Stapylococcal Superantigen-Like 5 (SSL5)

SSL5 has dual functions related to its potency to recognize glycoproteins (Sialyl-Lewis X) as discovered by Jovanka Bestebroer in 2007 and 2009. SSL5 binds to PSGL-1 and thereby interferes with the interaction with P-selectin resulting in decreased neutrophil rolling and extravasation. SSL5 targets several chemokine and anaphylatoxin receptors through their common glycosaminoglycan-binding site. This results in specific inhibition of ligand-induced cell activation including migration.





1) Staphylococcal superantigen-like 5 binds PSGL-1 and inhibits P-selectin-mediated neutrophil rolling.

2) Staphylococcal SSL5 inhibits leukocyte activation by chemokines and anaphylatoxins.9