In recent years, there has been much interest in harnessing the potential of bacterial glycolipids as vaccine adjuvants due to their ability to induce a strong Th-1 immune response. These molecules can be recognized by pattern recognition receptors (PRR) that are expressed by many cells of the immune system. Macrophage inducible C-type lectin (Mincle) is one such PRR that can recognize a wide range of molecules including both damage-associated and pathogen-associated molecular patterns.[1] Many studies have focussed on determining the scope of ligands that bind Mincle and how structural modifications to these ligands influence their immune response. In particular, trehalose glycolipids represent a potent class of promising Mincle agonists.[2] To this end, we sought to investigate how changes to the trehalose glycolipid structure influences Mincle agonistic activity, with a view that the findings could lead to the development of improved vaccine adjuvants.
- X. Lu, M. Nagata, S. Yamasaki. Mincle: 20 years of a versatile sensor of insults. Int. Immunol. 30, 6, 2018, 233–239.
- C. D. Braganza, T. Teunissen, M.S.M. Timmer, B.L. Stocker. Identification and Biological Activity of Synthetic Macrophage Inducible C-Type Lectin Ligands. Front. Immunol. 2018, 8, 1940.