Montaño R F, Romano E L
Instituto Venezolano de Investigaciones Cientificas (IVIC), Caracas.
Hum Antibodies Hybridomas. 1994;5(3-4):152-6.
The presence of the Gal alpha 1-3 Gal structure (Gal epitope) in the carbohydrate component of fifteen human monoclonal antibodies with specificity for the Rh blood group factor and produced by human-mouse heterohybridomas was evaluated. To do that, an antiglobulin-like agglutination test and an enzyme linked immunosorbent assay were performed using an affinity-purified anti-Gal antibody obtained from the serum of an AB blood group donor. Using the antiglobulin reaction, results were obtained showing that only five of the fifteen human monoclonal antibodies tested contained the structure at levels sufficient to allow agglutination. However, all fifteen monoclonals were positive using the more sensitive enzyme linked immunosorbent assay. By means of an indirect immunofluorescence assay the same anti-Gal antibody was used to test the presence of Gal epitopes on the surface of the producer heterohybridomas. Results were obtained indicating that twelve out of the fifteen hybridomas studied do express the Gal structure on its surface. The relevance of these findings is discussed in the context of therapeutic applications of human monoclonal antibodies.
对15种由人-鼠异源杂交瘤产生的、对Rh血型因子具有特异性的人单克隆抗体的碳水化合物成分中是否存在Galα1-3Gal结构（Gal表位）进行了评估。为此，使用从AB血型供体血清中获得的亲和纯化抗Gal抗体进行了抗球蛋白样凝集试验和酶联免疫吸附测定。利用抗球蛋白反应，结果显示，在测试的15种人单克隆抗体中，只有5种含有足以引起凝集的该结构。然而，使用更灵敏的酶联免疫吸附测定时，所有15种单克隆抗体均呈阳性。通过间接免疫荧光测定，使用相同的抗Gal抗体检测产生抗体的异源杂交瘤表面Gal表位的存在。结果表明，在所研究的15种杂交瘤中，有12种在其表面表达Gal结构。在人单克隆抗体的治疗应用背景下讨论了这些发现的相关性。
