Monoclonal antibody against l-lectin module of SraP blocks adhesion and protects mice against Staphylococcus aureus...

SraP is a serine-rich repeat protein (SRRP) from Staphylococcus aureus that binds to sialylated receptors to promote bacterial adhesion to and invasion into host epithelial cells, mediated by the l-lectin module of its ligand-binding region.

The sequence encoding the L-lectin module of SraP was inserted into pET28a plasmid, and the recombinant protein was purified by His label affinity chromatography. A monoclonal antibody (mAb) against the l-lectin module was obtained and confirmed by enzyme-linked immunosorbent assay and western blotting. The effect of the mAb on S. aureus adhesion and invasion was assessed in A₅₄₉ cells and mice subjected to S. aureus challenge.

We successfully obtained a mAb against the l-lectin module of SraP. Pre-incubation with the mAb dramatically inhibited the bacteria's ability to adhere to and invade A₅₄₉ cells. Moreover, mice administered mAb through tail vein injection had significantly fewer bacteria in the blood.

The anti-SraP_L-Lectin mAb significantly reduced the adherence and invasion of S. aureus to host cells. This study lays the foundation for the future development of the l-lectin module of SraP as a target for the prevention and treatment of S. aureus infection. Our findings suggest that specific subdomains of SRRPs may represent potential antibacterial drug targets for intervention.