Vibrio cholerae cytolysin (VCC) is a prominent member in the family of bacterial ß-barrel pore-forming proteins (ß-PFPs). VCC acts by forming transmembrane heptameric ß-barrel pores, thereby leading to the permeabilization of the target eukaryotic cell membranes. In spite of following the overall general scheme of the membrane pore-formation process of the bacterial ß-PFPs, structure-function mechanism of VCC highlights several unique features, functional implications of which still remain obscure. For example, VCC harbors two lectin-like domains that are not documented in the archetypical ß-PFPs. Also, membrane-interaction mechanism of VCC appears to involve a complex cross-talk between the protein and the membrane components, exact description of which remains unclear. Our ongoing research is focused toward understanding the mechanistic basis of the membrane pore-formation process of VCC, and its functional implications in the context of the host cellular responses and immunity. Toward exploring the membrane-interaction mechanism of VCC, we have shown that VCC employs a specific structural motif to recognize the phospholipid head-groups of the membrane lipid bilayer. In the absence of such recognition, membrane-bound form of VCC is unable to execute the functional pore-formation mechanism. Our study also reveals that the membrane-binding and pore-forming efficacy of VCC is critically regulated by the membrane cholesterol. VCC also exhibits a unique lectin-like activity that not only facilitates the efficient membrane-binding, but also regulates the oligomeric pore-formation mechanism. Through our studies, we have also elucidated the discrete steps of the membrane pore-formation process of VCC, which involve formation of the structurally distinct pre-pore intermediates. Finally, we have also explored the role of VCC in triggering the host cellular responses, particularly in the context of the host innate immune cells.