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Related Experiment Videos

Penicillin-binding proteins in Streptococcus faecalis and S. faecium.

H Y Chen, J D Williams

    Journal of Medical Microbiology
    |March 1, 1987
    PubMed
    Summary

    Penicillin-binding proteins (PBPs) in Streptococcus species were studied for their role in beta-lactam antibiotic resistance. Lower affinities of specific PBPs in resistant strains correlated with reduced antibiotic sensitivity.

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    Area of Science:

    • Microbiology
    • Biochemistry
    • Pharmacology

    Background:

    • Penicillin-binding proteins (PBPs) are crucial targets for beta-lactam antibiotics.
    • Understanding PBP characteristics is vital for explaining antibiotic resistance mechanisms in bacteria.

    Purpose of the Study:

    • To investigate the penicillin-binding proteins (PBPs) in Streptococcus faecalis and Streptococcus faecium.
    • To correlate PBP affinities for beta-lactam antibiotics with observed resistance levels.

    Main Methods:

    • Autoradiography was used to visualize PBPs in different bacterial strains.
    • Minimum Inhibitory Concentration (MIC) values were compared with PBP affinities for various beta-lactam antibiotics.

    Main Results:

    • Five PBPs were identified in S. faecalis NCTC 775 and six in S. faecium NCTC 7171.
    • PBPs 3 and 4 in S. faecalis, and PBPs 4 and 5 in S. faecium, showed affinities related to antibiotic sensitivity.
    • The highly resistant S. faecium strain 37 exhibited decreased affinities in PBPs 4 and 5, suggesting a role in resistance.

    Conclusions:

    • PBPs 3 and 4 of S. faecalis and PBPs 4 and 5 of S. faecium are likely the primary targets for the tested beta-lactams.
    • Reduced affinities of specific PBPs, particularly PBPs 4 and 5 in S. faecium, contribute significantly to beta-lactam antibiotic resistance.

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