Trehalose 6-behenate

Trehalose 6-behenate (TDB) exerts its effect through binding to the macrophage-inducible C-type lectin Mincle, a pathogen recognition receptor (PRR) that recognises pathogen-associated molecular patterns (PAMPs). The potential of Th1/Th17 skewing adjuvants in vaccine development provides a very real incentive for better definition of the structural motifs required for Mincle binding. Mincle is highly conserved between mice and humans, with 85 % protein similarity. In addition to being a receptor for TDMs, Trehalose 6-behenate (TDB), and the spliceosome-associated protein (SAP)130 (which activates Mincle at a binding site different to that involved in carbohydrate recognition), Mincle is also a receptor for Candida albicans, Malassezia, and Fonsecaea pedrosoi[1].

[1]. Stocker BL, et al. On one leg: trehalose monoesters activate macrophages in a Mincle-dependant manner. Chembiochem. 2014 Feb 10;15(3):382-8.