Competition of beta-lactam antibiotics for the penicillin-binding proteins of Pseudomonas aeruginosa, Enterobacter cloacae, Klebsiella aerogenes, Proteus rettgeri, and Escherichia coli: comparison with antibacterial activity and effects upon bacterial morphology
- PMID: 116592
- PMCID: PMC352854
- DOI: 10.1128/AAC.16.3.325
Competition of beta-lactam antibiotics for the penicillin-binding proteins of Pseudomonas aeruginosa, Enterobacter cloacae, Klebsiella aerogenes, Proteus rettgeri, and Escherichia coli: comparison with antibacterial activity and effects upon bacterial morphology
Abstract
The competition of a number of beta-lactam morphogenic probes for the penicillin-binding proteins (PBPs) of Pseudomonas aeruginosa, Enterobacter cloacae, Klebsiella aerogenes, Proteus rettgeri, and Escherichia coli has been studied. The results indicate that the various gram-negative bacteria have similar, but not identical, PBP patterns and that the individual proteins probably perform similar morphogenic functions as in E. coli K-12. Comparison of the 50% binding concentrations of the compounds for the various PBPs of the five strains with their antibacterial activity indicates that the different antibiotics are excluded to a greater or lesser degree by the outer membrane permeability barrier and that the exclusion is most pronounced in P. aeruginosa.
Similar articles
-
Outer membrane permeation of beta-lactam antibiotics in Escherichia coli, Proteus mirabilis, and Enterobacter cloacae.Antimicrob Agents Chemother. 1982 Oct;22(4):585-92. doi: 10.1128/AAC.22.4.585. Antimicrob Agents Chemother. 1982. PMID: 6758687 Free PMC article.
-
[In vitro antibacterial activity of a new parenteral penem, sulopenem].Jpn J Antibiot. 1996 Apr;49(4):324-37. Jpn J Antibiot. 1996. PMID: 8786624 Japanese.
-
[Competitive binding of various beta-lactam compounds to penicillin-binding proteins of Escherichia coli].Antibiot Khimioter. 1989 May;34(5):358-65. Antibiot Khimioter. 1989. PMID: 2662927 Russian.
-
Permeation of beta-lactam antibiotics into Escherichia coli, Pseudomonas aeruginosa, and other gram-negative bacteria.Rev Infect Dis. 1988 Jul-Aug;10(4):691-8. doi: 10.1093/clinids/10.4.691. Rev Infect Dis. 1988. PMID: 3142011 Review.
-
Role of permeability barriers in resistance to beta-lactam antibiotics.Pharmacol Ther. 1985;27(2):197-231. doi: 10.1016/0163-7258(85)90069-5. Pharmacol Ther. 1985. PMID: 2412244 Review. No abstract available.
Cited by
-
Affinities of beta-lactams for penicillin binding proteins of Chlamydia trachomatis and their antichlamydial activities.Antimicrob Agents Chemother. 2001 Jan;45(1):303-5. doi: 10.1128/AAC.45.1.303-305.2001. Antimicrob Agents Chemother. 2001. PMID: 11120983 Free PMC article.
-
Avian Pathogenic Escherichia coli through Pfs Affects the Tran-Scription of Membrane Proteins to Resist β-Lactam Antibiotics.Vet Sci. 2022 Feb 23;9(3):98. doi: 10.3390/vetsci9030098. Vet Sci. 2022. PMID: 35324826 Free PMC article.
-
Harnessing β-Lactam Antibiotics for Illumination of the Activity of Penicillin-Binding Proteins in Bacillus subtilis.ACS Chem Biol. 2020 May 15;15(5):1242-1251. doi: 10.1021/acschembio.9b00977. Epub 2020 Mar 20. ACS Chem Biol. 2020. PMID: 32155044 Free PMC article.
-
Detergent-resistant Streptococcus faecium derivatives that display conditional penicillin lysis.J Bacteriol. 1984 Aug;159(2):805-7. doi: 10.1128/jb.159.2.805-807.1984. J Bacteriol. 1984. PMID: 6565010 Free PMC article.
-
Penicillin-binding proteins of penicillin-susceptible and intrinsically resistant Neisseria gonorrhoeae.Antimicrob Agents Chemother. 1980 Nov;18(5):730-7. doi: 10.1128/AAC.18.5.730. Antimicrob Agents Chemother. 1980. PMID: 6778384 Free PMC article.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials
Miscellaneous