We are investigating the nature of the cell receptor for various bacterial adhesins. Experiments with thin layer chromatography (TLC) of glycolipid extracts indicate that virulent strains B. pertussis bind to certain glycolipids present in lung tissues. We are currently investigating the structure of the glycolipids involved in this adhesion. Using purified glycolipids separated on thin layer chromatography, we have demonstrated that the virulent strains of B. pertussis bind to sulfatides and to asialo GM1. Avirulent strains of this bacteria were found to also bind to asialo GM1 but not to sulfatides. We are also trying to identify which bacterial adhesins are interacting with the glycolipids. Since pertactin and FHA, bacterial adhesins, both contain the sequence Arginine-Glycine-Aspartic Acid (RGD), we are also investigating the role of integrin receptors in bacterial adherence to mammalian cells.
