Penicillin-binding proteins and beta-lactam resistance

FEMS Microbiol Rev. 2008 Mar;32(2):361-85. doi: 10.1111/j.1574-6976.2007.00095.x. Epub 2008 Jan 29.


A number of ways and means have evolved to provide resistance to eubacteria challenged by beta-lactams. This review is focused on pathogens that resist by expressing low-affinity targets for these antibiotics, the penicillin-binding proteins (PBPs). Even within this narrow focus, a great variety of strategies have been uncovered such as the acquisition of an additional low-affinity PBP, the overexpression of an endogenous low-affinity PBP, the alteration of endogenous PBPs by point mutations or homologous recombination or a combination of the above.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Anti-Bacterial Agents / pharmacology
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Enterococcus / drug effects
  • Molecular Sequence Data
  • Mutation
  • Neisseria / drug effects
  • Penicillin-Binding Proteins / chemistry*
  • Penicillin-Binding Proteins / classification
  • Penicillin-Binding Proteins / genetics
  • Penicillin-Binding Proteins / metabolism*
  • Sequence Alignment
  • Staphylococcus aureus / drug effects
  • Streptococcus pneumoniae / drug effects
  • beta-Lactam Resistance*
  • beta-Lactams / pharmacology


  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Penicillin-Binding Proteins
  • beta-Lactams