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Serine-aspartate repeat-containing protein D (SdrD) is a cell wall-anchored surface protein of Staphylococcus aureus and a member of the Microbial Surface Components Recognizing Adhesive Matrix Molecules (MSCRAMM) family. It plays a pivotal role in the initial stages of infection by mediating bacterial adhesion to host tissues, specifically binding to desmoglein 1 (DSG1) on human skin and nasal epithelial cells in a calcium-dependent manner. Beyond its adhesive properties, SdrD is a significant virulence factor that contributes to immune evasion by promoting resistance to neutrophil-mediated killing and enhancing bacterial survival within the bloodstream. The protein is implicated in a variety of staphylococcal diseases, including atopic dermatitis, sepsis, and bone infections, and its expression is often upregulated during systemic infection. Due to its critical role in colonization and pathogenesis, SdrD is considered a promising target for the development of novel anti-virulence therapies and multi-component vaccines aimed at preventing invasive S. aureus infections.
SdrD facilitates bacterial adhesion to host ligands, such as desmoglein 1 (DSG1), through a calcium-dependent mechanism. It also promotes immune evasion by inhibiting neutrophil-mediated killing and enhancing bacterial survival in the bloodstream.
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