Inhibition of the binding of penicillin to the pneumococcal penicillin-binding proteins (PBPs) by exogenous cell wall peptides.
Incubation of pneumococci with D-alanine-containing peptides naturally occurring in peptidoglycan protected cells against lysis and killing by beta-lactam antibiotics near MIC. Such peptides caused decreased binding of the antibiotic to penicillin-binding proteins (PBPs), primarily PBP 2B. This provides direct evidence in vivo for the hypothesis that beta-lactams act as substrate analogues and identifies PBP 2B as a killing target in pneumococci.
Tuomanen
E
E
Rockefeller University, New York, NY 10021.
Sande
S
S
D000409:Alanine / Q000378:metabolism; D001426:Bacterial Proteins; D001667:Binding, Competitive; D002352:Carrier Proteins / Q000378:metabolism*; D002473:Cell Wall; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase / Q000378:metabolism*; D046915:Penicillin-Binding Proteins; D010406:Penicillins / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism*; D010458:Peptidyl Transferases; D013296:Streptococcus pneumoniae / Q000378:metabolism*
D001426:Bacterial Proteins; D002352:Carrier Proteins; D046915:Penicillin-Binding Proteins; D010406:Penicillins; D010455:Peptides; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase; D000409:Alanine