Abstract
The binding of 14 structurally diverse beta-lactam antibiotics to penicillin-binding proteins of Staphylococcus aureus and Streptococcus faecalis was studied, and the results were examined in the context of the antibacterial activity of the compounds. Penicillin-binding proteins 1 (molecular weight, 87,000) and 3 (molecular weight, 75,000) of S. aureus and penicillin-binding proteins 1 (molecular weight, 105,000) and 3 (molecular weight, 79,000) of S. faecalis bound beta-lactam antibiotics at concentrations comparable to minimum inhibitory concentrations and might therefore be essential. The low affinity of S. faecalis penicillin-binding proteins, relative to that of S. aureus penicillin-binding proteins, toward most beta-lactam antibiotics is probably responsible for the resistance of the former organism to most of these compounds.
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Selected References
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- Coyette J., Ghuysen J. M., Fontana R. Solubilization and isolation of the membrane-bound DD-carboxypeptidase of Streptococcus faecalis ATCC9790. Properties of the purified enzyme. Eur J Biochem. 1978 Jul 17;88(1):297–305. doi: 10.1111/j.1432-1033.1978.tb12450.x. [DOI] [PubMed] [Google Scholar]
- Curtis N. A., Orr D., Ross G. W., Boulton M. G. 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. Antimicrob Agents Chemother. 1979 Sep;16(3):325–328. doi: 10.1128/aac.16.3.325. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Georgopapadakou N. H., Liu F. Y. Penicillin-binding proteins in bacteria. Antimicrob Agents Chemother. 1980 Jul;18(1):148–157. doi: 10.1128/aac.18.1.148. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kozarich J. W., Strominger J. L. A membrane enzyme from Staphylococcus aureus which catalyzes transpeptidase, carboxypeptidase, and penicillinase activities. J Biol Chem. 1978 Feb 25;253(4):1272–1278. [PubMed] [Google Scholar]
- 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]
- 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]
- Laskey R. A., Mills A. D. Quantitative film detection of 3H and 14C in polyacrylamide gels by fluorography. Eur J Biochem. 1975 Aug 15;56(2):335–341. doi: 10.1111/j.1432-1033.1975.tb02238.x. [DOI] [PubMed] [Google Scholar]
- Sabath L. D., Wheeler N., Laverdiere M., Blazevic D., Wilkinson B. J. A new type of penicillin resistance of Staphylococcus aureus. Lancet. 1977 Feb 26;1(8009):443–447. doi: 10.1016/s0140-6736(77)91941-9. [DOI] [PubMed] [Google Scholar]
- Spratt B. G. Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Proc Natl Acad Sci U S A. 1975 Aug;72(8):2999–3003. doi: 10.1073/pnas.72.8.2999. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Spratt B. G. The mechanism of action of mecillinam. J Antimicrob Chemother. 1977 Jul;3 (Suppl B):13–19. doi: 10.1093/jac/3.suppl_b.13. [DOI] [PubMed] [Google Scholar]
- Suzuki H., Nishimura Y., Hirota Y. On the process of cellular division in Escherichia coli: a series of mutants of E. coli altered in the penicillin-binding proteins. Proc Natl Acad Sci U S A. 1978 Feb;75(2):664–668. doi: 10.1073/pnas.75.2.664. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Toala P., McDonald A., Wilcox C., Finland M. Susceptibility of group D streptococcus (enterococcus) to 21 antibiotics in vitro, with special reference to species differences. Am J Med Sci. 1969 Dec;258(6):416–430. doi: 10.1097/00000441-196912000-00006. [DOI] [PubMed] [Google Scholar]
- Tomasz A., Waks S. Mechanism of action of penicillin: triggering of the pneumococcal autolytic enzyme by inhibitors of cell wall synthesis. Proc Natl Acad Sci U S A. 1975 Oct;72(10):4162–4166. doi: 10.1073/pnas.72.10.4162. [DOI] [PMC free article] [PubMed] [Google Scholar]