It is increasingly clear that membrane-bound cholesterol plays an important regulatory role in pathogenic processes.  For example, cholesterol has been shown to modulate glycolipid conformations, which can either inhibit or facilitate recognition processes involving raft-associated proteins.  There is also recent evidence that cholesterol may directly mask glycosphingolipids such as monosialotetrahexosylganglioside (GM1) and thereby protect the carbohydrate from recognition by toxin-derived proteins including cholera toxin.  When one considers these findings in the context of the discovery that many pathogenic bacteria produce enzymes that require extrusion of cholesterol from host cells, an intriguing interplay of cholesterol transport between host and pathogen emerges.  Recent advances in our laboratory have led to efficient syntheses of host- and pathogen-associated glycolipids to enable studies focused on glycolipidomic profiling and the influence of cholesterol in pathogenic processes.

Recent advances in glycolipidomic profiling of pathogenic processes

244th National Meeting (2012)

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