Extracellular adherence protein (Eap) (Eap)

Extracellular adherence protein (Eap) is a multifunctional secreted protein produced by Staphylococcus aureus that plays a critical role in bacterial colonization and immune evasion (Harraghy et al., 2003). It belongs to a class of proteins that lack a covalent cell-wall anchor but re-bind to the bacterial surface and host extracellular matrix components like fibronectin, fibrinogen, and laminin (UniProtKB - P0A0L3). Beyond its role as an adhesin, Eap acts as a potent immunomodulator by blocking the interaction between ICAM-1 and the integrin LFA-1, thereby preventing neutrophil recruitment to the site of infection (Chavakis et al., 2002). It also inhibits the complement system by binding to C3 and C3b, interfering with the formation of C3 convertase (Wiese et al., 2011). Due to its central role in promoting persistent infections and dampening the host immune response, Eap is considered a promising target for anti-virulence therapies, including monoclonal antibodies and small-molecule inhibitors. Research into Eap-targeted therapies aims to restore host immune clearance and prevent the systemic spread of S. aureus.

Other names

MHC class II analog proteinMapp70Eap/Map

Neutralization of Eap-mediated adhesion and inhibition of its immunosuppressive interactions with ICAM-1 and complement factors.