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Staphylococcus aureus cell-surface receptors, primarily comprising the Microbial Surface Components Recognizing Adhesive Matrix Molecules (MSCRAMMs) and other cell wall-anchored (CWA) proteins, are critical virulence factors that mediate the bacterium's interaction with the host [3, 4]. These proteins, such as Clumping factor A (ClfA), Fibronectin-binding proteins (FnBPs), and Protein A (Spa), are covalently attached to the peptidoglycan layer by the enzyme sortase A [3, 8]. They play essential roles in the initial stages of infection by facilitating adhesion to host extracellular matrix components (e.g., fibrinogen, fibronectin, collagen) and promoting the formation of biofilms, which protect the bacteria from antibiotics and the immune system [6, 14]. Additionally, these receptors contribute to immune evasion by binding to the Fc region of antibodies (Protein A) or interfering with the complement system [11]. Given their surface exposure and vital roles in pathogenesis, they are prime targets for the development of vaccines and monoclonal antibodies, such as Tefibazumab, which aims to neutralize their function and enhance bacterial clearance [10, 11]. However, the therapeutic targeting of these receptors is complicated by their high degree of redundancy and the significant genetic diversity across different S. aureus strains [11, 13].
Inhibition of bacterial adhesion to host extracellular matrix components, prevention of biofilm development, and neutralization of immune evasion mechanisms to facilitate opsonophagocytosis and bacterial clearance [3, 8, 11].
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