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Staphylococcus epidermidis surface protein C (SesC) is a cell wall-anchored protein that functions as an adhesin, playing a pivotal role in the pathogenesis of Staphylococcus epidermidis infections (Shahrooei et al., 2009). It belongs to the Microbial Surface Components Recognizing Adhesive Matrix Molecules (MSCRAMM) family and is instrumental in the initial attachment of bacteria to medical devices and host tissues, as well as the subsequent development of biofilms (UniProt Q5HKP6). SesC is highly conserved and widely expressed among clinical isolates, making it a significant factor in chronic infections associated with indwelling medical devices like catheters and prosthetic joints (Shahrooei et al., 2012). As a surface-exposed protein, it is a primary target for the development of vaccines and therapeutic antibodies aimed at preventing biofilm-mediated infections. Research indicates that blocking SesC can impair the ability of the bacteria to colonize surfaces, thereby increasing their susceptibility to host immune responses and antibiotic treatments. Consequently, SesC represents a strategic target for addressing the growing challenge of antibiotic-resistant staphylococcal infections in healthcare settings.
Inhibition of bacterial adhesion and biofilm formation by blocking the interaction of SesC with host extracellular matrix components or abiotic surfaces.
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