Escherichia coli penicillin-binding proteins 1A and IB. J. Bacteriol., in press.Google Scholar
  7. Schuster, C, Dobrinski, B. and Hakenbeck, R. (1990) Unusual septum formation in Streptococcus pneumoniae mutants with an alteration in the D,D-carboxypeptidase penicillin-binding protein 3. J. Bacteriol. 172, 6499–6505.PubMedGoogle Scholar
  8. Spratt, B.G. and Jobanputra, V. (1977) Mutants of Escherichia coli which lack a component of penicillin binding protein 1 are viable. FEMS Lett. 79, 374–378.Google Scholar
  9. Spratt, B.G. (1989) Resistance to β-lactam antibiotics mediated by alterations of penicillin binding proteins, in “Handbook of Experimental Pharmacology” (Bryan, L.E., Ed.) pp 77–100. Springer, Berlin.Google Scholar
  10. Williamson, R., Hakenbeck, R. and Tomasz, A. (1980) In vivo interaction of β-lactam antibiotics wiht the penicillin-binding proteins of Streptococcus pneumoniae. Antimicrob. Agents Chemother. 18, 629–637.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • Regine Hakenbeck
    • 1
  • Heinz Ellerbrok
    • 2
  • Christiane Martin
    • 1
  • Gioavanna Morelli
    • 1
  • Cordelia Schuster
    • 3
  • Anatol Severin
    • 4
  • Alex Tomasz
    • 4
  1. 1.Max-Planck Institut für molekulare GenetikBerlin 33Germany
  2. 2.INSERM U152Institut de Génétique MoléculaireParis CedexFrance
  3. 3.University of WalesBangor, GwyneddUK
  4. 4.Microbiology DepartmentThe Rockefeller UniversityNew YorkUSA

Personalised recommendations