1887

Abstract

Summary

Penicillin-binding proteins (PBPs) of NCTC 775, NCTC 7171 and an isolate of (strain 37) highly resistant to β-lactam antibiotics were visualised by autoradiography. Five PBPs were detected in NCTC 775 and six in NCTC 7171. Additional PBPs could not be found in the resistant isolate of

The PBP affinities of β lactams were compared with MIC values. The affinities of PBPs 3 and 4 of NCTC 775 for penicillin G, ampicillin, cefathiamidine, cephaloridine and cephazolin were related to the sensitivity of the strain to these antibiotics as were the affinities of PBPs 4 and 5 in each strain for the β lactams. It is postulated that PBPs 3 and 4 of NCTC 775 and PBPs 4 and 5 of are the relevant target enzymes of the test antibiotics. PBPs 4 and 5 of the highly β-lactam-resistant strain 37 showed proportionally low affinities for the five β lactams compared to that of the less resistant strain NCTC 7171. Decreased affinities of PBPs 4 and 5 may account for the resistance in strain 37 to β lactams. The affinities for PBP 1, 2 and 5 in NCTC 775 and PBPs 1, 2, 3 and 6 in were not related to the antibiotic sensitivities.

Loading

Article metrics loading...

/content/journal/jmm/10.1099/00222615-23-2-141
1987-03-01
2022-05-29
Loading full text...

Full text loading...

/deliver/fulltext/jmm/23/2/medmicro-23-2-141.html?itemId=/content/journal/jmm/10.1099/00222615-23-2-141&mimeType=html&fmt=ahah

References

  1. Blumberg P. M., Strominger J. L. 1974; Interaction of penicillin with the bacterial cell: 3 penicillin-binding proteins and penicillin-sensitive enzymes. Bacteriological Reviews 38:291–35
    [Google Scholar]
  2. Boulton M. G., Orr D. C. 1983; Detection of bacterial penicillinbinding proteins and their role in the interpretation of the role of action of beta-lactam antibiotics. In Russell A. D., Quesnal L. B. (eds) Antibiotics: assessment of antimicrobial activity and resistance. Academic Press; London: pp 161–182
    [Google Scholar]
  3. Chen H. Y., Williams J. D. 1983; The killing effects of cefathiamidine or ampicillin alone and in combination with gentamicin against enterococci. Journal of Antimicrobial Chemotherapy 12:19–26
    [Google Scholar]
  4. Eliopoulos G. M., Wennersten C., Moellering R. C. 1982; Resistance to beta-lactam antibiotics in Streptococcus faecium. Antimicrobial Agents and Chemotherapy 22:295–301
    [Google Scholar]
  5. Fontana R., Cerini R., Longoni P., Grossato A., Canepari P. 1983; Identification of a streptococcal penicillin-binding protein that reacts very slowly with penicillin. Journal of Bacteriology 155:1343–1350
    [Google Scholar]
  6. Fontana R., Grossato A., Rossi L., Cheng Y. R., Satta G. 1985; Transmission from resistance to hypersusceptibility to beta- lactam antibiotics associated with loss of a low-affinity penicillin-binding protein in a Streptococcus faecium mutant highly resistant to penicillin. Antimicrobial Agents and Chemotherapy 28:678–683
    [Google Scholar]
  7. Georgopapadakou N. H., Liu F. Y. 1980a; Penicillin-binding proteins in bacteria. Antimicrobial Agents and Chemotherapy 18:148–157
    [Google Scholar]
  8. Georgopapadakou N. H., Liu F. Y. 1980b; Binding of beta-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]
  9. 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]
  10. Hayes M. V., Curtis N. A. C., Wyke A. W., Ward J. B. 1981; Decreased affinity of a penicillin-binding protein for beta-lactam antibiotics in a clinical isolate of Staphylococcus aureus resistant to methicillin. FEMS Microbiology letters 10:119–122
    [Google Scholar]
  11. Huff E., Oxley H., Silverman C. S. 1964; Density-gradient patterns of Staphylococcus aureus cells and cell walls during growth and mechanical disruption. Journal of Bacteriology 88:1155–1162
    [Google Scholar]
  12. Matthew M., Harris A. M. 1976; Identification of beta-lactamases by analytical isoelectric focusing: correlation with bacterial taxonomy. Journal of General Microbiology 94:55–67
    [Google Scholar]
  13. Murray B. E., Mederski-Samaroj B. 1983; xTransferable beta- lactamase. A new mechanism for in-vitro penicillin resistance in Streptococcus faecalis. Journal of Clinical Investigation 72:1168–1171
    [Google Scholar]
  14. Nikaido H. 1981; Outer membrane permeability of bacteria: resistance and accessibility of targets. In Salton M. R. J., Shockman G. D. (eds) Beta-lactam antibiotics: mode of action, new developments and future prospects. Academic Press; New York: pp 249–260
    [Google Scholar]
  15. Spratt B. G. 1983; Penicillin-binding proteins and the future of beta-lactam antibiotics. Journal of General Microbiology 129:1247–1260
    [Google Scholar]
  16. Spratt B. G., Pardee A. B. 1975; Penicillin-binding proteins and cell shape in E. coli. Nature 254:516–517
    [Google Scholar]
  17. Strominger J. L., Willoughby E., Kamiryo T., Blumberg P. M., Yocum R. R. 1974; Penicillin-sensitive enzymes and penicillin-binding components in bacterial cells. Annals of the New York Academy of Sciences 235:210–224
    [Google Scholar]
  18. Ubukata K., Yamashita N., Konno M. 1985; Occurrence of a beta- lactam-inducible penicillin-binding protein in methicillin- resistant Staphylococci. Antimicrobial Agents and Chemotherapy 27:851–857
    [Google Scholar]
  19. Williamson R., Calderwood S. B., Moellering R. C., Tomasz A. 1983; Studies on the mechanism of intrinsic resistance to beta-lactam antibiotics in Group D streptococci. Journal of General Microbiology 129:813–822
    [Google Scholar]
  20. Wyke A. W., Ward J. B., Hayes M. V. 1982; Synthesis of peptidoglycan in vivo in methicillin-resistant Staphylococcus aureus. European Journal of Biochemistry 127:553–558
    [Google Scholar]
  21. Zighelboim S., Tomasz A. 1980; Penicillin-binding proteins of multiply antibiotic-resistant South African strains of Streptococcus pneumoniae. Antimicrobial Agents and Chemotherapy 17:434–442
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jmm/10.1099/00222615-23-2-141
Loading
/content/journal/jmm/10.1099/00222615-23-2-141
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error