Binding of collagen to Staphylococcus aureus Cowan 1.
Collagen binds to a receptor protein present on the surfaces of Staphylococcus aureus cells. Binding of 125I-labeled type II collagen to its bacterial receptor is reversible, and Scatchard plot analysis indicates the presence of one class of receptor that occurs on an average of 3 X 10(4) copies per cell and binds type II collagen with a Kd of 10(-7) M. Studies on the specificity of collagen cell binding indicate that the receptor does not recognize noncollagenous proteins but binds all of the different collagen types tested (types I to VI). Furthermore, isolated collagen alpha chains and peptides generated by cyanogen bromide cleavage of type I collagen alpha chains are recognized by the receptor as indicated by the ability of these polypeptides to inhibit binding of 125I-labeled type II collagen to staphylococcal cells. Synthetic collagen analogs were tested as inhibitors of type II collagen binding to bacterial cells. The peptides (Pro-Gly-Pro)n, (Pro-Pro-Gly)10, and (Pro-OH-Pro-Gly)10 were recognized by the receptor, whereas the peptides (Pro-Ala-Gly)n and polyproline showed no inhibitory activity.
D003094:Collagen / Q000031:analogs & derivatives / Q000378:metabolism*; D003488:Cyanogen Bromide; D010455:Peptides / Q000378:metabolism / Q000494:pharmacology; D038981:Receptors, Collagen; D011971:Receptors, Immunologic / Q000032:analysis / Q000378:metabolism*; D013211:Staphylococcus aureus / Q000378:metabolism*
D010455:Peptides; D038981:Receptors, Collagen; D011971:Receptors, Immunologic; D003094:Collagen; D003488:Cyanogen Bromide