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. 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. 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.
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