Skip to main content
PMC home page
Antimicrobial Agents and Chemotherapy logoLink to Antimicrobial Agents and Chemotherapy
. 1997 Sep;41(9):2013–2015. doi: 10.1128/aac.41.9.2013

Penicillin-binding proteins and induction of AmpC beta-lactamase.

C C Sanders 1, P A Bradford 1, A F Ehrhardt 1, K Bush 1, K D Young 1, T A Henderson 1, W E Sanders Jr 1
PMCID: PMC164055  PMID: 9303404

Abstract

In competition assays for radiolabeled penicillin, penicillin-binding proteins (PBPs) 4, 7a, and 7b showed very high affinities for strong inducers of AmpC beta-lactamase. Loss of PBP 4 resulted in diminished inducibility. This suggests that if PBPs are involved in induction of AmpC beta-lactamase, there is probably a redundancy in function among the different PBPs.

Full Text

The Full Text of this article is available as a PDF (197.6 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Dietz H., Pfeifle D., Wiedemann B. Location of N-acetylmuramyl-L-alanyl-D-glutamylmesodiaminopimelic acid, presumed signal molecule for beta-lactamase induction, in the bacterial cell. Antimicrob Agents Chemother. 1996 Sep;40(9):2173–2177. doi: 10.1128/aac.40.9.2173. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Dietz H., Wiedemann B. The role of N-actylglucosaminyl-1,6 anhydro N-acetylmuramyl-L-alanyl-D-glutamyl-meso-diaminopimelic acid-D-alanine for the induction of beta-lactamase in Enterobacter cloacae. Zentralbl Bakteriol. 1996 Jul;284(2-3):207–217. doi: 10.1016/s0934-8840(96)80096-x. [DOI] [PubMed] [Google Scholar]
  3. Fellay R., Frey J., Krisch H. Interposon mutagenesis of soil and water bacteria: a family of DNA fragments designed for in vitro insertional mutagenesis of gram-negative bacteria. Gene. 1987;52(2-3):147–154. doi: 10.1016/0378-1119(87)90041-2. [DOI] [PubMed] [Google Scholar]
  4. Henderson T. A., Dombrosky P. M., Young K. D. Artifactual processing of penicillin-binding proteins 7 and 1b by the OmpT protease of Escherichia coli. J Bacteriol. 1994 Jan;176(1):256–259. doi: 10.1128/jb.176.1.256-259.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Henderson T. A., Templin M., Young K. D. Identification and cloning of the gene encoding penicillin-binding protein 7 of Escherichia coli. J Bacteriol. 1995 Apr;177(8):2074–2079. doi: 10.1128/jb.177.8.2074-2079.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Höltje J. V., Kopp U., Ursinus A., Wiedemann B. The negative regulator of beta-lactamase induction AmpD is a N-acetyl-anhydromuramyl-L-alanine amidase. FEMS Microbiol Lett. 1994 Sep 15;122(1-2):159–164. doi: 10.1111/j.1574-6968.1994.tb07159.x. [DOI] [PubMed] [Google Scholar]
  7. Jacobs C., Huang L. J., Bartowsky E., Normark S., Park J. T. Bacterial cell wall recycling provides cytosolic muropeptides as effectors for beta-lactamase induction. EMBO J. 1994 Oct 3;13(19):4684–4694. doi: 10.1002/j.1460-2075.1994.tb06792.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Jacobs C., Joris B., Jamin M., Klarsov K., Van Beeumen J., Mengin-Lecreulx D., van Heijenoort J., Park J. T., Normark S., Frère J. M. AmpD, essential for both beta-lactamase regulation and cell wall recycling, is a novel cytosolic N-acetylmuramyl-L-alanine amidase. Mol Microbiol. 1995 Feb;15(3):553–559. doi: 10.1111/j.1365-2958.1995.tb02268.x. [DOI] [PubMed] [Google Scholar]
