[Bacterial penicillin-binding proteins as specific targets of beta-lactam-antibiotics and as factors of resistance to antibiotics (author's transl)].
Bacteria contain several isofunctional, beta-lactam sensitive membrane enzymes engaged in the synthesis of cell wall peptidoglycan (peptidoglycan-DD-carboxypeptidases, -transpeptidases, -endopeptidases) as members of sets of even more numerous membrane proteins with specific, high binding-affinity for beta-lactam antibiotics (penicillin-binding proteins, PBPs). Effective inhibition of bacterial growth by beta-lactam antibiotics requires simultaneous inactivation of the essential functions of several PBPs by formation of stable enzyme-antibiotic complexes. Failure to achieve permanent inactivation of all essential targets by a given beta-lactam appears to be another cause of bacterial beta-lactam resistance, in addition to known resistance mechanisms based on action of beta-lactamases and on screening off targets from antibiotic by a penetration barrier. Different groups of beta-lactam antibiotics vary characteristically in their affinity for specific essential PBPs. Combined application of two beta-lactams which complement each other in the inactivation to essential targets is a possibility to overcome resistance of single antibiotics.
D000900:Anti-Bacterial Agents / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism; D010403:Penicillin Resistance; D010406:Penicillins / Q000378:metabolism*; D011485:Protein Binding; D047090:beta-Lactams
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D010406:Penicillins; D047090:beta-Lactams
Penicillinbindeproteine der Bakterien als spezifische Wirkorte der beta-Laktam-Antibiotika und als Faktoren der Antibiotikaresistenz.