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Enterococcal surface protein (Esp) is a high-molecular-weight, cell wall-associated protein found on the surface of Enterococcus faecalis and Enterococcus faecium. It is primarily encoded on a pathogenicity island and is significantly enriched in clinical isolates, particularly those associated with hospital-acquired infections. Esp plays a critical role in the pathogenesis of enterococcal infections by promoting primary attachment to abiotic surfaces, such as medical devices, and facilitating the formation of robust biofilms. Beyond its structural role in biofilms, Esp has been shown to interact with host cells, enhancing adhesion to epithelial cells and triggering pro-inflammatory responses through the activation of the NF-κB pathway. Due to its prevalence in virulent strains and its contribution to persistent infections, Esp is considered a promising therapeutic target for the development of vaccines and anti-biofilm strategies. While no drugs are currently approved specifically targeting Esp, experimental approaches including monoclonal antibodies and small-molecule inhibitors of its expression are under investigation to combat multidrug-resistant enterococcal infections.
Inhibition of biofilm formation, neutralization of bacterial adhesion to host tissues and abiotic surfaces, and inhibition of Esp gene expression to reduce virulence.
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