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.
Cottin
J
J
UFR Médecine-Pharmacie, Laboratoire de Bactériologie, Angers, France.
Robert
R
R
Leynia de la Jarrige
P
P
Loiseau
O
O
Mahaza
C
C
Carbonnelle
B
B
Senet
J M
JM
D000418:Albumins / Q000378:metabolism* / Q000493:pharmacokinetics; D004305:Dose-Response Relationship, Drug; D066298:In Vitro Techniques; D037102:Lectins / Q000378:metabolism*; D008089:Listeria monocytogenes / Q000378:metabolism*; D011485:Protein Binding / Q000502:physiology*; D013960:Thyroid Function Tests
D000418:Albumins; D037102:Lectins