Comparison of affinity chromatography and adsorption to vaccinia virus recombinant infected cells for depletion of antibodies directed against respiratory syncytial virus glycoproteins present in a human immunoglobulin preparation.

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.