We have described how lipid membranes affect formation of transmembrane pores in lipid membranes. We published this in an excellent journal from the field of chemistry. We have described, also based on some of our published results, that lipid membranes affect binding of proteins to lipid membranes, their oligomerization and insertion in the membranes in order to form transnembrane pores.
We have shown tha listeriolysin O form pores at different pH values. This is physiologically important. We have also shown that pH affects the pore formation. In addition pores can fuse to larger oligomeric complexes.
We have succeeded in expressing and purifying murine perforin. Murine perforin has similar functional properties as the native human perforin. It also forms pores on the surface of liposomes. We will use this protocol for the preparation of perforin mutants that will be instrumental in understanding of perforin mechanism of pore formation.
We have shown that listeriolysin O dsirupts the integrity of Caco-2 cellular monolayer in pore dependent, but calcium ions independent manner.
We have published a review paper in esteemed biochemical journal. We have described an important group of enzymes, metallophosphoesterases, that are abundatnly present in mycobacteria and can thus be a good target for development of novel drugs.