  9. Korat B., Mottl H., Keck W. Penicillin-binding protein 4 of Escherichia coli: molecular cloning of the dacB gene, controlled overexpression, and alterations in murein composition. Mol Microbiol. 1991 Mar;5(3):675–684. doi: 10.1111/j.1365-2958.1991.tb00739.x. [DOI] [PubMed] [Google Scholar]
  10. Korfmann G., Sanders C. C., Moland E. S. Altered phenotypes associated with ampD mutations in Enterobacter cloacae. Antimicrob Agents Chemother. 1991 Feb;35(2):358–364. doi: 10.1128/aac.35.2.358. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Korfmann G., Sanders C. C. ampG is essential for high-level expression of AmpC beta-lactamase in Enterobacter cloacae. Antimicrob Agents Chemother. 1989 Nov;33(11):1946–1951. doi: 10.1128/aac.33.11.1946. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kulakauskas S., Wikström P. M., Berg D. E. Efficient introduction of cloned mutant alleles into the Escherichia coli chromosome. J Bacteriol. 1991 Apr;173(8):2633–2638. doi: 10.1128/jb.173.8.2633-2638.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  14. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  15. Lederberg E M, Lederberg J. Genetic Studies of Lysogenicity in Escherichia Coli. Genetics. 1953 Jan;38(1):51–64. doi: 10.1093/genetics/38.1.51. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Lindberg F., Lindquist S., Normark S. Inactivation of the ampD gene causes semiconstitutive overproduction of the inducible Citrobacter freundii beta-lactamase. J Bacteriol. 1987 May;169(5):1923–1928. doi: 10.1128/jb.169.5.1923-1928.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Lindberg F., Normark S. Common mechanism of ampC beta-lactamase induction in enterobacteria: regulation of the cloned Enterobacter cloacae P99 beta-lactamase gene. J Bacteriol. 1987 Feb;169(2):758–763. doi: 10.1128/jb.169.2.758-763.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Lindquist S., Lindberg F., Normark S. Binding of the Citrobacter freundii AmpR regulator to a single DNA site provides both autoregulation and activation of the inducible ampC beta-lactamase gene. J Bacteriol. 1989 Jul;171(7):3746–3753. doi: 10.1128/jb.171.7.3746-3753.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Lindquist S., Weston-Hafer K., Schmidt H., Pul C., Korfmann G., Erickson J., Sanders C., Martin H. H., Normark S. AmpG, a signal transducer in chromosomal beta-lactamase induction. Mol Microbiol. 1993 Aug;9(4):703–715. doi: 10.1111/j.1365-2958.1993.tb01731.x. [DOI] [PubMed] [Google Scholar]
  20. Romeis T., Höltje J. V. Penicillin-binding protein 7/8 of Escherichia coli is a DD-endopeptidase. Eur J Biochem. 1994 Sep 1;224(2):597–604. doi: 10.1111/j.1432-1033.1994.00597.x. [DOI] [PubMed] [Google Scholar]
  21. Spratt B. G. Properties of the penicillin-binding proteins of Escherichia coli K12,. Eur J Biochem. 1977 Jan;72(2):341–352. doi: 10.1111/j.1432-1033.1977.tb11258.x. [DOI] [PubMed] [Google Scholar]
  22. Vieira J., Messing J. The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene. 1982 Oct;19(3):259–268. doi: 10.1016/0378-1119(82)90015-4. [DOI] [PubMed] [Google Scholar]
  23. Yang Y., Bhachech N., Bush K. Biochemical comparison of imipenem, meropenem and biapenem: permeability, binding to penicillin-binding proteins, and stability to hydrolysis by beta-lactamases. J Antimicrob Chemother. 1995 Jan;35(1):75–84. doi: 10.1093/jac/35.1.75. [DOI] [PubMed] [Google Scholar]

Articles from Antimicrobial Agents and Chemotherapy are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES