Specific interaction between Listeria monocytogenes and glycosylated albumins.

We have previously shown that Listeria monocytogenes serovar 1/2b can bind strongly to bovine albumin (BA) glycosylated by glucosamine or fucosylamine with about 20 to 30 carbohydrate residues per albumin molecule. We now show that the binding is time-dependent, reversible, saturable and specific. The two glycosylated compounds inhibit each other competitively. Scatchard analysis showed that about 100 molecules of BA-glucosamide (heptameric configuration) and 14,300 molecules of BA-fucosylamide (monomeric configuration) bound per bacterial cell. The apparent dissociation constants for BA-glucosamide and BA-fucosylamide were found to be 3.9 x 10(-14) M and 3.5 x 10(-13) M, respectively.