Sastre Patricia, Melero José A, García-Barreno Blanca, Palomo Concepción
Centro Nacional de Microbiología, Instituto de Salud Carlos III, Majadahonda, Madrid, Spain.
J Med Virol. 2005 Jun;76(2):248-55. doi: 10.1002/jmv.20349.
Antibodies directed against human respiratory syncytial virus (HRSV) glycoproteins were depleted from a commercial immunoglobulin preparation (RespiGam) by two different methods. The first method consisted of repeated adsorption of RespiGam to Sepharose beads with covalently bound soluble forms of the two major viral glycoproteins (F or G). The second method consisted of adsorption of immunoglobulins to live cells expressing F or G glycoproteins on their surfaces after infection with vaccinia virus recombinants. While the first method removed efficiently antibodies that reacted with F and/or G glycoproteins by ELISA, it was inefficient in the elimination of anti-HRSV neutralizing antibodies. In contrast, the second method removed efficiently anti-HRSV antibodies that both reacted by ELISA and neutralized virus infectivity. These results confirm that human neutralizing antibodies are directed exclusively against HRSV F and G glycoproteins, and, they raise the possibility that F and G glycoproteins inserted into cell membranes differ antigenically from their soluble forms linked covalently to Sepharose beads.
采用两种不同方法从一种商业免疫球蛋白制剂（RespiGam）中去除针对人类呼吸道合胞病毒（HRSV）糖蛋白的抗体。第一种方法是将RespiGam反复吸附到共价结合有两种主要病毒糖蛋白（F或G）可溶性形式的琼脂糖珠上。第二种方法是在痘苗病毒重组体感染后，将免疫球蛋白吸附到表面表达F或G糖蛋白的活细胞上。虽然第一种方法能有效去除通过酶联免疫吸附测定（ELISA）与F和/或G糖蛋白反应的抗体，但在消除抗HRSV中和抗体方面效率不高。相比之下，第二种方法能有效去除通过ELISA反应且中和病毒感染性的抗HRSV抗体。这些结果证实，人类中和抗体仅针对HRSV F和G糖蛋白，并且，它们增加了插入细胞膜的F和G糖蛋白在抗原性上与其共价连接到琼脂糖珠上的可溶性形式不同的可能性。
