Webster P, Russo D C, Black S J
International Laboratory for Research on Animal Diseases, Nairobi, Kenya.
J Cell Sci. 1990 Jun;96 ( Pt 2):249-55. doi: 10.1242/jcs.96.2.249.
Binding to Trypanosoma brucei of polyvalent IgMs and IgGs, monoclonal IgGs and Fab1 fragments of monoclonal IgGs specific for exposed epitopes of T. brucei variant surface glycoproteins (VSGs) was monitored by both immunofluorescence and immunocytochemistry. All antibodies and antibody fragments, were uniformly distributed over the parasite surface after incubation with the organism at 0 degrees C. Upon warming to 37 degrees C bound antibodies and fragments were detected in the flagellar pocket and intracellular organelles. Removal of single layers of bound antibody, or Fab1 fragments, from the cell surface at 37 degrees C, as determined by immunofluorescence, was complete within 20 min and occurred in the presence or absence of protein synthesis. Parasites that had shown an altered distribution of surface-bound antibody after warming remained fully covered with VSGs of the original antigen type as shown by immunocytochemistry.
通过免疫荧光和免疫细胞化学监测了多价IgM和IgG、单克隆IgG以及针对布氏锥虫可变表面糖蛋白（VSG）暴露表位的单克隆IgG的Fab1片段与布氏锥虫的结合情况。在0摄氏度下与该生物体孵育后，所有抗体和抗体片段均均匀分布在寄生虫表面。升温至37摄氏度后，在鞭毛袋和细胞内细胞器中检测到结合的抗体和片段。通过免疫荧光测定，在37摄氏度下从细胞表面去除单层结合抗体或Fab1片段在20分钟内完成，且无论有无蛋白质合成均会发生。如免疫细胞化学所示，升温后表面结合抗体分布发生改变的寄生虫仍完全被原始抗原类型的VSG覆盖。
