Staphylococcus aureus peptidoglycan pentaglycine interpeptide bridge

The **Staphylococcus aureus peptidoglycan pentaglycine interpeptide bridge** is a unique structural feature of the S. aureus cell wall, consisting of a chain of five glycine residues that links the lysine on one stem peptide to the d-alanine on another, enabling high levels of cross-linking (up to 90%) in the peptidoglycan meshwork. This extensive crosslinking provides S. aureus with mechanical strength to withstand internal turgor, shapes cellular morphology, and serves as a platform for the covalent attachment of surface proteins involved in adhesion and virulence. Genetic or chemical inhibition of pentaglycine bridge formation results in severe defects in cell wall stability, increased susceptibility to β-lactam antibiotics, cell lysis, and impaired viability, highlighting its essential role in bacterial growth, pathogenesis, and antibiotic resistance. The enzymes FemX, FemA, and FemB sequentially add each glycine residue to the bridge, and their activities are essential for bridge formation and, consequently, for S. aureus survival[1][3][4][7][8]. **Note:** This "target" is a structural motif, not a typical macromolecular drug target (such as an enzyme or receptor), but it is considered valid as an antibiotic target due to its essential role in viability and resistance[1].

Other names

Pentaglycine bridge of Staphylococcus aureus peptidoglycanS. aureus pentaglycine interpeptide bridge

Inhibition of bridge synthesis compromises cell wall integrity, leading to cell lysis[1][7] Disrupting cross-linking enhances β-lactam antibiotic susceptibility[1]