Cellular and Molecular Life Sciences CMLS

, Volume 54, Issue 4, pp 332–340

Resistant penicillin-binding proteins

  • R. Hakenbeck
  • J. Coyette

DOI: 10.1007/s000180050160

Cite this article as:
Hakenbeck, R. & Coyette, J. CMLS, Cell. Mol. Life Sci. (1998) 54: 332. doi:10.1007/s000180050160


Low-affinity penicillin-binding proteins (PBPs), which participate in the β-lactam resistance of several pathogenic bacteria, have different origins. Natural transformation and recombination events with DNA acquired from neighbouring intrinsically resistant organisms are responsible for the appearance of mosaic genes encoding two or three low-affinity PBPs in highly resistant strains of transformable microorganisms such as Neisseria and Streptococcus pneumoniae. Methicillin-resistant Staphylococcus aureus and coagulase-negative staphylococcal strains possess the mecA determinant gene, which probably evolved within the Staphylococcus genus from a closely related and physiologically functional gene that was modified by point mutations. The expression of mecA is either inducible or constitutive. A stable high-level resistant phenotype requires the synthesis of a normally constituted peptidoglycan. Enterococci have a natural low susceptibility to β-lactams related to the presence of an intrinsic low-affinity PBP. Highly resistant enterococcal strains overexpress this PBP and/or reduce its affinity.

Key words. Penicillin-binding protein; penicillin resistance; mosaic genes; Streptococcus pneumoniae; Neisseria gonorrhoeae; Staphylococcus aureus; Enterococcus faecium; Enterococcus hirae.

Copyright information

© Birkhäuser Verlag Basel 1998

Authors and Affiliations

  • R. Hakenbeck
    • 1
  • J. Coyette
    • 2
  1. 1.Institut für Mikrobiologie, Universität Kaiserslautern, Paul-Ehrlich Str., D-67663 Kaiserslautern (Germany), Fax +49 631 205 3799, e-mail: hakenb@rhrk.uni-kl.deDE
  2. 2.Centre d’Ingénierie des Protéines, Université de Liège, Institut de Chimie B6, Sart Tilman, B-4000 Liège (Belgium)BE