Synthesis Of Penicillin-binding Protein Research Articles

Persistent acylation of high-molecular-weight penicillin-binding proteins by penicillin induces the postantibiotic effect in Streptococcus pyogenes.

Penicillin at 10X MIC induced a postantibiotic effect (PAE) of 2.1 h in Streptococcus pyogenes. Progressive increases in the densities of penicillin-binding proteins (PBPs) 1-3 of the bacterium were detected at 30, 60, and 90 min during the postantibiotic phase. The increase in colony-forming units during this phase paralleled the kinetics of incorporation of lysine into proteins, suggesting that growth was triggered by de novo synthesis of PBPs. The question was raised as to whether the progressive increases in densities of PBPs were due to the restoration of preexisting PBPs or to synthesis of new PBPs. With 10X MIC of clindamycin to inhibit PBP synthesis during the postantibiotic phase, the temporal increase in densities of PBPs 1-3 were totally inhibited. These results suggest that the PAE of penicillin in S. pyogenes is caused by irreversible binding of penicillin to PBPs 1-3 and represents the time necessary for synthesis of new PBPs required for normal growth.

Induction of penicillin-binding proteins under catabolite-repressed conditions.

Decoyinine, an inhibitor of GMP synthetase, was used to induce sporulation under catabolite-repressed conditions in Bacillus subtilis. Sporulation-specific penicillin-binding proteins 4* and 5* were produced in abundance, and there was an increase in vegetative penicillin-binding proteins 2B and 3. These results, which were completely blocked by addition of guanosine, suggest that synthesis of penicillin-binding proteins is neither catabolite repressed nor directly dependent on the stringent response.

Synthesis of penicillin-binding proteins in penicillin-treated Streptococcus pneumoniae

Synthesis of penicillin-binding proteins in penicillin-treated Streptococcus pneumoniae

Synthesis of penicillin-binding protein 6 by stationary-phase Escherichia coli.

The level of penicillin-binding protein 6, a D-alanine carboxypeptidase I, was found to be 2- to 10-fold higher in stationary-phase cells than in exponentially growing cells of Escherichia coli. This increase appeared to be due to de novo synthesis rather than to an unmasking of preexisting material. There was no comparable change in the amount of any of the other six penicillin-binding proteins.