Shibata K, Sawa Y, Inoue S, Noda M, Watanabe T
Department of Oral Bacteriology, Hokkaido University School of Dentistry, Japan.
FEMS Microbiol Lett. 1994 Nov 1;123(3):305-9. doi: 10.1111/j.1574-6968.1994.tb07239.x.
Mycoplasma salivarium cells bound the Fc fragment of human immunoglobulin G. The activity was remarkably enhanced by Mn2+, but not by Mg2+ and Ca2+; significantly inhibited by D-mannose; and reduced by pronase treatment of the cells. About 90% of the cells treated with pronase were not disrupted. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of proteins of the cells treated with pronase indicated that proteins with molecular masses of 88, 90 and 150 kDa (88 kp, 90 kp and 150 kp) were specifically digested. The results presented suggest that 88 kp, 90 kp and 150 kp, located in the outer surface of the cell membrane, are responsible for the activity of the M. salivarium cells and interact with a carbohydrate-containing moiety (D-mannose) of the Fc fragment in a Mn(2+)-dependent manner.
唾液支原体细胞结合人免疫球蛋白G的Fc片段。该活性在Mn2+存在时显著增强，而在Mg2+和Ca2+存在时无此现象；D-甘露糖可显著抑制该活性；用链霉蛋白酶处理细胞后活性降低。约90%经链霉蛋白酶处理的细胞未被破坏。对经链霉蛋白酶处理的细胞蛋白进行十二烷基硫酸钠-聚丙烯酰胺凝胶电泳表明，分子量为88、90和150 kDa（88 kp、90 kp和150 kp）的蛋白质被特异性消化。呈现的结果表明，位于细胞膜外表面的88 kp、90 kp和150 kp负责唾液支原体细胞的活性，并以Mn(2+)依赖的方式与Fc片段的含碳水化合物部分（D-甘露糖）相互作用。
