Serine-aspartate repeat-containing protein G (SdrG)

Serine-aspartate repeat-containing protein G (SdrG) is a cell-surface adhesin found in certain Gram-positive bacteria such as *Staphylococcus epidermidis* and *Staphylococcus aureus*. It plays a key role in bacterial pathogenesis by binding specifically to the N-terminal region of the B beta-chain of human fibrinogen. This interaction interferes with thrombin-mediated cleavage and release of fibrinopeptide B from fibrinogen. SdrG also mediates weak homophilic bonds between bacterial cells that facilitate biofilm formation on surfaces such as indwelling medical devices. These properties make it an important virulence factor contributing to infection persistence and immune evasion. Experimental studies have shown that peptides derived from β-neurexin can inhibit SdrG-mediated adhesion and biofilm accumulation[5][7].

Other names

SdrGserine-aspartate repeat protein Gserine-aspartate dipeptide repeat protein G

Binds to the N-terminal region of the B beta-chain of human fibrinogen, interfering with thrombin cleavage and release of fibrinopeptide B. Mediates homophilic interactions that promote cell–cell adhesion in biofilms. Can be inhibited by peptides derived from β-neurexin that block its adhesive functions.