Meropenem permeation through the outer membrane of Pseudomonas aeruginosa can involve pathways other than the OprD porin channel

Chemotherapy. May-Jun 1996;42(3):210-14. doi: 10.1159/000239444.


The outer membrane protein (OMP) OprD is the major channel through which carbapenems permeate the outer membrane of Pseudomonas aeruginosa. In this study, we analyzed the OMP profiles of several P. aeruginosa clinical isolates showing diminished susceptibility to imipenem while remaining susceptible to meropenem. All these isolates lacked OprD or showed a reduced expression of this porin. Susceptibility to meropenem was thus independent of the level of OprD expression, indicating that the antimicrobial could be taken up via an alternative route. The level of expression of OprC (70 kD) was also unrelated to meropenem susceptibility. Nevertheless, OMPs OprF and OprE were expressed by all isolates, suggesting that in the absence of OprD, these porins might be involved in the permeation of meropenem.

MeSH terms

  • Drug Resistance, Microbial
  • Humans
  • Imipenem / pharmacokinetics
  • Imipenem / pharmacology*
  • Meropenem
  • Microbial Sensitivity Tests
  • Porins / analysis*
  • Pseudomonas aeruginosa / chemistry*
  • Pseudomonas aeruginosa / drug effects
  • Pseudomonas aeruginosa / metabolism
  • Thienamycins / pharmacokinetics
  • Thienamycins / pharmacology*


  • Porins
  • Thienamycins
  • OprD protein, Pseudomonas aeruginosa
  • Imipenem
  • Meropenem