Interaction of Mycoplasma gallisepticum with sialyl glycoproteins.
The binding of several glycoproteins to freshly grown and harvested cells of Mycoplasma gallisepticum was examined. Only human glycophorin, the major sialoglycoprotein of the erythrocyte membrane, bound tightly as judged by direct binding assays with 125I-labeled glycoproteins. Neuraminidase-treated glycophorin did not bind, suggesting that binding is mediated through sialic acid groups. Although other sialoglycoproteins did not appear to bind M. gallisepticum by direct binding assays, some inhibited the binding of glycophorin. The best inhibitors had a mucin-like structure, with high molecular weights and high sialic acid contents. N-acetylneuraminic acid appeared to be the favored sialic acid structure for binding, but there was no strict specificity for its anomeric linkage. Neuraminidase activity could not be detected on the surface of M. gallisepticum, suggesting that this enzyme is not involved in the mechanism of adherence of sialoglycoproteins. Binding of sialoglycoproteins was time dependent, however, and markedly diminished with increasing ionic strength, but was largely unaffected between pH 4 and 9.
D001665:Binding Sites; D001667:Binding, Competitive; D006021:Glycophorins / Q000378:metabolism; D006388:Hemagglutinins / Q000032:analysis; D009174:Mycoplasma / Q000378:metabolism*; D009961:Orosomucoid / Q000378:metabolism; D012795:Sialoglycoproteins / Q000378:metabolism*; D013329:Structure-Activity Relationship; D000509:alpha-Fetoproteins / Q000378:metabolism
D006021:Glycophorins; D006388:Hemagglutinins; D009961:Orosomucoid; D012795:Sialoglycoproteins; D000509:alpha-Fetoproteins