Many bacteria produce toxins that cause damage through the formation of pores in the host cell membrane. Some of these toxins, such as aerolysin, use glycosylphosphatidylinositols (GPIs) as their binding receptors to assist the pore formation on the host cell surface and the subsequent insertion of the resultant pores into the cell membrane. GPIs are a class of complex glycolipids that anchor surface proteins and glycoproteins onto the cell membrane in eukaryotic species. This review has summarized the reported evidences supporting the GPI-dependent pore-forming mechanism for aerolysin-type of toxins and analyzed the possibility of targeting this unique process for the design and development of novel GPI-based inhibitors for these pore-forming bacterial toxins.
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