Abstract
A mutant of the R plasmid R1 which synthesizes a beta-lactamase with altered kinetic characteristics was isolated. The level of penicillin resistance specified by this plasmid was correctly predicted from the properties of the wild-type R1 according to a simple theoretical model published by Zimmermann and Rosselet (Antimicrob. Agents Chemother. 12:368--372, 1977). The model also accounts for the high level of penicillin resistance specified by the R plasmid RP1.
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Selected References
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- Crowlesmith I., Howe T. G. Characterization of beta-lactamase-deficient (bla) mutants of the R plasmid R1 in Escherichia coli K-12 and comparison with similar mutants of RP1. Antimicrob Agents Chemother. 1980 Nov;18(5):667–674. doi: 10.1128/aac.18.5.667. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Curtis N. A., Brown C., Boxall M., Boulton M. G. Inhibition of Escherichia coli K-12 by beta-lactam antibiotics with poor antibacterial activity: interaction of permeability and intrinsic activity against penicillin-binding proteins. Antimicrob Agents Chemother. 1979 Mar;15(3):332–336. doi: 10.1128/aac.15.3.332. [DOI] [PMC free article] [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]
- Curtis N. A., Richmond M. H. Effect of R-factor-mediated genes on some surface properties of Escherichia coli. Antimicrob Agents Chemother. 1974 Dec;6(6):666–671. doi: 10.1128/aac.6.6.666. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Datta N., Richmond M. H. The purification and properties of a penicillinase whose synthesis is mediated by an R-factor in Escherichia coli. Biochem J. 1966 Jan;98(1):204–209. doi: 10.1042/bj0980204. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Grinsted J., Saunders J. R., Ingram L. C., Sykes R. B., Richmond M. H. Properties of a R factor which originated in Pseudomonas aeruginosa 1822. J Bacteriol. 1972 May;110(2):529–537. doi: 10.1128/jb.110.2.529-537.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
- MALAMY M. H., HORECKER B. L. RELEASE OF ALKALINE PHOSPHATASE FROM CELLS OF ESCHERICHIA COLI UPON LYSOZYME SPHEROPLAST FORMATION. Biochemistry. 1964 Dec;3:1889–1893. doi: 10.1021/bi00900a017. [DOI] [PubMed] [Google Scholar]
- Matthew M., Hedges R. W. Analytical isoelectric focusing of R factor-determined beta-lactamases: correlation with plasmid compatibility. J Bacteriol. 1976 Feb;125(2):713–718. doi: 10.1128/jb.125.2.713-718.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Meynell E., Datta N. The relation of resistance transfer factors to the F-factor (sex-factor) of Escherichia coli K12. Genet Res. 1966 Feb;7(1):134–140. doi: 10.1017/s0016672300009538. [DOI] [PubMed] [Google Scholar]
- Neu H. C., Chou J. Release of surface enzymes in Enterobacteriaceae by osmotic shock. J Bacteriol. 1967 Dec;94(6):1934–1945. doi: 10.1128/jb.94.6.1934-1945.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
- O'Callaghan C., Morris A. Inhibition of beta-lactamases by beta-lactam antibiotics. Antimicrob Agents Chemother. 1972 Dec;2(6):442–448. doi: 10.1128/aac.2.6.442. [DOI] [PMC free article] [PubMed] [Google Scholar]
- PERRET C. J. Iodometric assay of penicillinase. Nature. 1954 Nov 27;174(4439):1012–1013. doi: 10.1038/1741012a0. [DOI] [PubMed] [Google Scholar]
- Richmond M. H., Sykes R. B. The beta-lactamases of gram-negative bacteria and their possible physiological role. Adv Microb Physiol. 1973;9:31–88. doi: 10.1016/s0065-2911(08)60376-8. [DOI] [PubMed] [Google Scholar]
- Samuni A. A direct spectrophotometric assay and determination of Michaelis constants for the beta-lactamase reaction. Anal Biochem. 1975 Jan;63(1):17–26. doi: 10.1016/0003-2697(75)90185-2. [DOI] [PubMed] [Google Scholar]
- Sawai T., Takahashi K., Yamagishi S., Mitsuhashi S. Variant of penicillinase mediated by an R factor in Escherichia coli. J Bacteriol. 1970 Nov;104(2):620–629. doi: 10.1128/jb.104.2.620-629.1970. [DOI] [PMC free article] [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]
- Sutcliffe J. G. Nucleotide sequence of the ampicillin resistance gene of Escherichia coli plasmid pBR322. Proc Natl Acad Sci U S A. 1978 Aug;75(8):3737–3741. doi: 10.1073/pnas.75.8.3737. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sykes R. B., Matthew M. The beta-lactamases of gram-negative bacteria and their role in resistance to beta-lactam antibiotics. J Antimicrob Chemother. 1976 Jun;2(2):115–157. doi: 10.1093/jac/2.2.115. [DOI] [PubMed] [Google Scholar]
- Uhlin B. E., Nordström K. R plasmid gene dosage effects in Escherichia coli K-12: copy mutants of the R plasmic R1drd-19. Plasmid. 1977 Nov;1(1):1–7. doi: 10.1016/0147-619x(77)90003-8. [DOI] [PubMed] [Google Scholar]
- WILKINSON G. N. Statistical estimations in enzyme kinetics. Biochem J. 1961 Aug;80:324–332. doi: 10.1042/bj0800324. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Zimmermann W., Rosselet A. Function of the outer membrane of Escherichia coli as a permeability barrier to beta-lactam antibiotics. Antimicrob Agents Chemother. 1977 Sep;12(3):368–372. doi: 10.1128/aac.12.3.368. [DOI] [PMC free article] [PubMed] [Google Scholar]