Caldwell H D, Perry L J
Infect Immun. 1982 Nov;38(2):745-54. doi: 10.1128/iai.38.2.745-754.1982.
Rabbit immunoglobulin G (IgG) antibodies raised against the major outer membrane protein of the Chlamydia trachomatis lymphogranuloma venereum strain 434 neutralized the infectivity of the parasite for HeLa 229 cells. The mechanism by which anti-major outer membrane protein IgG prevented C. trachomatis from establishing infection was studied by using intrinsically 14C-radiolabeled elementary bodies. Neutralized elementary bodies were filterable through a polycarbonate filter (pore diameter, 600 nm), demonstrating that reduction in infectivity was not due to the aggregation of elementary bodies by cross-linking IgG. Antibody-neutralized elementary bodies attached to and penetrated HeLa cells at rats nearly identical to those for infectious organisms exposed to nonneutralizing control IgG. These results suggest that antibody interferes with the infectious process of the parasite after its internalization. Anti-major outer membrane protein Fab fragments could not be substituted for neutralizing IgG antibodies. The requirement for intact IgG implies that cross-linking of antibodies to the major outer membrane protein on the surfaces of the organisms may be instrumental in neutralization.
针对沙眼衣原体淋巴肉芽肿性病株434主要外膜蛋白产生的兔免疫球蛋白G（IgG）抗体，可中和该病原体对HeLa 229细胞的感染性。利用内源性14C放射性标记的原体，研究了抗主要外膜蛋白IgG阻止沙眼衣原体建立感染的机制。经中和的原体可通过聚碳酸酯滤膜（孔径600nm）过滤，表明感染性降低并非由于交联IgG导致原体聚集所致。抗体中和的原体与暴露于非中和对照IgG的感染性生物体相比，附着并穿透HeLa细胞的效率几乎相同。这些结果表明，抗体在原体内化后干扰其感染过程。抗主要外膜蛋白Fab片段不能替代中和IgG抗体。完整IgG的必要性表明，抗体与生物体表面主要外膜蛋白的交联可能在中和过程中起作用。
