Glycosylphosphatidylinositol (GPI) attachment to the protein C-terminus is one of the most common and important natural posttranslational modifications. Therefore, GPIs are ubiquitous in eukaryotic cells and play an important role in various biological and pathological processes. Some pore-forming bacterial toxins use GPI anchors on the host cell surface as their binding partners to help their formation of porous oligomers and then insertion of these oligomers into cell membrane, so as to break the cell membrane permeability barrier and cause cell death. To have an in-depth understanding of this process and identify the critical structural motifs of GPI anchors for toxin binding, a series of structurally homogeneous and well-defined GPI anchors and GPI derivatives were synthesized and evaluated for binding with bacterial toxins and for the influence on interactions between toxins and host cells. The resultant structure-activity relationship information is useful for the design of pore-forming bacterial toxin inhibitors as a new type of therapeutics against bacterial infections.

Investigation of pore-forming bacterial toxin-GPI interactions using synthetic GPIs

2019 Spring National Meeting

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