(Pro-Gly-Pro)., (Pro-Pro-Gly)jo, and (Pro-OH-Pro-Gly)j0 were recognized by the receptor, whereas the peptides (Pro-Ala-Gly). and polyproline showed no inhibitory activity.The matrix proteins fibronectin and laminin may mediate the substrate adhesion of eucaryotic cells, and putative receptors present on the surfaces of cells are believed to recognize distinct sites in the adhesive proteins (35). Some eucaryotic cells (e.g., hepatocytes and chondrocytes) may also adhere to collagen substrate, and the presence of collagen-specific receptors has been implicated (18,22). The collagen receptor on hepatocytes appears to have broad specificity, since it binds to several different types of collagen as well as to isolated collagen a chains, collagen peptides, and synthetic collagen analogs (22).In the process of tissue adherence of pathogenic bacteria, structures at the host cell surface or in the extracellular matrix are recognized by specific receptors present on the bacterial cells. Previous studies have shown that bacteria may bind to fibronectin (7, 15, 23, 25, 26, 32), laminin (7, 16, 27, 29, 32), and collagen (3, 7, 12, 32) Chemicals. Type II collagen was purified from bovine nasal septum as described by Strawich and Nimmi (28). Native collagen types I and III were isolated with neutral salt from fetal bovine skin and purified by NaCl precipitation and DEAE chromatography (30). Type IV collagen was isolated from mouse tumor (31). Type V and VI collagens were purified from a pepsin digest of human placenta (1,20). The 1(I) and 2(I) chains both from calf and rat skin type I collagens were purified by carboxymethyl cellulose chromatography (21). The rat a chains were treated with cyanogen bromide, and the generated peptides (CB peptides) were purified as previously described (2, 6). The isolated peptides included CB2, CB5, CB6, CB7, and CB8 from the 1(I) chain and CB3, CB4, and CB5 from the a2 chain of rat type