Penicillin-binding protein (PBP) (PBP)

Penicillin-binding proteins (PBPs) in Helicobacter pylori are essential enzymes involved in the synthesis and maintenance of the bacterial cell wall. These proteins, which include PBP1A, PBP2, and PBP3, catalyze the transpeptidation reaction that cross-links peptidoglycan chains, providing the structural integrity necessary for the bacterium to survive the acidic environment of the human stomach (Deloney & Schiller, 2000). PBPs are the primary targets for beta-lactam antibiotics, most notably amoxicillin, which is a key component of first-line eradication therapies for H. pylori infections (Gerrits et al., 2006). The antibiotics act by covalently binding to the active site of the PBPs, thereby inhibiting cell wall assembly and leading to bacterial lysis. Resistance to these treatments is increasingly common and is primarily driven by point mutations in the PBP-encoding genes, particularly pbp1A, which reduce the binding affinity of the antibiotic to the target protein (Rimbara et al., 2008). Understanding the structural and functional variations of these proteins is critical for developing new therapeutic strategies against multi-drug resistant H. pylori strains (Mégraud et al., 2013).

Other names

DD-transpeptidasePeptidoglycan synthasePenicillin-binding protein 1APenicillin-binding protein 2Penicillin-binding protein 3PBP1APBP2PBP3HP0597HP1556HP1565

Inhibition of the transpeptidation step in peptidoglycan synthesis by covalent binding to the active site serine residue, leading to cell wall weakening and bacterial lysis.