Studies on the Mechanism of Intrinsic Resistance to -Lactam Antibiotics in Group D Streptococci Free

Abstract

Six penicillin-binding proteins (PBPs) were detected in clinical isolates of each one of three group D streptococci: and When examined in whole organisms, the PBPs of the most penicillin-resistant species of group D streptococci, generally had lower affinities for the antibiotic than those of (intermediate penicillin resistance), which in turn were of lower affinity than those of (penicillin-sensitive): On the other hand, no quantitative correlation could be established between the binding of penicillin to any one PBP or group of PBPs, and the penicillin MIC value for the corresponding micro-organism. Examination of the amounts of antibiotic bound and the rates of binding to PBPs of equal numbers of protoplasts and whole bacteria of and indicated that there was no permeability barrier to benzylpenicillin in the cell walls of these species. The lower antibacterial effectiveness of cephalothin compared with ampicillin in group D streptococci was paralleled by the higher concentrations of cephalothin needed in competition assays to inhibit the lower molecular size PBPs of these bacteria.

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1983-03-01
2024-03-28
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References

  1. Chase H. A., Fuller C., Reynolds P. E. 1981; The role of penicillin-binding proteins in the action of cephalosporins against Escherichia coli and Salmonella typhimurium . European Journal of Biochemistry 117:301–310
    [Google Scholar]
  2. Coyette J., Ghuysen J., Fontana R. 1978; Solubilization and isolation of the membrane-bound DD-carboxypeptidase of Streptococcus faecalisATCC 9790. European Journal of Biochemistry 88:297–305
    [Google Scholar]
  3. Dougherty T. J., Roller A. E., Tomasz A. 1980; Penicillin-binding proteins of penicillin- susceptible and intrinsically resistant Neisseria gonorrhoeae . Antimicrobial Agents and Chemotherapy 18:730–737
    [Google Scholar]
  4. Facklam R. R. 1972; Recognition of group D streptococcal species of human origin by biochemical and physiological tests. Applied Microbiology 23:1131–1139
    [Google Scholar]
  5. Fontana R., Canepari P., Satta G., Coyette J. 1980; Identification of the lethal target of benzyl- penicillin in Streptococcus faecalis by in vivo penicillin binding studies. Nature; London: 28770–72
    [Google Scholar]
  6. Georgopapadakou N. H., Liu F. Y. 1980a; Penicillin-binding proteins in bacteria. Antimicrobial Agents and Chemotherapy 18:148–157
    [Google Scholar]
  7. Georgopapadakou N. H., Liu F. Y. 1980b; Binding of β-lactam antibiotics to penicillin-binding proteins of Staphylococcus aureus and Streptococcus faecalis: relation to antibacterial activity. Antimicrobial Agents and Chemotherapy 18:834–836
    [Google Scholar]
  8. Gross K. C., Houghton M. P., Senterfit L. B. 1975; Presumptive speciation of Streptococcus bovisand other group D streptococci from human sources by using arginine and pyruvate tests. Journal of Clinical Microbiology 1:54–60
    [Google Scholar]
  9. Gutmann L., Williamson R., Tomasz A. 1981; Physiological properties of penicillin-binding proteins in group A streptococci. Antimicrobial Agents and Chemotherapy 19:872–880
    [Google Scholar]
  10. Hakenbeck R., Tarpay M., Tomasz A. 1980; Multiple changes of penicillin-binding proteins in penicillin-resistant clinical isolates of Streptococcus pneumoniae . Antimicrobial Agents and Chemotherapy 17:364–371
    [Google Scholar]
  11. Hartman B., Tomasz A. 1981; Altered penicillinbinding proteins in methicillin-resistant strains of Staphylococcus aureus . Antimicrobial Agents and Chemotherapy 19:726–735
    [Google Scholar]
  12. Krogstad D. J., Parquette A. R. 1980; Defective killing of enterococci: a common property of antimicrobial agents acting on the cell wall. Antimicrobial Agents and Chemotherapy 17:965–968
    [Google Scholar]
  13. Moellering R. C. Jr 1981; Antimicrobial susceptibility of enterococci: in vitro studies of the action of antibiotics alone and in combination. In Treatment of Infective Endocarditis pp. 81–96 Bisno A. L. Edited by New York: Grune and Stratton;
    [Google Scholar]
  14. Moellering R. C. Jr Watson B. K., Kunz L. J. 1974; Endocarditis due to group D streptococci. American Journal of Medicine 57:239–250
    [Google Scholar]
  15. Moellering R. C. Jr Korzeniowski O. M., Sande M. K., Wennersten C. B. 1979; Species- specific resistance to antimicrobial synergism in Streptococcus faecium and Streptococcus faecalis . Journal of Infectious Diseases 140:203–208
    [Google Scholar]
  16. Siegel J. L., Hurst S. F., Liberman E. S., Coleman S. E., Bleiweis A. S. 1981; Mutanolysin-induced spheroplasts of Streptococcus mutans are true protoplasts. Infection and Immunity 31:808–815
    [Google Scholar]
  17. Smith D. G. 1970; The identity of Streptococcus faecalis ATCC 9790. Journal of Applied Bacteriology 33:474–477
    [Google Scholar]
  18. Thornsberry C., Baker C. N., Facklam R. R. 1974; Antibiotic susceptibility of Streptococcus bovis and other group D streptococci causing endocarditis. Antimicrobial Agents and Chemotherapy 5:228–233
    [Google Scholar]
  19. Toala P., Mcdonald A., Wilcox C., Finland M. 1969; Susceptibility of group D streptococcus (enterococcus) to 21 antibiotics in vitro, with special reference to species differences. American Journal of Medical Science 258:416–430
    [Google Scholar]
  20. Weinstein A. J., Moellering R. C. Jr 1975; Studies of cephalothin: aminoglycoside synergism against enterococci. Antimicrobial Agents and Chemotherapy 7:522–529
    [Google Scholar]
  21. Williamson R., Hakenbeck R., Tomasz A. 1980; The penicillin-binding proteins of Streptococcus pneumoniae grown under lysis-permissive and lysis- protective (tolerant) conditions. FEMS Microbiology Letters 7:127–131
    [Google Scholar]
  22. Zighelboim S., Tomasz A. 1980; Penicillinbinding proteins of multiply antibiotic-resistant South African strains of Streptococcus pneumoniae . Antimicrobial Agents and Chemotherapy 17:434–442
    [Google Scholar]
  23. Zimmerman W. 1980; Penetration of β-lactam antibiotics into their target enzymes in Pseudomonas aeruginosa: comparison of a highly sensitive mutant with its parent strain. Antimicrobial Agents and Chemotherapy 18:94–100
    [Google Scholar]
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