Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (11)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Livermore, D. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Livermore, D. M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Journal of Antimicrobial Chemotherapy (1987) 19, 733-742
© 1987 The British Society for Antimicrobial Chemotherapy

research-article

Radiolabelling of penicillin-binding proteins (PBPs) in intact Pseudomonas aeruginosa cells: consequences of ß-lactamase activity by PBP-5

D. M. Livermore

Department of Medical Microbiology, The London Hospital Medical College London El 2AD, England

accepted 22 December 1986

The time-course of labelling of penicillin-binding proteins (PBPs) was compared for intact and sonicated cell preparations of nine Pseudomonas aeruginosa strains, all of which gave identical PBP profiles. Saturation of all the PBPs in cell-sonicates occurred within 2 min of exposure to 35 mg/l 14[C] benzylpenicillin. PBP-5 formed an unstable penicilloyl-complex: the other PBPs formed highly stable complexes. Saturation of PBP-4 in intact cells occurred within 2 min of exposure to the antibiotic, correlating with the high affinity of this protein for penicillin. Labelling of PBPs la, lb and 3 was slow but progressive, suggesting that these proteins were shielded by the permeability barrier(s) of the cell. Labelling of PBP-5 in intact cells achieved 10–20% saturation within 2–10 min of exposure to 35 mg/l 14[C] benzylpenicillin, but did not increase subsequently. This behaviour may indicate the establishment of a steady state between the formation and breakdown of the PBP-5, penicillin complex, suggesting that PBP-5, potentiated by the permeability barrier, functions as a feeble ß-lactamase. Such activity may distort the labelling of other PBPs by reducing the concentration of penicillin in the periplasm, thus invalidating the PBP accessibility experiments that have been recommended as probes of bacterial permeability. The ß-lactamase activity also may be significant in resistance, since Noguchi et al. (Journal of Antibiotics, 1980, 33, 1521–6) have previously associated the loss of PBP-5-ß-lactamase activity with hypersusceptibility to ß-lactams in P. aeruginosa.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Antimicrob. Agents Chemother.Home page
J. B. Bulitta, N. S. Ly, J. C. Yang, A. Forrest, W. J. Jusko, and B. T. Tsuji
Development and Qualification of a Pharmacodynamic Model for the Pronounced Inoculum Effect of Ceftazidime against Pseudomonas aeruginosa
Antimicrob. Agents Chemother., January 1, 2009; 53(1): 46 - 56.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.