Swanson A F, Kuo C C
Department of Pathobiology, University of Washington, Seattle 98195.
Infect Immun. 1990 Feb;58(2):502-7. doi: 10.1128/iai.58.2.502-507.1990.
Lectin-binding proteins of chlamydiae were detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting. All three Chlamydia species tested expressed two proteins when whole-elementary-body lysates were reacted with the biotinylated lectin Dolichos biflorus agglutinin. The protein with a molecular mass of 18 kilodaltons (kDa) responded strongly compared with a higher-molecular-mass protein that varied from 27 to 32 kDa with each chlamydia strain tested. Among six lectins tested, including concanavalin A, D. biflorus agglutinin, Ulex europaeus agglutinin, soybean agglutinin, peanut agglutinin, and wheat germ agglutinin, the latter was the only lectin that did not recognize any chlamydial protein. For each lectin that reacted against the elementary body of serovar L2 of Chlamydia trachomatis, the same two peptides, an 18-kDa peptide and a 32-kDa peptide, were revealed. These two polypeptides adhered to HeLa cell surface components. Binding of a lectin to the L2 reticulate body resulted in a reduced response at the 18-kDa peptide. The 18- and 32-kDa peptides were purified from L2 serovar elementary bodies by affinity chromatography. The two proteins isolated from a concanavalin A-agarose column maintained their lectin-binding capacities and elicited hemagglutinating properties against mouse erythrocytes. Periodate oxidation abolished the abilities of the peptides to adhere to any of the lectins tested. These results suggest that these lectin-binding proteins are glycoproteins that may be an essential factor for attachment of chlamydial organisms to host cells.
通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳和免疫印迹法检测衣原体的凝集素结合蛋白。当全原体裂解物与生物素化凝集素双花扁豆凝集素反应时，所有测试的三种衣原体物种均表达两种蛋白质。与分子量在27至32 kDa之间变化的高分子量蛋白质相比，分子量为18千道尔顿（kDa）的蛋白质反应强烈，每种测试的衣原体菌株均如此。在测试的六种凝集素中，包括伴刀豆球蛋白A、双花扁豆凝集素、欧洲荆豆凝集素、大豆凝集素、花生凝集素和麦胚凝集素，后者是唯一不识别任何衣原体蛋白的凝集素。对于每种与沙眼衣原体血清型L2原体反应的凝集素，均显示出相同的两种肽，即18 kDa肽和32 kDa肽。这两种多肽粘附于HeLa细胞表面成分。凝集素与L2网状体的结合导致18 kDa肽处的反应减弱。通过亲和色谱法从L2血清型原体中纯化出18 kDa和32 kDa的肽。从伴刀豆球蛋白A-琼脂糖柱分离出的两种蛋白质保持了它们的凝集素结合能力，并引发了针对小鼠红细胞的血凝特性。高碘酸盐氧化消除了这些肽粘附于任何测试凝集素的能力。这些结果表明，这些凝集素结合蛋白是糖蛋白，可能是衣原体生物体附着于宿主细胞的关键因素。
