TLR4 and infection: Mapping the active domain within tenascin-C revealed a unique structural epitope in the fibrinogen-like globe (FBG) that is essential for binding to and activating TLR4.8 10 Distinct modes of receptor activation and diverse downstream signalling induced by FBG compared with pathogenic TLR4 agonists,11 revealed an opportunity to ablate pathological ‘sterile’ inflammation, leaving intact host defence against infection.