Enterococcus surface protein (Esp) (Esp)

Enterococcus surface protein (Esp) is a high-molecular-weight, cell-wall-associated protein primarily found in pathogenic strains of Enterococcus faecalis and Enterococcus faecium (UniProt Q9L9N1). It belongs to the MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules) family and is characterized by a large N-terminal domain followed by a series of tandem repeats (Sillanpää et al., 2004, PubMed: 15150608). Esp plays a critical role in the pathogenesis of enterococcal infections by promoting primary attachment to host surfaces and facilitating the development of complex biofilm structures, which protect the bacteria from host immune responses and antibiotic treatment (Toledo-Arana et al., 2001, PubMed: 11544235). The presence of the esp gene is strongly correlated with clinical isolates from urinary tract infections and endocarditis, often residing on a pathogenicity island (Shankar et al., 1999, PubMed: 10411911). As a therapeutic target, Esp is being investigated for the development of vaccines and monoclonal antibodies aimed at neutralizing its adhesive properties and preventing biofilm-associated chronic infections (He et al., 2008, PubMed: 18621124). Targeting Esp offers a strategy to reduce the virulence of multidrug-resistant enterococci without necessarily killing the bacteria, thereby exerting less selective pressure for resistance. This approach is particularly relevant given the increasing prevalence of vancomycin-resistant enterococci (VRE) in healthcare settings.

Other names

EspEnterococcal surface proteinSurface protein EspEsp protein

Inhibition of bacterial adhesion to host tissues and disruption of biofilm architecture by targeting the N-terminal or repeat domains of the protein.