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Related Experiment Videos

The penicillin-binding proteins in Streptococcus faecalis ATCC 9790.

J Coyette, J M Ghuysen, R Fontana

    European Journal of Biochemistry
    |September 1, 1980
    PubMed
    Summary

    Streptococcus faecalis ATCC 9790 has seven membrane-bound penicillin-binding proteins with varying stabilities and functions. None of these proteins act as a sole lethal target for beta-lactam antibiotics in living cells.

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    Area of Science:

    • Microbiology
    • Biochemistry

    Background:

    • Streptococcus faecalis ATCC 9790 possesses seven distinct membrane-bound penicillin-binding proteins (PBPs).
    • These PBPs exhibit varying molecular weights, abundance, and stability.
    • Their specificities towards 15 different beta-lactam antibiotics were investigated.

    Purpose of the Study:

    • To characterize the seven membrane-bound penicillin-binding proteins of Streptococcus faecalis ATCC 9790.
    • To determine their stability, molecular weights, and antibiotic specificity.
    • To elucidate the mechanisms of beta-lactam antibiotic interaction and breakdown by these proteins.

    Main Methods:

    • Characterization of PBPs through analysis of molecular weights, abundance, and stability under various conditions.
    • Assessment of specificity profiles using 15 different beta-lactam antibiotics.

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  • Investigation of protein conversion, release, and enzymatic activity, including DD-carboxypeptidase activity and interaction with p-chloromercuribenzoate.
  • Analysis of [14C]benzylpenicillin complex breakdown with specific PBPs.

    • Main Results:

    • Most native PBPs have half-lives exceeding 20 hours, with exceptions like protein 3b (approx. 600 min) and protein 4 (approx. 175 min).
    • Short-lived proteins 4 and 3b spontaneously convert into water-soluble forms (proteins 4 and X, respectively), with release maximized under alkaline conditions.
    • Penicillin-binding protein 6 (a DD-carboxypeptidase) yields a soluble form (protein 6) after trypsin exposure, retaining both enzyme and binding activities, with thiol group involvement suggested.
    • Breakdown of [14C]benzylpenicillin complexes involves enzyme catalysis (protein 1, protein 6) or proteolysis (intermediate proteins), with penicilloate as a likely product for protein 1.

    Conclusions:

    • Penicillin-binding proteins 4 and X are spontaneously released from membranes under alkaline conditions.
    • Penicillin-binding protein 6 exhibits DD-carboxypeptidase activity, with a thiol group crucial for its active center.
    • While some PBPs catalyze benzylpenicillin breakdown, none individually serve as the sole lethal target for beta-lactam antibiotics in Streptococcus faecalis.