Abstract
Penicillin-resistant and penicillin-tolerant mutants have been isolated from group A streptococci mutagenized by ethyl methane sulfonate. The resistant mutants had an elevated minimal growth inhibitory concentration for benzylpenicillin (minimal inhibitory concentration, 0.2 microgram/ml, as compared with the minimal inhibitory concentration of 0.006 microgram/ml in the penicillin-susceptible parent strain); they also had an abnormal cellular morphology and showed altered penicillin-binding proteins. Penicillin-tolerant mutants were killed more slowly than were the parental cells during treatment with penicillin; they had virtually unchanged minimal inhibitory concentration values for penicillin and normal cellular morphology and penicillin-binding proteins.
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- Allen J. L., Sprunt K. Discrepancy between minimum inhibitory and minimum bactericidal concentrations of penicillin for group A and group B beta-hemolytic streptococci. J Pediatr. 1978 Jul;93(1):69–71. doi: 10.1016/s0022-3476(78)80603-9. [DOI] [PubMed] [Google Scholar]
- Brown D. F., Reynolds P. E. Intrinsic resistance to beta-lactam antibiotics in Staphylococcus aureus. FEBS Lett. 1980 Dec 29;122(2):275–278. doi: 10.1016/0014-5793(80)80455-8. [DOI] [PubMed] [Google Scholar]
- Buchanan C. E., Strominger J. L. Altered penicillin-binding components in penicillin-resistant mutants of Bacillus subtilis. Proc Natl Acad Sci U S A. 1976 Jun;73(6):1816–1820. doi: 10.1073/pnas.73.6.1816. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dougherty T. J., Koller A. E., Tomasz A. Penicillin-binding proteins of penicillin-susceptible and intrinsically resistant Neisseria gonorrhoeae. Antimicrob Agents Chemother. 1980 Nov;18(5):730–737. doi: 10.1128/aac.18.5.730. [DOI] [PMC free article] [PubMed] [Google Scholar]
- EAGLE H. The binding of penicillin in relation to its cytotoxic action. II. The reactivity with penicillin of resistant variants of streptococci, pneumococci, and staphylococci. J Exp Med. 1954 Jul 1;100(1):103–115. doi: 10.1084/jem.100.1.103. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fischetti V. A., Gotschlich E. C., Bernheimer A. W. Purification and physical properties of group C streptococcal phage-associated lysin. J Exp Med. 1971 May 1;133(5):1105–1117. doi: 10.1084/jem.133.5.1105. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Giles A. F., Reynolds R. E. Bacillus megaterium resistance to cloxacillin accompanied by a compensatory change in penicillin binding proteins. Nature. 1979 Jul 12;280(5718):167–168. doi: 10.1038/280167a0. [DOI] [PubMed] [Google Scholar]
- Gutmann L., Williamson R., Tomasz A. Physiological properties of penicillin-binding proteins in group A streptococci. Antimicrob Agents Chemother. 1981 May;19(5):872–880. doi: 10.1128/aac.19.5.872. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hakenbeck R., Tarpay M., Tomasz A. Multiple changes of penicillin-binding proteins in penicillin-resistant clinical isolates of Streptococcus pneumoniae. Antimicrob Agents Chemother. 1980 Mar;17(3):364–371. doi: 10.1128/aac.17.3.364. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Horne D., Hakenbeck R., Tomasz A. Secretion of lipids induced by inhibition of peptidoglycan synthesis in streptococci. J Bacteriol. 1977 Nov;132(2):704–717. doi: 10.1128/jb.132.2.704-717.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Horne D., Tomasz A. Tolerant response of Streptococcus sanguis to beta-lactams and other cell wall inhibitors. Antimicrob Agents Chemother. 1977 May;11(5):888–896. doi: 10.1128/aac.11.5.888. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Horodniceanu T., Bougueleret L., Bieth G. Conjugative transfer of multiple-antibiotic resistance markers in beta-hemolytic group A, B, F, and G streptococci in the absence of extrachromosomal deoxyribonucleic acid. Plasmid. 1981 Mar;5(2):127–137. doi: 10.1016/0147-619x(81)90014-7. [DOI] [PubMed] [Google Scholar]
- Simionescu N., Simionescu M. Galloylglucoses of low molecular weight as mordant in electron microscopy. I. Procedure, and evidence for mordanting effect. J Cell Biol. 1976 Sep;70(3):608–621. doi: 10.1083/jcb.70.3.608. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sprunt K., Redman W., Leidy G. Penicillin resistant alpha Streptococci in pharynx of patients given oral penicillin. Pediatrics. 1968 Dec;42(6):957–968. [PubMed] [Google Scholar]
- TOMASZ A., JAMIESON J. D., OTTOLENGHI E. THE FINE STRUCTURE OF DIPLOCOCCUS PNEUMONIAE. J Cell Biol. 1964 Aug;22:453–467. doi: 10.1083/jcb.22.2.453. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tomasz A. The mechanism of the irreversible antimicrobial effects of penicillins: how the beta-lactam antibiotics kill and lyse bacteria. Annu Rev Microbiol. 1979;33:113–137. doi: 10.1146/annurev.mi.33.100179.000553. [DOI] [PubMed] [Google Scholar]
- Ubukata K., Konno M., Fujii R. Transduction of drug resistance to tetracycline, chloramphenicol, macrolides, lincomycin and clindamycin with phages induced from Streptococcus pyogenes. J Antibiot (Tokyo) 1975 Sep;28(9):681–688. doi: 10.7164/antibiotics.28.681. [DOI] [PubMed] [Google Scholar]
- Zighelboim S., Tomasz A. Penicillin-binding proteins of multiply antibiotic-resistant South African strains of Streptococcus pneumoniae. Antimicrob Agents Chemother. 1980 Mar;17(3):434–442. doi: 10.1128/aac.17.3.434. [DOI] [PMC free article] [PubMed] [Google Scholar]



